atrial natriuretic peptide-converting enzyme isoform 2 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
698-929 | 3.90e-85 | ||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. : Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 272.61 E-value: 3.90e-85
|
||||||||
| CRD_corin_2 | cd07888 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
350-471 | 1.47e-83 | ||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD. : Pssm-ID: 143579 [Multi-domain] Cd Length: 122 Bit Score: 264.18 E-value: 1.47e-83
|
||||||||
| CRD_corin_1 | cd07445 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
69-196 | 1.08e-74 | ||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD. : Pssm-ID: 143554 Cd Length: 130 Bit Score: 240.61 E-value: 1.08e-74
|
||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
476-510 | 1.65e-08 | ||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 51.05 E-value: 1.65e-08
|
||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
239-273 | 2.04e-08 | ||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 50.67 E-value: 2.04e-08
|
||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
283-310 | 2.82e-08 | ||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 50.28 E-value: 2.82e-08
|
||||||||
| SR | smart00202 | Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ... |
586-682 | 7.73e-08 | ||||
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO. : Pssm-ID: 214555 [Multi-domain] Cd Length: 101 Bit Score: 51.19 E-value: 7.73e-08
|
||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
551-585 | 1.25e-07 | ||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 48.36 E-value: 1.25e-07
|
||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
202-237 | 2.08e-07 | ||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure : Pssm-ID: 238060 Cd Length: 35 Bit Score: 47.97 E-value: 2.08e-07
|
||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
698-929 | 3.90e-85 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 272.61 E-value: 3.90e-85
|
|||||||||
| CRD_corin_2 | cd07888 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
350-471 | 1.47e-83 | |||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD. Pssm-ID: 143579 [Multi-domain] Cd Length: 122 Bit Score: 264.18 E-value: 1.47e-83
|
|||||||||
| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
697-926 | 3.58e-82 | |||||
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. Pssm-ID: 214473 Cd Length: 229 Bit Score: 264.54 E-value: 3.58e-82
|
|||||||||
| CRD_corin_1 | cd07445 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
69-196 | 1.08e-74 | |||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD. Pssm-ID: 143554 Cd Length: 130 Bit Score: 240.61 E-value: 1.08e-74
|
|||||||||
| Trypsin | pfam00089 | Trypsin; |
698-926 | 1.07e-62 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 211.53 E-value: 1.07e-62
|
|||||||||
| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
690-930 | 5.10e-62 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 211.05 E-value: 5.10e-62
|
|||||||||
| Fz | pfam01392 | Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ... |
351-458 | 1.01e-30 | |||||
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines. Pssm-ID: 460190 Cd Length: 116 Bit Score: 116.90 E-value: 1.01e-30
|
|||||||||
| FRI | smart00063 | Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ... |
351-460 | 3.12e-26 | |||||
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)]. Pssm-ID: 214498 Cd Length: 113 Bit Score: 103.93 E-value: 3.12e-26
|
|||||||||
| Fz | pfam01392 | Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ... |
72-179 | 1.38e-22 | |||||
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines. Pssm-ID: 460190 Cd Length: 116 Bit Score: 93.79 E-value: 1.38e-22
|
|||||||||
| FRI | smart00063 | Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ... |
72-176 | 3.95e-15 | |||||
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)]. Pssm-ID: 214498 Cd Length: 113 Bit Score: 72.34 E-value: 3.95e-15
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
476-510 | 1.65e-08 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 51.05 E-value: 1.65e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
239-273 | 2.04e-08 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 50.67 E-value: 2.04e-08
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
476-510 | 2.21e-08 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 50.71 E-value: 2.21e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
283-310 | 2.82e-08 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 50.28 E-value: 2.82e-08
|
|||||||||
| SR | smart00202 | Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ... |
586-682 | 7.73e-08 | |||||
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO. Pssm-ID: 214555 [Multi-domain] Cd Length: 101 Bit Score: 51.19 E-value: 7.73e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
551-585 | 1.25e-07 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 48.36 E-value: 1.25e-07
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
