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Conserved domains on  [gi|1269201230|gb|ATN95154|]
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Growth hormone receptor [Eschrichtius robustus]

Protein Classification

FN3 and GHBP domain-containing protein( domain architecture ID 10414142)

protein containing domains FN3, and GHBP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 317-619 0e+00

Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP (growth hormone-binding protein), or, in rodents, by alternative processing of the GHR transcript. The sheddase proteolytic enzyme responsible for the cleavage is TACE (tumour necrosis factor-alpha-converting enzyme). Growth hormone (GH) binding to GH receptor (GHR) is the initial step that leads to the physiological functions of the hormone. The biological effects of GHBP are determined by the serum levels of growth hormone (GH), which can vary. Low levels of GH can result in a dwarf phenotype and have been positively correlated with an increased life expectancy. High levels of GH can lead to gigantism or a clinical syndrome termed acromegaly and have been implicated in diabetic eye and kidney damage.


:

Pssm-ID: 463696  Cd Length: 303  Bit Score: 525.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 317 EGKLEEVNTILAIHDNYKHEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNDHEKSLNILGAKDDDSGRTSCYEPDIL 396
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 397 ETDFNASDMCDGTSEVAQPQRLKGEADRLCLDQK-NQNNSPSNDAAPASQQPSV-ILGEENKPRSLLIGGTESTHQAGHT 474
Cdd:pfam12772  81 ETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSLERTPATEQPERpLQSEGNKPRPLLTDSTESTSPLVQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 475 qQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGISQCDMHPEVVSPCQANFIMDNAYFCEADAKKCIALAPHVEV 554
Cdd:pfam12772 161 -QLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSEA 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269201230 555 ESHVEPSFNQEDIYITTESLTTTAGRSGTAERvPSSEMPVPDYTSIHIVQSPQGLVLNATALPLP 619
Cdd:pfam12772 240 EPGVGYQTNNEDPYITTESLTTTAVSSETAEL-PSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 49-127 4.04e-13

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


The actual alignment was detected with superfamily member pfam09067:

Pssm-ID: 473895  Cd Length: 104  Bit Score: 65.91  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230  49 KKPKFTKCRSPELETFSCHWTDGVHHGLqsPGSIQLFYirrstQEWTQEWKECPDYVSAGENS-----CYFNSSYTSIWI 123
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEEDGGL--PTTYSFSY-----AYENETVKECPLYSTSGANStrlfiCFFPKNDVSLFV 81


                  ....
gi 1269201230 124 PYCI 127
Cdd:pfam09067  82 PLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 149-250 5.46e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.13  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 149 PDPPIglnwtllNISLTGIHAD-IQVRWEPPPNadvqKGWIVLEYELQYKEVNETQWKMMDPVL--STSVPVYSLRLDKE 225
Cdd:cd00063     1 PSPPT-------NLRVTDVTSTsVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....*
gi 1269201230 226 YEVRVRSrqRNSEKYGEFSEVLFVT 250
Cdd:cd00063    70 YEFRVRA--VNGGGESPPSESVTVT 92
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 317-619 0e+00

Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP (growth hormone-binding protein), or, in rodents, by alternative processing of the GHR transcript. The sheddase proteolytic enzyme responsible for the cleavage is TACE (tumour necrosis factor-alpha-converting enzyme). Growth hormone (GH) binding to GH receptor (GHR) is the initial step that leads to the physiological functions of the hormone. The biological effects of GHBP are determined by the serum levels of growth hormone (GH), which can vary. Low levels of GH can result in a dwarf phenotype and have been positively correlated with an increased life expectancy. High levels of GH can lead to gigantism or a clinical syndrome termed acromegaly and have been implicated in diabetic eye and kidney damage.


Pssm-ID: 463696  Cd Length: 303  Bit Score: 525.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 317 EGKLEEVNTILAIHDNYKHEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNDHEKSLNILGAKDDDSGRTSCYEPDIL 396
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 397 ETDFNASDMCDGTSEVAQPQRLKGEADRLCLDQK-NQNNSPSNDAAPASQQPSV-ILGEENKPRSLLIGGTESTHQAGHT 474
Cdd:pfam12772  81 ETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSLERTPATEQPERpLQSEGNKPRPLLTDSTESTSPLVQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 475 qQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGISQCDMHPEVVSPCQANFIMDNAYFCEADAKKCIALAPHVEV 554
Cdd:pfam12772 161 -QLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSEA 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269201230 555 ESHVEPSFNQEDIYITTESLTTTAGRSGTAERvPSSEMPVPDYTSIHIVQSPQGLVLNATALPLP 619
Cdd:pfam12772 240 EPGVGYQTNNEDPYITTESLTTTAVSSETAEL-PSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 49-127 4.04e-13

Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through induction of the JAK2/STAT5 signaling cascade. The domain adopts a secondary structure composed of a short amino-terminal helix, followed by two beta-sandwich regions.


