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Conserved domains on  [gi|23503291|ref|NP_699191|]
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protein APCDD1-like isoform 1 precursor [Homo sapiens]

Protein Classification

APCDDC domain-containing protein( domain architecture ID 10633044)

APCDDC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 37-263 3.74e-107

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


:

Pssm-ID: 464377  Cd Length: 235  Bit Score: 318.52  E-value: 3.74e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291    37 CQQ---PLPDRVPSTAILPPRLNGPWISTGCEVRPGPEFLTRAYTFYPSRLFRAHQFYYEDPFCGEPAHSLLVKGKVRLR 113
Cdd:pfam14921   2 CRQalrHIQNGARITADIPPRLEGHWVSQRCEVRPGPEFLTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   114 RASWVTRGATEADYHLHKVGIVFHSRRALVDVTGRLNQTragrdCARRLPPARAWLPGALYELRSARA----QGDCLEAL 189
Cdd:pfam14921  82 QASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQS-----CPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23503291   190 GLTMHELSLVRVQRRLQPQPRaspRLVEELYLGDIHTDPAERRHYRPTGYQRPLQSALHHVQPCPACGLIARSD 263
Cdd:pfam14921 157 GFSMHELSLLRVEKQYHLHGQ---QPVEELFLGDIHTDWSQRRHYRPTSYQPPLQNAMNHTHPCPICGLISRST 227
APCDDC super family cl20807
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 282-452 1.49e-21

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


The actual alignment was detected with superfamily member pfam14921:

Pssm-ID: 464377  Cd Length: 235  Bit Score: 93.56  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   282 GWWVSSGCEVRPAVLFLTRLFTFHgHSRSWEGYYHHFSDPACRQPTFTVYAAGRYTRGTPSTRVRGGTELVFEVTRAHVT 361
Cdd:pfam14921  25 GHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVIRGKIRLRQASWIVRGATEADYHLHKVHIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   362 PMDQVttAMLNFSE--PSSCGG----AGAWSMGTERDVTATNG-------CL-PLGI---RLPHVEYELFKMEQDPLGQS 424
Cdd:pfam14921 104 PHSQA--VAHKLAQrlNQSCPGplppWRPWVPGTLYELLRQHNakfnsrdCLeAFGFsmhELSLLRVEKQYHLHGQQPVE 181

                         170       180
                  ....*....|....*....|....*...
gi 23503291   425 LLFIGQRPTDGSSPDTpeKRPTSYQAPL 452
Cdd:pfam14921 182 ELFLGDIHTDWSQRRH--YRPTSYQPPL 207
 
Name Accession Description Interval E-value
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 37-263 3.74e-107

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 318.52  E-value: 3.74e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291    37 CQQ---PLPDRVPSTAILPPRLNGPWISTGCEVRPGPEFLTRAYTFYPSRLFRAHQFYYEDPFCGEPAHSLLVKGKVRLR 113
Cdd:pfam14921   2 CRQalrHIQNGARITADIPPRLEGHWVSQRCEVRPGPEFLTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   114 RASWVTRGATEADYHLHKVGIVFHSRRALVDVTGRLNQTragrdCARRLPPARAWLPGALYELRSARA----QGDCLEAL 189
Cdd:pfam14921  82 QASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQS-----CPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23503291   190 GLTMHELSLVRVQRRLQPQPRaspRLVEELYLGDIHTDPAERRHYRPTGYQRPLQSALHHVQPCPACGLIARSD 263
Cdd:pfam14921 157 GFSMHELSLLRVEKQYHLHGQ---QPVEELFLGDIHTDWSQRRHYRPTSYQPPLQNAMNHTHPCPICGLISRST 227
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 282-452 1.49e-21

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 93.56  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   282 GWWVSSGCEVRPAVLFLTRLFTFHgHSRSWEGYYHHFSDPACRQPTFTVYAAGRYTRGTPSTRVRGGTELVFEVTRAHVT 361
Cdd:pfam14921  25 GHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVIRGKIRLRQASWIVRGATEADYHLHKVHIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   362 PMDQVttAMLNFSE--PSSCGG----AGAWSMGTERDVTATNG-------CL-PLGI---RLPHVEYELFKMEQDPLGQS 424
Cdd:pfam14921 104 PHSQA--VAHKLAQrlNQSCPGplppWRPWVPGTLYELLRQHNakfnsrdCLeAFGFsmhELSLLRVEKQYHLHGQQPVE 181

                         170       180
                  ....*....|....*....|....*...
gi 23503291   425 LLFIGQRPTDGSSPDTpeKRPTSYQAPL 452
Cdd:pfam14921 182 ELFLGDIHTDWSQRRH--YRPTSYQPPL 207
 
Name Accession Description Interval E-value
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 37-263 3.74e-107

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 318.52  E-value: 3.74e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291    37 CQQ---PLPDRVPSTAILPPRLNGPWISTGCEVRPGPEFLTRAYTFYPSRLFRAHQFYYEDPFCGEPAHSLLVKGKVRLR 113
Cdd:pfam14921   2 CRQalrHIQNGARITADIPPRLEGHWVSQRCEVRPGPEFLTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   114 RASWVTRGATEADYHLHKVGIVFHSRRALVDVTGRLNQTragrdCARRLPPARAWLPGALYELRSARA----QGDCLEAL 189
Cdd:pfam14921  82 QASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQS-----CPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAF 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23503291   190 GLTMHELSLVRVQRRLQPQPRaspRLVEELYLGDIHTDPAERRHYRPTGYQRPLQSALHHVQPCPACGLIARSD 263
Cdd:pfam14921 157 GFSMHELSLLRVEKQYHLHGQ---QPVEELFLGDIHTDWSQRRHYRPTSYQPPLQNAMNHTHPCPICGLISRST 227
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 282-452 1.49e-21

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 93.56  E-value: 1.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   282 GWWVSSGCEVRPAVLFLTRLFTFHgHSRSWEGYYHHFSDPACRQPTFTVYAAGRYTRGTPSTRVRGGTELVFEVTRAHVT 361
Cdd:pfam14921  25 GHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVIRGKIRLRQASWIVRGATEADYHLHKVHIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23503291   362 PMDQVttAMLNFSE--PSSCGG----AGAWSMGTERDVTATNG-------CL-PLGI---RLPHVEYELFKMEQDPLGQS 424
Cdd:pfam14921 104 PHSQA--VAHKLAQrlNQSCPGplppWRPWVPGTLYELLRQHNakfnsrdCLeAFGFsmhELSLLRVEKQYHLHGQQPVE 181

                         170       180
                  ....*....|....*....|....*...
gi 23503291   425 LLFIGQRPTDGSSPDTpeKRPTSYQAPL 452
Cdd:pfam14921 182 ELFLGDIHTDWSQRRH--YRPTSYQPPL 207
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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