283-310 | 1.51e-07 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 48.40 E-value: 1.51e-07
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
202-237 | 2.08e-07 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 47.97 E-value: 2.08e-07
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
202-237 | 3.02e-07 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 47.24 E-value: 3.02e-07
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
239-273 | 3.57e-07 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 47.24 E-value: 3.57e-07
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
239-270 | 9.80e-07 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 45.70 E-value: 9.80e-07
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
475-507 | 1.12e-06 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 45.70 E-value: 1.12e-06
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
283-307 | 1.16e-06 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 45.70 E-value: 1.16e-06
|
|||||||||
| SRCR_2 | pfam15494 | Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ... |
609-690 | 4.89e-06 | |||||
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin. Pssm-ID: 464747 Cd Length: 99 Bit Score: 45.78 E-value: 4.89e-06
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
202-234 | 1.86e-05 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 42.24 E-value: 1.86e-05
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
551-582 | 2.28e-05 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 41.85 E-value: 2.28e-05
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
551-585 | 9.48e-05 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 40.31 E-value: 9.48e-05
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
698-929 | 3.90e-85 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 272.61 E-value: 3.90e-85
|
|||||||||
| CRD_corin_2 | cd07888 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
350-471 | 1.47e-83 | |||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD. Pssm-ID: 143579 [Multi-domain] Cd Length: 122 Bit Score: 264.18 E-value: 1.47e-83
|
|||||||||
| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
697-926 | 3.58e-82 | |||||
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. Pssm-ID: 214473 Cd Length: 229 Bit Score: 264.54 E-value: 3.58e-82
|
|||||||||
| CRD_corin_1 | cd07445 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
69-196 | 1.08e-74 | |||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD. Pssm-ID: 143554 Cd Length: 130 Bit Score: 240.61 E-value: 1.08e-74
|
|||||||||
| Trypsin | pfam00089 | Trypsin; |
698-926 | 1.07e-62 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 211.53 E-value: 1.07e-62
|
|||||||||
| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
690-930 | 5.10e-62 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 211.05 E-value: 5.10e-62
|
|||||||||
| CRD_FZ | cd07066 | CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ... |
350-471 | 7.99e-34 | |||||
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143549 Cd Length: 119 Bit Score: 126.08 E-value: 7.99e-34
|
|||||||||
| CRD_FZ4 | cd07448 | Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ... |
350-467 | 5.06e-31 | |||||
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 4 (Fz4) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and the Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 4 (Fz4) activates the Ca(2+)/calmodulin-dependent protein kinase II and protein kinase C of the Wnt/Ca(2+) signaling pathway during retinal angiogenesis. Mutations in Fz4 lead to familial exudative vitreoretinopathy (FEVR), a hereditary ocular disorder characterized by failure of the peripheral retinal vascularization. In addition, the interplay between Fz4 and norrin as a receptor-ligand pair plays an important role in vascular development in the retina and inner ear in a Wnt-independent manner. Pssm-ID: 143557 Cd Length: 126 Bit Score: 118.33 E-value: 5.06e-31
|
|||||||||
| Fz | pfam01392 | Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ... |
351-458 | 1.01e-30 | |||||
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines. Pssm-ID: 460190 Cd Length: 116 Bit Score: 116.90 E-value: 1.01e-30
|
|||||||||
| CRD_FZ1_like | cd07458 | Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ... |
349-463 | 1.81e-29 | |||||
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1), frizzled 2 (Fz2), and frizzled 7 (Fz7) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143567 Cd Length: 119 Bit Score: 113.28 E-value: 1.81e-29
|
|||||||||
| FRI | smart00063 | Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ... |
351-460 | 3.12e-26 | |||||
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)]. Pssm-ID: 214498 Cd Length: 113 Bit Score: 103.93 E-value: 3.12e-26
|
|||||||||
| CRD_FZ | cd07066 | CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ... |
72-194 | 1.76e-25 | |||||
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143549 Cd Length: 119 Bit Score: 102.20 E-value: 1.76e-25
|
|||||||||
| CRD_FZ9_like | cd07457 | Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ... |
349-467 | 3.10e-25 | |||||
