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Conserved domains on  [gi|1622942936|ref|XP_028704954|]
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growth hormone receptor isoform X2 [Macaca mulatta]

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 ...
 314-615 6.37e-172

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: 491.32  E-value: 6.37e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 314 EGKLEEVNAILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKNEGSDTDRLLSSDHQKSHSNLGVKDGDSGRTSCYEPDIL 393
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 394 ETDFNANNIHEGTSEVAQPQRLKGEADLLCLDQK-NQNKSPYHDACPATQQPSV-IQAEKNKPQPLPTDGAESTHQAAHI 471
Cdd:pfam12772  81 ETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSLERTPATEQPERpLQSEGNKPRPLLTDSTESTSPLVQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 472 QLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHLEMVSLCQEDFIMDNAYFCEADAKKCIPVAPHIKVE 551
Cdd:pfam12772 161 QLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSEAE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942936 552 SHIEPSFNQEDIYITTESLTTTAGRPGTTEhIPGSEMPVPDYTSIHIVQSPQGLILNATALPLP 615
Cdd:pfam12772 241 PGVGYQTNNEDPYITTESLTTTAVSSETAE-LPSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 47-125 6.33e-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: 65.13  E-value: 6.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936  47 KEPKFTKCRSPERETFSCHWTDAVhhgSKSLGPI-QLFYTRRNiqgqtQEWKECPDYVSAGENS-----CYFNSSFTSVW 120
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEE---DGGLPTTySFSYAYEN-----ETVKECPLYSTSGANStrlfiCFFPKNDVSLF 80


                  ....*
gi 1622942936 121 IPYCI 125
Cdd:pfam09067  81 VPLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 147-248 2.71e-11

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: 60.20  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 147 PDPPIalnwtllNVSLTGIHAD-IQVRWEAPPNadiqKGWMVLEYELQYKEVNETKWKMMD--PILSTSVPVYSLKVDKE 223
Cdd:cd00063     1 PSPPT-------NLRVTDVTSTsVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....*
gi 1622942936 224 YEVRVRSkrRNSRNYGEFSEVLYVT 248
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 ...
 314-615 6.37e-172

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: 491.32  E-value: 6.37e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 314 EGKLEEVNAILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKNEGSDTDRLLSSDHQKSHSNLGVKDGDSGRTSCYEPDIL 393
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 394 ETDFNANNIHEGTSEVAQPQRLKGEADLLCLDQK-NQNKSPYHDACPATQQPSV-IQAEKNKPQPLPTDGAESTHQAAHI 471
Cdd:pfam12772  81 ETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSLERTPATEQPERpLQSEGNKPRPLLTDSTESTSPLVQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 472 QLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHLEMVSLCQEDFIMDNAYFCEADAKKCIPVAPHIKVE 551
Cdd:pfam12772 161 QLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSEAE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942936 552 SHIEPSFNQEDIYITTESLTTTAGRPGTTEhIPGSEMPVPDYTSIHIVQSPQGLILNATALPLP 615
Cdd:pfam12772 241 PGVGYQTNNEDPYITTESLTTTAVSSETAE-LPSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 47-125 6.33e-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: 65.13  E-value: 6.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936  47 KEPKFTKCRSPERETFSCHWTDAVhhgSKSLGPI-QLFYTRRNiqgqtQEWKECPDYVSAGENS-----CYFNSSFTSVW 120
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEE---DGGLPTTySFSYAYEN-----ETVKECPLYSTSGANStrlfiCFFPKNDVSLF 80


                  ....*
gi 1622942936 121 IPYCI 125
Cdd:pfam09067  81 VPLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 147-248 2.71e-11

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: 60.20  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 147 PDPPIalnwtllNVSLTGIHAD-IQVRWEAPPNadiqKGWMVLEYELQYKEVNETKWKMMD--PILSTSVPVYSLKVDKE 223
Cdd:cd00063     1 PSPPT-------NLRVTDVTSTsVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....*
gi 1622942936 224 YEVRVRSkrRNSRNYGEFSEVLYVT 248
Cdd:cd00063    70 YEFRVRA--VNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 147-239 4.66e-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: 47.99  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936  147 PDPPIalnwtllNVSLTGIHAD-IQVRWEAPPNADIqkGWMVLEYELQYKEVNETKWKMMDPILSTSVPVYSLKVDKEYE 225
Cdd:smart00060   1 PSPPS-------NLRVTDVTSTsVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71

