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Conserved domains on  [gi|525342595|ref|NP_001266530|]
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growth hormone receptor a precursor [Oreochromis niloticus]

Protein Classification

FN3 and GHBP domain-containing protein( domain architecture ID 10414125)

protein containing domains FN3, and GHBP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GHBP super family cl15082
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 304-607 1.43e-96

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.


The actual alignment was detected with superfamily member pfam12772:

Pssm-ID: 463696  Cd Length: 303  Bit Score: 298.33  E-value: 1.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  304 KGKLDELNFMLSGRGmdglpIYAPDFYQDEPWVELMEVDETedvDNGEKkdNRGSDTQKLLGqsqpvsqHININCSNSVS 383
Cdd:pfam12772   1 KGKLEEVNFILAGHD-----SYKPDFYNDDSWVEFIELDIE---DSDEK--NEGSDTDRLLG-------HDHLKSSNCLG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  384 GPDAESSQATCYNTDLPEEET-----------------LMLMATLLPGQPDEEETSLDTVERSSASETGER--------- 437
Cdd:pfam12772  64 AKDDDSGRASCYEPDIPETDFsasdtcdgtsdiaqskkLEKEADLLCLQPKDNETSLPSLERTPATEQPERplqsegnkp 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  438 ------------QLIQTQTRGPQTWVNTDFYAQVTNVMPTGGVVLSPGQQLRIQESISAAeketkkkrkesedseeseER 505
Cdd:pfam12772 144 rplltdstestsPLVQTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSAS------------------ER 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  506 KQKEPQFQLLVVDpegSAYSTESSIQQIstpppsspmpgegyhIIHPQPVEPRPAATME-LNQSPYIIPDS--PQFF--- 579
Cdd:pfam12772 206 ETQTKGKQNFVVD---SAYFCEADVKKC---------------IAVTPPSEAEPGVGYQtNNEDPYITTESltTTAVsse 267

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 525342595  580 --------APVADYTVVQELDSHHSLLLNPPCHQTP 607
Cdd:pfam12772 268 taelpsseMPVADYTSIHIVQSPQGLVLNATALPVP 303
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 42-114 1.32e-08

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: 52.81  E-value: 1.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525342595   42 EPHFTECISRDQETFHCWWSPGSFHNLSSPGAlrvFYLKKEPPTsqWKECPEYI----HSNRE--CFFDEAHTSIWITY 114
Cdd:pfam09067  10 KPEDIKCFSREKEDFTCFWEEEEDGGLPTTYS---FSYAYENET--VKECPLYStsgaNSTRLfiCFFPKNDVSLFVPL 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 141-243 5.18e-08

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: 50.96  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595 141 PDPPVNLNWTLLNTSpsglnyDVMINWEPPPTADVRLgwmrVEYELQYRERNTTNWEALDIQRQSHQ--TIYGLRLGKEY 218
Cdd:cd00063    1 PSPPTNLRVTDVTST------SVTLSWTPPEDDGGPI----TGYVVEYREKGSGDWKEVEVTPGSETsyTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....*
gi 525342595 219 EVHIRCRMQAFIkfGEFSESVFIQV 243
Cdd:cd00063   71 EFRVRAVNGGGE--SPPSESVTVTT 93
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 304-607 1.43e-96

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: 298.33  E-value: 1.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  304 KGKLDELNFMLSGRGmdglpIYAPDFYQDEPWVELMEVDETedvDNGEKkdNRGSDTQKLLGqsqpvsqHININCSNSVS 383
Cdd:pfam12772   1 KGKLEEVNFILAGHD-----SYKPDFYNDDSWVEFIELDIE---DSDEK--NEGSDTDRLLG-------HDHLKSSNCLG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  384 GPDAESSQATCYNTDLPEEET-----------------LMLMATLLPGQPDEEETSLDTVERSSASETGER--------- 437
Cdd:pfam12772  64 AKDDDSGRASCYEPDIPETDFsasdtcdgtsdiaqskkLEKEADLLCLQPKDNETSLPSLERTPATEQPERplqsegnkp 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  438 ------------QLIQTQTRGPQTWVNTDFYAQVTNVMPTGGVVLSPGQQLRIQESISAAeketkkkrkesedseeseER 505
Cdd:pfam12772 144 rplltdstestsPLVQTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSAS------------------ER 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  506 KQKEPQFQLLVVDpegSAYSTESSIQQIstpppsspmpgegyhIIHPQPVEPRPAATME-LNQSPYIIPDS--PQFF--- 579
Cdd:pfam12772 206 ETQTKGKQNFVVD---SAYFCEADVKKC---------------IAVTPPSEAEPGVGYQtNNEDPYITTESltTTAVsse 267

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 525342595  580 --------APVADYTVVQELDSHHSLLLNPPCHQTP 607
Cdd:pfam12772 268 taelpsseMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 42-114 1.32e-08

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: 52.81  E-value: 1.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525342595   42 EPHFTECISRDQETFHCWWSPGSFHNLSSPGAlrvFYLKKEPPTsqWKECPEYI----HSNRE--CFFDEAHTSIWITY 114
Cdd:pfam09067  10 KPEDIKCFSREKEDFTCFWEEEEDGGLPTTYS---FSYAYENET--VKECPLYStsgaNSTRLfiCFFPKNDVSLFVPL 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 141-243 5.18e-08