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) and frizzled 10 (Fz10) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143566 Cd Length: 121 Bit Score: 101.42 E-value: 3.10e-25
|
|||||||||
| CRD_FZ5_like | cd07456 | Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ... |
351-471 | 4.47e-25 | |||||
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) and frizzled 8 (Fz8) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143565 Cd Length: 120 Bit Score: 100.94 E-value: 4.47e-25
|
|||||||||
| CRD_FZ10 | cd07462 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ... |
350-467 | 2.27e-24 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 10 (Fz10) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. The cellular functon of Fz10 is unknown. Pssm-ID: 143571 Cd Length: 127 Bit Score: 99.32 E-value: 2.27e-24
|
|||||||||
| CRD_FZ9 | cd07463 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ... |
349-471 | 2.57e-24 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz9 may play a signaling role in lymphoid development and maturation, particularly at points where B cells undergo self-renewal prior to further differentiation. Pssm-ID: 143572 Cd Length: 127 Bit Score: 98.94 E-value: 2.57e-24
|
|||||||||
| Fz | pfam01392 | Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ... |
72-179 | 1.38e-22 | |||||
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines. Pssm-ID: 460190 Cd Length: 116 Bit Score: 93.79 E-value: 1.38e-22
|
|||||||||
| CRD_FZ3 | cd07449 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ... |
351-458 | 1.73e-22 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 3 (Fz3) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz3 plays a vital role in the anterior-posterior guidance of commissural axons. Knockout mice without Fz3 show defects in fiber tracts in the rostral CNS. Pssm-ID: 143558 [Multi-domain] Cd Length: 127 Bit Score: 93.92 E-value: 1.73e-22
|
|||||||||
| CRD_FZ2 | cd07464 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ... |
351-467 | 6.08e-22 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 2 (Fz2) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz2 is involved in the Wnt/beta-catenin signaling pathway and in the activation of protein kinase C and calcium/calmodulin-dependent protein kinase (CaM kinase). Pssm-ID: 143573 Cd Length: 127 Bit Score: 92.46 E-value: 6.08e-22
|
|||||||||
| CRD_FZ7 | cd07466 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ... |
351-457 | 1.39e-21 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 7 (Fz7) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz7 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula. Pssm-ID: 143575 [Multi-domain] Cd Length: 125 Bit Score: 91.30 E-value: 1.39e-21
|
|||||||||
| CRD_FZ8 | cd07461 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ... |
350-467 | 1.87e-21 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 8 (Fz8) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz8 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula. Pssm-ID: 143570 Cd Length: 125 Bit Score: 90.81 E-value: 1.87e-21
|
|||||||||
| CRD_FZ5 | cd07460 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ... |
351-467 | 5.28e-21 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz5 plays critical regulating roles in the yolk sac and placental angiogenesis, in the maturation of the Paneth cell phenotype, in governing the neural potential of progenitors in the developing retina, and in neuronal survival in the parafascicular nucleus. Pssm-ID: 143569 [Multi-domain] Cd Length: 127 Bit Score: 89.69 E-value: 5.28e-21
|
|||||||||
| CRD_SFRP3 | cd07441 | Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ... |
348-473 | 7.12e-21 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), which plays important roles in embryogenesis and postnatal development as an antagonist of Wnt proteins, key players in a number of fundamental cellular processes. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled proteins (Fz), thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP3 regulates Wnt signaling activity in bone development and homeostasis. It is also involved in the control of planar cell polarity. Pssm-ID: 143550 Cd Length: 126 Bit Score: 89.34 E-value: 7.12e-21
|
|||||||||
| CRD_FZ1 | cd07465 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ... |
351-457 | 9.22e-21 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Pssm-ID: 143574 Cd Length: 127 Bit Score: 88.96 E-value: 9.22e-21
|
|||||||||
| CRD_SFRP2 | cd07446 | Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ... |
349-469 | 5.05e-18 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt activity; The cysteine-rich-domain (CRD) is an essential part of the secreted frizzled related protein 2 (SFRP2), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. As a Wnt antagonist, SFRP2 regulates Nkx2.2 expression in the ventral spinal cord and anteroposterior axis elongation. SFRP2 also has a Wnt-independent function as an enhancer of procollagen cleavage by the TLD proteinases. SFRP2 binds both procollagen and TLD, thus facilitating the enzymatic reaction by bringing together the proteinase and its substrate. Pssm-ID: 143555 Cd Length: 128 Bit Score: 81.11 E-value: 5.05e-18