Pssm-ID: 401127  Cd Length: 104  Bit Score: 65.91  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230  49 KKPKFTKCRSPELETFSCHWTDGVHHGLqsPGSIQLFYirrstQEWTQEWKECPDYVSAGENS-----CYFNSSYTSIWI 123
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEEDGGL--PTTYSFSY-----AYENETVKECPLYSTSGANStrlfiCFFPKNDVSLFV 81


                  ....
gi 1269201230 124 PYCI 127
Cdd:pfam09067  82 PLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 149-250 5.46e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.13  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 149 PDPPIglnwtllNISLTGIHAD-IQVRWEPPPNadvqKGWIVLEYELQYKEVNETQWKMMDPVL--STSVPVYSLRLDKE 225
Cdd:cd00063     1 PSPPT-------NLRVTDVTSTsVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....*
gi 1269201230 226 YEVRVRSrqRNSEKYGEFSEVLFVT 250
Cdd:cd00063    70 YEFRVRA--VNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 149-233 7.66e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 7.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230  149 PDPPIglnwtllNISLTGIHAD-IQVRWEPPPNADVqkGWIVLEYELQYKEVNETQWKMMDPVLSTSVPVYSLRLDKEYE 227
Cdd:smart00060   1 PSPPS-------NLRVTDVTSTsVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71


                   ....*.
gi 1269201230  228 VRVRSR 233
Cdd:smart00060  72 FRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
161-244 1.13e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 161 NISLTGIHAD-IQVRWEPPPNADVQkgwiVLEYELQYKEVNETQWKMMDPVLST--SVPVYSLRLDKEYEVRVRSrqRNS 237
Cdd:pfam00041   5 NLTVTDVTSTsLTVSWTPPPDGNGP----ITGYEVEYRPKNSGEPWNEITVPGTttSVTLTGLKPGTEYEVRVQA--VNG 78


                  ....*..
gi 1269201230 238 EKYGEFS 244
Cdd:pfam00041  79 GGEGPPS 85
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 317-619 0e+00

Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP (growth hormone-binding protein), or, in rodents, by alternative processing of the GHR transcript. The sheddase proteolytic enzyme responsible for the cleavage is TACE (tumour necrosis factor-alpha-converting enzyme). Growth hormone (GH) binding to GH receptor (GHR) is the initial step that leads to the physiological functions of the hormone. The biological effects of GHBP are determined by the serum levels of growth hormone (GH), which can vary. Low levels of GH can result in a dwarf phenotype and have been positively correlated with an increased life expectancy. High levels of GH can lead to gigantism or a clinical syndrome termed acromegaly and have been implicated in diabetic eye and kidney damage.


Pssm-ID: 463696  Cd Length: 303  Bit Score: 525.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 317 EGKLEEVNTILAIHDNYKHEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNDHEKSLNILGAKDDDSGRTSCYEPDIL 396
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 397 ETDFNASDMCDGTSEVAQPQRLKGEADRLCLDQK-NQNNSPSNDAAPASQQPSV-ILGEENKPRSLLIGGTESTHQAGHT 474
Cdd:pfam12772  81 ETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSLERTPATEQPERpLQSEGNKPRPLLTDSTESTSPLVQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 475 qQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGISQCDMHPEVVSPCQANFIMDNAYFCEADAKKCIALAPHVEV 554
Cdd:pfam12772 161 -QLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSEA 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269201230 555 ESHVEPSFNQEDIYITTESLTTTAGRSGTAERvPSSEMPVPDYTSIHIVQSPQGLVLNATALPLP 619
Cdd:pfam12772 240 EPGVGYQTNNEDPYITTESLTTTAVSSETAEL-PSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 49-127 4.04e-13

Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin (EPO), with subsequent initiation of the downstream chain of events associated with binding of EPO to the receptor, including EPO-induced erythroblast proliferation and differentiation through induction of the JAK2/STAT5 signaling cascade. The domain adopts a secondary structure composed of a short amino-terminal helix, followed by two beta-sandwich regions.


Pssm-ID: 401127  Cd Length: 104  Bit Score: 65.91  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230  49 KKPKFTKCRSPELETFSCHWTDGVHHGLqsPGSIQLFYirrstQEWTQEWKECPDYVSAGENS-----CYFNSSYTSIWI 123
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEEDGGL--PTTYSFSY-----AYENETVKECPLYSTSGANStrlfiCFFPKNDVSLFV 81


                  ....
gi 1269201230 124 PYCI 127
Cdd:pfam09067  82 PLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 149-250 5.46e-12

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 62.13  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 149 PDPPIglnwtllNISLTGIHAD-IQVRWEPPPNadvqKGWIVLEYELQYKEVNETQWKMMDPVL--STSVPVYSLRLDKE 225
Cdd:cd00063     1 PSPPT-------NLRVTDVTSTsVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEVTPgsETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....*
gi 1269201230 226 YEVRVRSrqRNSEKYGEFSEVLFVT 250
Cdd:cd00063    70 YEFRVRA--VNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 149-233 7.66e-09

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 53.00  E-value: 7.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230  149 PDPPIglnwtllNISLTGIHAD-IQVRWEPPPNADVqkGWIVLEYELQYKEVNETQWKMMDPVLSTSVPVYSLRLDKEYE 227
Cdd:smart00060   1 PSPPS-------NLRVTDVTSTsVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71


                   ....*.
gi 1269201230  228 VRVRSR 233
Cdd:smart00060  72 FRVRAV 77
fn3 pfam00041
Fibronectin type III domain;
161-244 1.13e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.64  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269201230 161 NISLTGIHAD-IQVRWEPPPNADVQkgwiVLEYELQYKEVNETQWKMMDPVLST--SVPVYSLRLDKEYEVRVRSrqRNS 237
Cdd:pfam00041   5 NLTVTDVTSTsLTVSWTPPPDGNGP----ITGYEVEYRPKNSGEPWNEITVPGTttSVTLTGLKPGTEYEVRVQA--VNG 78


                  ....*..
gi 1269201230 238 EKYGEFS 244
Cdd:pfam00041  79 GGEGPPS 85
 
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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