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Conserved domains on  [gi|556503394|ref|NP_001273299|]
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growth hormone receptor isoform 1 precursor [Mus musculus]

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 ...
 325-628 4.24e-179

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: 510.19  E-value: 4.24e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  325 EGKLEEVNTILGIHDNYKPDFYNDDSWVEFIELDIDeaDVDEKTEGSDTDRLLSNDHEKSAGILGAKDDDSGRTSCYDPD 404
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIE--DSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  405 ILDTDFHTSDMCDGTLKFAQSQKLNMEADLLCLDQK-NLKNLPY-DASLGSLHPSITQTVEENKPQPLLSSETEATHQLA 482
Cdd:pfam12772  79 IPETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSlERTPATEQPERPLQSEGNKPRPLLTDSTESTSPLV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  483 STPMSNPTSLANIDFYAQVSDITPAGGVVLSPGQKIKAGIAQGNTQREVATPCQENYSMNSAYFCESDAKKCIAVAPRME 562
Cdd:pfam12772 159 QTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSE 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556503394  563 ATSCIKPSFNQEDIYITTESLTTTAQMSETADIaPDAEMSVPDYTTVHTVQSPRGLILNATALPLP 628
Cdd:pfam12772 239 AEPGVGYQTNNEDPYITTESLTTTAVSSETAEL-PSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 49-135 4.01e-14

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: 68.60  E-value: 4.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394   49 GKPRFTKCRSPELETFSCYWTEGDNPDLKTPGSiqLYYAKREsqrqaariahewtQEWKECPDYVSAGKNS-----CYFN 123
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEEDGGLPTTYS--FSYAYEN-------------ETVKECPLYSTSGANStrlfiCFFP 73

                          90
                  ....*....|..
gi 556503394  124 SSYTSIWIPYCI 135
Cdd:pfam09067  74 KNDVSLFVPLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 157-258 6.85e-09

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: 53.27  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394 157 PDPPIGLNWTLLNisltgiRGDIQVSWQPPPNadvlKGWIILEYEIQYKEVNESKWKVMGPIWL--TYCPVYSLRMDKEH 234
Cdd:cd00063    1 PSPPTNLRVTDVT------STSVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....
gi 556503394 235 EVRVRSrqRSFEKYSEFSEVLRVI 258
Cdd:cd00063   71 EFRVRA--VNGGGESPPSESVTVT 92
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 325-628 4.24e-179

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: 510.19  E-value: 4.24e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  325 EGKLEEVNTILGIHDNYKPDFYNDDSWVEFIELDIDeaDVDEKTEGSDTDRLLSNDHEKSAGILGAKDDDSGRTSCYDPD 404
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIE--DSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  405 ILDTDFHTSDMCDGTLKFAQSQKLNMEADLLCLDQK-NLKNLPY-DASLGSLHPSITQTVEENKPQPLLSSETEATHQLA 482
Cdd:pfam12772  79 IPETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSlERTPATEQPERPLQSEGNKPRPLLTDSTESTSPLV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  483 STPMSNPTSLANIDFYAQVSDITPAGGVVLSPGQKIKAGIAQGNTQREVATPCQENYSMNSAYFCESDAKKCIAVAPRME 562
Cdd:pfam12772 159 QTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSE 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556503394  563 ATSCIKPSFNQEDIYITTESLTTTAQMSETADIaPDAEMSVPDYTTVHTVQSPRGLILNATALPLP 628
Cdd:pfam12772 239 AEPGVGYQTNNEDPYITTESLTTTAVSSETAEL-PSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 49-135 4.01e-14

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: 68.60  E-value: 4.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394   49 GKPRFTKCRSPELETFSCYWTEGDNPDLKTPGSiqLYYAKREsqrqaariahewtQEWKECPDYVSAGKNS-----CYFN 123
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEEDGGLPTTYS--FSYAYEN-------------ETVKECPLYSTSGANStrlfiCFFP 73

                          90
                  ....*....|..
gi 556503394  124 SSYTSIWIPYCI 135
Cdd:pfam09067  74 KNDVSLFVPLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 157-258 6.85e-09