|
|||||||||
| CRD_LIN_17 | cd07454 | Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ... |
350-473 | 1.49e-17 | |||||
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. The protein lin-17 is involved in cell type specification during Caenorhabditis elegans vulval development. Pssm-ID: 143563 Cd Length: 124 Bit Score: 79.83 E-value: 1.49e-17
|
|||||||||
| CRD_SFRP4 | cd07442 | Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ... |
351-475 | 1.96e-17 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. Pssm-ID: 143551 Cd Length: 127 Bit Score: 79.30 E-value: 1.96e-17
|
|||||||||
| CRD_corin_1 | cd07445 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
347-465 | 6.94e-16 | |||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD. Pssm-ID: 143554 Cd Length: 130 Bit Score: 74.97 E-value: 6.94e-16
|
|||||||||
| CRD_corin_2 | cd07888 | One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ... |
72-194 | 1.46e-15 | |||||
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD. Pssm-ID: 143579 [Multi-domain] Cd Length: 122 Bit Score: 73.90 E-value: 1.46e-15
|
|||||||||
| FRI | smart00063 | Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ... |
72-176 | 3.95e-15 | |||||
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)]. Pssm-ID: 214498 Cd Length: 113 Bit Score: 72.34 E-value: 3.95e-15
|
|||||||||
| CRD_FZ6 | cd07450 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ... |
351-457 | 9.21e-15 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 6 (Fz6) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 6 (Fz6) is expressed in the skin and hair follicles and controls hair patterning in mammals using a Fz-dependent tissue polarity system, which is similar to the one that patterns the Drosophila cuticle. Pssm-ID: 143559 [Multi-domain] Cd Length: 127 Bit Score: 71.72 E-value: 9.21e-15
|
|||||||||
| CRD_sizzled | cd07452 | Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ... |
349-469 | 3.21e-13 | |||||
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential part of the sizzled protein, which regulates bone morphogenetic protein (Bmp) signaling by stabilizing chordin, and plays a critical role in the patterning of vertebrate and invertebrate embryos. Sizzled also functions in the ventral region as a Wnt inhibitor and modulates canonical Wnt signaling. Sizzled proteins belong to the secreted frizzled-related protein family (SFRP), and have be identified in the genomes of birds, fishes and frogs, but not mammals. Pssm-ID: 143561 Cd Length: 141 Bit Score: 67.60 E-value: 3.21e-13
|
|||||||||
| CRD_Carboxypeptidase_Z | cd07447 | Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ... |
350-456 | 3.41e-13 | |||||
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The cysteine-rich-domain (CRD) is an essential part of carboxypeptidase Z, a member of the carboxypeptidase E family of metallocarboxypeptidases. This is a group of Zn-dependent enzymes implicated in the intra- and extracellular processing of proteins. Carboxypeptidase Z removes C-terminal basic amino acid residues from its substrates, particularly arginine. The CRD acts as a ligand-binding domain for Wnts involved in developmental processes. CPZ binds and may process Wnt-4, CPZ has also been found to enhance the induction of the homeobox gene Cdx1. During vertebrate embryogenesis, the CRD of CPZ upregulates Pax3, a Wnt reporter gene essential for patterning of somites and limb development. Pssm-ID: 143556 Cd Length: 128 Bit Score: 67.09 E-value: 3.41e-13
|
|||||||||
| CRD_SFRP1 | cd07443 | Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ... |
353-459 | 4.26e-13 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 1 (SFRP1), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP1 is expressed in many tissues and is involved in the regulation of Wnt signaling in osteoblasts, leading to enhanced trabecular bone formation in adults; it has also been shown to control the growth of retinal ganglion cell axons and the elongation of the antero-posterior axis. Pssm-ID: 143552 Cd Length: 124 Bit Score: 66.85 E-value: 4.26e-13
|
|||||||||
| CRD_FZ4 | cd07448 | Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ... |
72-198 | 7.62e-12 | |||||
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 4 (Fz4) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and the Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 4 (Fz4) activates the Ca(2+)/calmodulin-dependent protein kinase II and protein kinase C of the Wnt/Ca(2+) signaling pathway during retinal angiogenesis. Mutations in Fz4 lead to familial exudative vitreoretinopathy (FEVR), a hereditary ocular disorder characterized by failure of the peripheral retinal vascularization. In addition, the interplay between Fz4 and norrin as a receptor-ligand pair plays an important role in vascular development in the retina and inner ear in a Wnt-independent manner. Pssm-ID: 143557 Cd Length: 126 Bit Score: 63.25 E-value: 7.62e-12