                           90
                   ....*....|....
gi 1622942936  226 VRVRSkrRNSRNYG 239
Cdd:smart00060  72 FRVRA--VNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
159-242 1.60e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 159 NVSLTGIHAD-IQVRWEAPPNADIQkgwmVLEYELQYKEVNETKWKMMDPILST--SVPVYSLKVDKEYEVRVRSkrRNS 235
Cdd:pfam00041   5 NLTVTDVTSTsLTVSWTPPPDGNGP----ITGYEVEYRPKNSGEPWNEITVPGTttSVTLTGLKPGTEYEVRVQA--VNG 78


                  ....*..
gi 1622942936 236 RNYGEFS 242
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 ...
 314-615 6.37e-172

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: 491.32  E-value: 6.37e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 314 EGKLEEVNAILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKNEGSDTDRLLSSDHQKSHSNLGVKDGDSGRTSCYEPDIL 393
Cdd:pfam12772   1 KGKLEEVNFILAGHDSYKPDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 394 ETDFNANNIHEGTSEVAQPQRLKGEADLLCLDQK-NQNKSPYHDACPATQQPSV-IQAEKNKPQPLPTDGAESTHQAAHI 471
Cdd:pfam12772  81 ETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKdNETSLPSLERTPATEQPERpLQSEGNKPRPLLTDSTESTSPLVQT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 472 QLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHLEMVSLCQEDFIMDNAYFCEADAKKCIPVAPHIKVE 551
Cdd:pfam12772 161 QLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCIAVTPPSEAE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942936 552 SHIEPSFNQEDIYITTESLTTTAGRPGTTEhIPGSEMPVPDYTSIHIVQSPQGLILNATALPLP 615
Cdd:pfam12772 241 PGVGYQTNNEDPYITTESLTTTAVSSETAE-LPSSEMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 47-125 6.33e-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: 65.13  E-value: 6.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936  47 KEPKFTKCRSPERETFSCHWTDAVhhgSKSLGPI-QLFYTRRNiqgqtQEWKECPDYVSAGENS-----CYFNSSFTSVW 120
Cdd:pfam09067   9 EKPEDIKCFSREKEDFTCFWEEEE---DGGLPTTySFSYAYEN-----ETVKECPLYSTSGANStrlfiCFFPKNDVSLF 80


                  ....*
gi 1622942936 121 IPYCI 125
Cdd:pfam09067  81 VPLHI 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 147-248 2.71e-11

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: 60.20  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 147 PDPPIalnwtllNVSLTGIHAD-IQVRWEAPPNadiqKGWMVLEYELQYKEVNETKWKMMD--PILSTSVPVYSLKVDKE 223
Cdd:cd00063     1 PSPPT-------NLRVTDVTSTsVTLSWTPPED----DGGPITGYVVEYREKGSGDWKEVEvtPGSETSYTLTGLKPGTE 69

                          90       100
                  ....*....|....*....|....*
gi 1622942936 224 YEVRVRSkrRNSRNYGEFSEVLYVT 248
Cdd:cd00063    70 YEFRVRA--VNGGGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 147-239 4.66e-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: 47.99  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936  147 PDPPIalnwtllNVSLTGIHAD-IQVRWEAPPNADIqkGWMVLEYELQYKEVNETKWKMMDPILSTSVPVYSLKVDKEYE 225
Cdd:smart00060   1 PSPPS-------NLRVTDVTSTsVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYE 71

                           90
                   ....*....|....
gi 1622942936  226 VRVRSkrRNSRNYG 239
Cdd:smart00060  72 FRVRA--VNGAGEG 83
fn3 pfam00041
Fibronectin type III domain;
159-242 1.60e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 46.25  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942936 159 NVSLTGIHAD-IQVRWEAPPNADIQkgwmVLEYELQYKEVNETKWKMMDPILST--SVPVYSLKVDKEYEVRVRSkrRNS 235
Cdd:pfam00041   5 NLTVTDVTSTsLTVSWTPPPDGNGP----ITGYEVEYRPKNSGEPWNEITVPGTttSVTLTGLKPGTEYEVRVQA--VNG 78


                  ....*..
gi 1622942936 236 RNYGEFS 242
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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