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: 53.27  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394 157 PDPPIGLNWTLLNisltgiRGDIQVSWQPPPNadvlKGWIILEYEIQYKEVNESKWKVMGPIWL--TYCPVYSLRMDKEH 234
Cdd:cd00063    1 PSPPTNLRVTDVT------STSVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....
gi 556503394 235 EVRVRSrqRSFEKYSEFSEVLRVI 258
Cdd:cd00063   71 EFRVRA--VNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 157-241 3.38e-07

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: 48.38  E-value: 3.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394   157 PDPPIGLNWTLLNisltgiRGDIQVSWQPPPNADVlkGWIILEYEIQYKEVNESKWKVMGPIWLTYCPVYSLRMDKEHEV 236
Cdd:smart00060   1 PSPPSNLRVTDVT------STSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72


                   ....*
gi 556503394   237 RVRSR 241
Cdd:smart00060  73 RVRAV 77
fn3 pfam00041
Fibronectin type III domain;
169-241 1.78e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.48  E-value: 1.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556503394  169 NISLTGIRGD-IQVSWQPPPNADVlkgwIILEYEIQYKEVNESKWKVMGPI--WLTYCPVYSLRMDKEHEVRVRSR 241
Cdd:pfam00041   5 NLTVTDVTSTsLTVSWTPPPDGNG----PITGYEVEYRPKNSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAV 76
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 325-628 4.24e-179

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: 510.19  E-value: 4.24e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  325 EGKLEEVNTILGIHDNYKPDFYNDDSWVEFIELDIDeaDVDEKTEGSDTDRLLSNDHEKSAGILGAKDDDSGRTSCYDPD 404
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIE--DSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  405 ILDTDFHTSDMCDGTLKFAQSQKLNMEADLLCLDQK-NLKNLPY-DASLGSLHPSITQTVEENKPQPLLSSETEATHQLA 482
Cdd:pfam12772  79 IPETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSlERTPATEQPERPLQSEGNKPRPLLTDSTESTSPLV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394  483 STPMSNPTSLANIDFYAQVSDITPAGGVVLSPGQKIKAGIAQGNTQREVATPCQENYSMNSAYFCESDAKKCIAVAPRME 562
Cdd:pfam12772 159 QTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSE 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556503394  563 ATSCIKPSFNQEDIYITTESLTTTAQMSETADIaPDAEMSVPDYTTVHTVQSPRGLILNATALPLP 628
Cdd:pfam12772 239 AEPGVGYQTNNEDPYITTESLTTTAVSSETAEL-PSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 49-135 4.01e-14

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: 68.60  E-value: 4.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394   49 GKPRFTKCRSPELETFSCYWTEGDNPDLKTPGSiqLYYAKREsqrqaariahewtQEWKECPDYVSAGKNS-----CYFN 123
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEEDGGLPTTYS--FSYAYEN-------------ETVKECPLYSTSGANStrlfiCFFP 73

                          90
                  ....*....|..
gi 556503394  124 SSYTSIWIPYCI 135
Cdd:pfam09067  74 KNDVSLFVPLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 157-258 6.85e-09

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: 53.27  E-value: 6.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394 157 PDPPIGLNWTLLNisltgiRGDIQVSWQPPPNadvlKGWIILEYEIQYKEVNESKWKVMGPIWL--TYCPVYSLRMDKEH 234
Cdd:cd00063    1 PSPPTNLRVTDVT------STSVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....
gi 556503394 235 EVRVRSrqRSFEKYSEFSEVLRVI 258
Cdd:cd00063   71 EFRVRA--VNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 157-241 3.38e-07

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: 48.38  E-value: 3.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556503394   157 PDPPIGLNWTLLNisltgiRGDIQVSWQPPPNADVlkGWIILEYEIQYKEVNESKWKVMGPIWLTYCPVYSLRMDKEHEV 236
Cdd:smart00060   1 PSPPSNLRVTDVT------STSVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72


                   ....*
gi 556503394   237 RVRSR 241
Cdd:smart00060  73 RVRAV 77
fn3 pfam00041
Fibronectin type III domain;
169-241 1.78e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 40.48  E-value: 1.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556503394  169 NISLTGIRGD-IQVSWQPPPNADVlkgwIILEYEIQYKEVNESKWKVMGPI--WLTYCPVYSLRMDKEHEVRVRSR 241
Cdd:pfam00041   5 NLTVTDVTSTsLTVSWTPPPDGNG----PITGYEVEYRPKNSGEPWNEITVpgTTTSVTLTGLKPGTEYEVRVQAV 76
 
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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