|
|||||||||
| CRD_SFRP5 | cd07444 | Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ... |
349-467 | 1.17e-11 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. Pssm-ID: 143553 Cd Length: 127 Bit Score: 63.04 E-value: 1.17e-11
|
|||||||||
| CRD_FZ1_like | cd07458 | Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ... |
70-176 | 3.37e-11 | |||||
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1), frizzled 2 (Fz2), and frizzled 7 (Fz7) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143567 Cd Length: 119 Bit Score: 61.27 E-value: 3.37e-11
|
|||||||||
| CRD_crescent | cd07453 | Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ... |
353-485 | 3.98e-11 | |||||
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential part of the crescent protein, a member of the secreted frizzled-related protein (SFRP) family, which regulates convergent extension movements (CEMs) during gastrulation and neurulation. Xenopus laevis crescent efficiently forms inhibitory complexes with Wnt5a and Wnt11, but this effect is cancelled in the presence of another member of the SFRP family, Frzb1. A potential role for Crescent in head formation is to regulate a non-canonical Wnt pathway positively in the adjacent posterior mesoderm, and negatively in the overlying anterior neuroectoderm. Pssm-ID: 143562 [Multi-domain] Cd Length: 135 Bit Score: 61.50 E-value: 3.98e-11
|
|||||||||
| CRD_FZ3 | cd07449 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ... |
71-182 | 4.17e-11 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 3 (Fz3) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz3 plays a vital role in the anterior-posterior guidance of commissural axons. Knockout mice without Fz3 show defects in fiber tracts in the rostral CNS. Pssm-ID: 143558 [Multi-domain] Cd Length: 127 Bit Score: 61.18 E-value: 4.17e-11
|
|||||||||
| CRD_LIN_17 | cd07454 | Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ... |
70-198 | 4.07e-10 | |||||
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. The protein lin-17 is involved in cell type specification during Caenorhabditis elegans vulval development. Pssm-ID: 143563 Cd Length: 124 Bit Score: 58.25 E-value: 4.07e-10
|
|||||||||
| CRD_FZ2 | cd07464 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ... |
70-176 | 9.93e-10 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 2 (Fz2) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz2 is involved in the Wnt/beta-catenin signaling pathway and in the activation of protein kinase C and calcium/calmodulin-dependent protein kinase (CaM kinase). Pssm-ID: 143573 Cd Length: 127 Bit Score: 57.40 E-value: 9.93e-10
|
|||||||||
| CRD_FZ7 | cd07466 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ... |
70-176 | 1.14e-09 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 7 (Fz7) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz7 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula. Pssm-ID: 143575 [Multi-domain] Cd Length: 125 Bit Score: 57.02 E-value: 1.14e-09
|
|||||||||
| CRD_FZ1 | cd07465 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ... |
70-176 | 1.20e-09 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Pssm-ID: 143574 Cd Length: 127 Bit Score: 56.99 E-value: 1.20e-09
|
|||||||||
| CRD_FZ5_like | cd07456 | Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ... |
108-192 | 3.93e-09 | |||||
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) and frizzled 8 (Fz8) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143565 Cd Length: 120 Bit Score: 55.48 E-value: 3.93e-09
|
|||||||||
| eMpr | COG3591 | V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
713-904 | 1.22e-08 | |||||
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 55.84 E-value: 1.22e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
476-510 | 1.65e-08 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 51.05 E-value: 1.65e-08
|
|||||||||
| CRD_FZ10 | cd07462 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ... |
70-181 | 1.72e-08 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 10 (Fz10) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. The cellular functon of Fz10 is unknown. Pssm-ID: 143571 Cd Length: 127 Bit Score: 53.87 E-value: 1.72e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
239-273 | 2.04e-08 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 50.67 E-value: 2.04e-08
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
476-510 | 2.21e-08 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 50.71 E-value: 2.21e-08
|
|||||||||
| CRD_SFRP2 | cd07446 | Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ... |
116-176 | 2.59e-08 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt activity; The cysteine-rich-domain (CRD) is an essential part of the secreted frizzled related protein 2 (SFRP2), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. As a Wnt antagonist, SFRP2 regulates Nkx2.2 expression in the ventral spinal cord and anteroposterior axis elongation. SFRP2 also has a Wnt-independent function as an enhancer of procollagen cleavage by the TLD proteinases. SFRP2 binds both procollagen and TLD, thus facilitating the enzymatic reaction by bringing together the proteinase and its substrate. Pssm-ID: 143555 Cd Length: 128 Bit Score: 53.37 E-value: 2.59e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