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: 50.96  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595 141 PDPPVNLNWTLLNTSpsglnyDVMINWEPPPTADVRLgwmrVEYELQYRERNTTNWEALDIQRQSHQ--TIYGLRLGKEY 218
Cdd:cd00063    1 PSPPTNLRVTDVTST------SVTLSWTPPEDDGGPI----TGYVVEYREKGSGDWKEVEVTPGSETsyTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....*
gi 525342595 219 EVHIRCRMQAFIkfGEFSESVFIQV 243
Cdd:cd00063   71 EFRVRAVNGGGE--SPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 141-225 8.69e-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: 47.22  E-value: 8.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595   141 PDPPVNLNWTLLNTSpsglnyDVMINWEPPPTADVrlGWMRVEYELQYRERNTTNWEALDIQRQSHQTIYGLRLGKEYEV 220
Cdd:smart00060   1 PSPPSNLRVTDVTST------SVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72


                   ....*
gi 525342595   221 HIRCR 225
Cdd:smart00060  73 RVRAV 77
fn3 pfam00041
Fibronectin type III domain;
142-223 1.10e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.16  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  142 DPPVNLNWTllNTSPSGLNydvmINWEPPPTADVRLgwmrVEYELQYRERNTTNWEA-LDIQRQSHQ-TIYGLRLGKEYE 219
Cdd:pfam00041   1 SAPSNLTVT--DVTSTSLT----VSWTPPPDGNGPI----TGYEVEYRPKNSGEPWNeITVPGTTTSvTLTGLKPGTEYE 70


                  ....
gi 525342595  220 VHIR 223
Cdd:pfam00041  71 VRVQ 74
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 304-607 1.43e-96

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: 298.33  E-value: 1.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  304 KGKLDELNFMLSGRGmdglpIYAPDFYQDEPWVELMEVDETedvDNGEKkdNRGSDTQKLLGqsqpvsqHININCSNSVS 383
Cdd:pfam12772   1 KGKLEEVNFILAGHD-----SYKPDFYNDDSWVEFIELDIE---DSDEK--NEGSDTDRLLG-------HDHLKSSNCLG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  384 GPDAESSQATCYNTDLPEEET-----------------LMLMATLLPGQPDEEETSLDTVERSSASETGER--------- 437
Cdd:pfam12772  64 AKDDDSGRASCYEPDIPETDFsasdtcdgtsdiaqskkLEKEADLLCLQPKDNETSLPSLERTPATEQPERplqsegnkp 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  438 ------------QLIQTQTRGPQTWVNTDFYAQVTNVMPTGGVVLSPGQQLRIQESISAAeketkkkrkesedseeseER 505
Cdd:pfam12772 144 rplltdstestsPLVQTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSAS------------------ER 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  506 KQKEPQFQLLVVDpegSAYSTESSIQQIstpppsspmpgegyhIIHPQPVEPRPAATME-LNQSPYIIPDS--PQFF--- 579
Cdd:pfam12772 206 ETQTKGKQNFVVD---SAYFCEADVKKC---------------IAVTPPSEAEPGVGYQtNNEDPYITTESltTTAVsse 267

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 525342595  580 --------APVADYTVVQELDSHHSLLLNPPCHQTP 607
Cdd:pfam12772 268 taelpsseMPVADYTSIHIVQSPQGLVLNATALPVP 303
EpoR_lig-bind pfam09067
Erythropoietin receptor, ligand binding; Members of this family interact with erythropoietin ...
 42-114 1.32e-08

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: 52.81  E-value: 1.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525342595   42 EPHFTECISRDQETFHCWWSPGSFHNLSSPGAlrvFYLKKEPPTsqWKECPEYI----HSNRE--CFFDEAHTSIWITY 114
Cdd:pfam09067  10 KPEDIKCFSREKEDFTCFWEEEEDGGLPTTYS---FSYAYENET--VKECPLYStsgaNSTRLfiCFFPKNDVSLFVPL 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 141-243 5.18e-08

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: 50.96  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595 141 PDPPVNLNWTLLNTSpsglnyDVMINWEPPPTADVRLgwmrVEYELQYRERNTTNWEALDIQRQSHQ--TIYGLRLGKEY 218
Cdd:cd00063    1 PSPPTNLRVTDVTST------SVTLSWTPPEDDGGPI----TGYVVEYREKGSGDWKEVEVTPGSETsyTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|....*
gi 525342595 219 EVHIRCRMQAFIkfGEFSESVFIQV 243
Cdd:cd00063   71 EFRVRAVNGGGE--SPPSESVTVTT 93
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 141-225 8.69e-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: 47.22  E-value: 8.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595   141 PDPPVNLNWTLLNTSpsglnyDVMINWEPPPTADVrlGWMRVEYELQYRERNTTNWEALDIQRQSHQTIYGLRLGKEYEV 220
Cdd:smart00060   1 PSPPSNLRVTDVTST------SVTLSWEPPPDDGI--TGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEF 72


                   ....*
gi 525342595   221 HIRCR 225
Cdd:smart00060  73 RVRAV 77
fn3 pfam00041
Fibronectin type III domain;
142-223 1.10e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.16  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525342595  142 DPPVNLNWTllNTSPSGLNydvmINWEPPPTADVRLgwmrVEYELQYRERNTTNWEA-LDIQRQSHQ-TIYGLRLGKEYE 219
Cdd:pfam00041   1 SAPSNLTVT--DVTSTSLT----VSWTPPPDGNGPI----TGYEVEYRPKNSGEPWNeITVPGTTTSvTLTGLKPGTEYE 70


                  ....
gi 525342595  220 VHIR 223
Cdd:pfam00041  71 VRVQ 74
 
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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