283-310 | 2.82e-08 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 50.28 E-value: 2.82e-08
|
|||||||||
| CRD_SFRP3 | cd07441 | Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ... |
71-176 | 2.83e-08 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), which plays important roles in embryogenesis and postnatal development as an antagonist of Wnt proteins, key players in a number of fundamental cellular processes. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled proteins (Fz), thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP3 regulates Wnt signaling activity in bone development and homeostasis. It is also involved in the control of planar cell polarity. Pssm-ID: 143550 Cd Length: 126 Bit Score: 53.13 E-value: 2.83e-08
|
|||||||||
| CRD_FZ8 | cd07461 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ... |
71-179 | 3.84e-08 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 8 (Fz8) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz8 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula. Pssm-ID: 143570 Cd Length: 125 Bit Score: 52.68 E-value: 3.84e-08
|
|||||||||
| CRD_FZ9_like | cd07457 | Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ... |
70-185 | 4.96e-08 | |||||
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) and frizzled 10 (Fz10) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. Pssm-ID: 143566 Cd Length: 121 Bit Score: 52.11 E-value: 4.96e-08
|
|||||||||
| CRD_Collagen_XVIII | cd07455 | Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ... |
353-460 | 6.30e-08 | |||||
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling. Pssm-ID: 143564 Cd Length: 123 Bit Score: 52.13 E-value: 6.30e-08
|
|||||||||
| SR | smart00202 | Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ... |
586-682 | 7.73e-08 | |||||
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO. Pssm-ID: 214555 [Multi-domain] Cd Length: 101 Bit Score: 51.19 E-value: 7.73e-08
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
551-585 | 1.25e-07 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 48.36 E-value: 1.25e-07
|
|||||||||
| CRD_FZ9 | cd07463 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ... |
72-176 | 1.33e-07 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz9 may play a signaling role in lymphoid development and maturation, particularly at points where B cells undergo self-renewal prior to further differentiation. Pssm-ID: 143572 Cd Length: 127 Bit Score: 51.18 E-value: 1.33e-07
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
283-310 | 1.51e-07 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 48.40 E-value: 1.51e-07
|
|||||||||
| LDLa | cd00112 | Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ... |
202-237 | 2.08e-07 | |||||
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure Pssm-ID: 238060 Cd Length: 35 Bit Score: 47.97 E-value: 2.08e-07
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
202-237 | 3.02e-07 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 47.24 E-value: 3.02e-07
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
239-273 | 3.57e-07 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 47.24 E-value: 3.57e-07
|
|||||||||
| CRD_FZ6 | cd07450 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ... |
72-186 | 4.44e-07 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 6 (Fz6) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 6 (Fz6) is expressed in the skin and hair follicles and controls hair patterning in mammals using a Fz-dependent tissue polarity system, which is similar to the one that patterns the Drosophila cuticle. Pssm-ID: 143559 [Multi-domain] Cd Length: 127 Bit Score: 49.76 E-value: 4.44e-07
|
|||||||||
| CRD_SFRP1 | cd07443 | Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ... |
115-176 | 8.30e-07 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 1 (SFRP1), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP1 is expressed in many tissues and is involved in the regulation of Wnt signaling in osteoblasts, leading to enhanced trabecular bone formation in adults; it has also been shown to control the growth of retinal ganglion cell axons and the elongation of the antero-posterior axis. Pssm-ID: 143552 Cd Length: 124 Bit Score: 48.74 E-value: 8.30e-07
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
239-270 | 9.80e-07 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 45.70 E-value: 9.80e-07
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
475-507 | 1.12e-06 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 45.70 E-value: 1.12e-06
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
283-307 | 1.16e-06 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 45.70 E-value: 1.16e-06
|
|||||||||
| CRD_SFRP5 | cd07444 | Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ... |
116-176 | 1.23e-06 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. Pssm-ID: 143553 Cd Length: 127 Bit Score: 48.40 E-value: 1.23e-06
|
|||||||||
| CRD_FZ5 | cd07460 | Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ... |
72-176 | 1.62e-06 | |||||
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz5 plays critical regulating roles in the yolk sac and placental angiogenesis, in the maturation of the Paneth cell phenotype, in governing the neural potential of progenitors in the developing retina, and in neuronal survival in the parafascicular nucleus. Pssm-ID: 143569 [Multi-domain] Cd Length: 127 Bit Score: 48.09 E-value: 1.62e-06
|
|||||||||
| CRD_Carboxypeptidase_Z | cd07447 | Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ... |
72-176 | 3.13e-06 | |||||
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The cysteine-rich-domain (CRD) is an essential part of carboxypeptidase Z, a member of the carboxypeptidase E family of metallocarboxypeptidases. This is a group of Zn-dependent enzymes implicated in the intra- and extracellular processing of proteins. Carboxypeptidase Z removes C-terminal basic amino acid residues from its substrates, particularly arginine. The CRD acts as a ligand-binding domain for Wnts involved in developmental processes. CPZ binds and may process Wnt-4, CPZ has also been found to enhance the induction of the homeobox gene Cdx1. During vertebrate embryogenesis, the CRD of CPZ upregulates Pax3, a Wnt reporter gene essential for patterning of somites and limb development. Pssm-ID: 143556 Cd Length: 128 Bit Score: 47.44 E-value: 3.13e-06
|
|||||||||
| SRCR_2 | pfam15494 | Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ... |
609-690 | 4.89e-06 | |||||
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin. Pssm-ID: 464747 Cd Length: 99 Bit Score: 45.78 E-value: 4.89e-06
|
|||||||||
| CRD_SFRP4 | cd07442 | Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ... |
116-193 | 6.92e-06 | |||||
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. Pssm-ID: 143551 Cd Length: 127 Bit Score: 46.17 E-value: 6.92e-06
|
|||||||||
| CRD_sizzled | cd07452 | Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ... |
78-176 | 7.46e-06 | |||||
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential part of the sizzled protein, which regulates bone morphogenetic protein (Bmp) signaling by stabilizing chordin, and plays a critical role in the patterning of vertebrate and invertebrate embryos. Sizzled also functions in the ventral region as a Wnt inhibitor and modulates canonical Wnt signaling. Sizzled proteins belong to the secreted frizzled-related protein family (SFRP), and have be identified in the genomes of birds, fishes and frogs, but not mammals. Pssm-ID: 143561 Cd Length: 141 Bit Score: 46.41 E-value: 7.46e-06
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
202-234 | 1.86e-05 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 42.24 E-value: 1.86e-05
|
|||||||||
| CRD_crescent | cd07453 | Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ... |
116-196 | 1.92e-05 | |||||
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential part of the crescent protein, a member of the secreted frizzled-related protein (SFRP) family, which regulates convergent extension movements (CEMs) during gastrulation and neurulation. Xenopus laevis crescent efficiently forms inhibitory complexes with Wnt5a and Wnt11, but this effect is cancelled in the presence of another member of the SFRP family, Frzb1. A potential role for Crescent in head formation is to regulate a non-canonical Wnt pathway positively in the adjacent posterior mesoderm, and negatively in the overlying anterior neuroectoderm. Pssm-ID: 143562 [Multi-domain] Cd Length: 135 Bit Score: 45.32 E-value: 1.92e-05
|
|||||||||
| LDLa | smart00192 | Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ... |
551-582 | 2.28e-05 | |||||
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia. Pssm-ID: 197566 Cd Length: 33 Bit Score: 41.85 E-value: 2.28e-05
|
|||||||||
| Ldl_recept_a | pfam00057 | Low-density lipoprotein receptor domain class A; |
551-585 | 9.48e-05 | |||||
Low-density lipoprotein receptor domain class A; Pssm-ID: 395011 Cd Length: 37 Bit Score: 40.31 E-value: 9.48e-05
|
|||||||||
| CRD_SMO | cd07451 | Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ... |
83-173 | 1.97e-04 | |||||
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The cysteine-rich domain (CRD) is part of the smoothened receptor (Smo), an integral membrane protein and one of the key players in the Hedgehog (Hh) signaling pathway, critical for development, cell growth and migration, as well as stem cell maintenance. The CRD of Smo is conserved in vertebrates and can also be identified in invertebrates. The precise function of the CRD in Smo is unknown. Mutations in the Drosophila CRD disrupt Smo activity in vivo, while deletion of the CRD in mammalian cells does not seem to affect the activity of overexpressed Smo. Pssm-ID: 143560 Cd Length: 132 Bit Score: 42.35 E-value: 1.97e-04
|
|||||||||
| Blast search parameters | ||||
|
