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Conserved domains on  [gi|1918140648|gb|QOP76497|]
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growth hormone receptor, partial [Stylodipus telum]

Protein Classification

growth hormone receptor binding protein( domain architecture ID 10579657)

growth hormone receptor binding protein (GHBP) is produced either by proteolysis of the GHR (growth hormone receptor) at the cell surface thereby releasing its extracellular domain, the GHBP, or by alternative processing of the GHR transcript

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 ...
 1-201 1.77e-103

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: 300.26  E-value: 1.77e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918140648   1 PEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLNNDHQRSLNILGAKDDDSGRTSCYDPDILETDFPASDMCDGASGVAQ 80
Cdd:pfam12772  19 PDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIPETDFSASDTCDGTSDIAQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918140648  81 PQRLKGEADLLCLDQK-NQNNLPY-DASPATQQPS-TTLTEEDKPQPLLTSETESTHQLASMQISNPSSLANIDFYAQVS 157
Cdd:pfam12772  99 SKKLEKEADLLCLQPKdNETSLPSlERTPATEQPErPLQSEGNKPRPLLTDSTESTSPLVQTQLSNPQSLANTDFYAQVS 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1918140648 158 DITPAGSVVLSPGQKSKAGIPPCDiMHPEVISVCQANYNLDSAY 201
Cdd:pfam12772 179 DITPAGGVVLSPGQKLKAGESQSA-SERETQTKGKQNFVVDSAY 221
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 1-201 1.77e-103

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: 300.26  E-value: 1.77e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918140648   1 PEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLNNDHQRSLNILGAKDDDSGRTSCYDPDILETDFPASDMCDGASGVAQ 80
Cdd:pfam12772  19 PDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIPETDFSASDTCDGTSDIAQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918140648  81 PQRLKGEADLLCLDQK-NQNNLPY-DASPATQQPS-TTLTEEDKPQPLLTSETESTHQLASMQISNPSSLANIDFYAQVS 157
Cdd:pfam12772  99 SKKLEKEADLLCLQPKdNETSLPSlERTPATEQPErPLQSEGNKPRPLLTDSTESTSPLVQTQLSNPQSLANTDFYAQVS 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1918140648 158 DITPAGSVVLSPGQKSKAGIPPCDiMHPEVISVCQANYNLDSAY 201
Cdd:pfam12772 179 DITPAGGVVLSPGQKLKAGESQSA-SERETQTKGKQNFVVDSAY 221
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 1-201 1.77e-103

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: 300.26  E-value: 1.77e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918140648   1 PEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLNNDHQRSLNILGAKDDDSGRTSCYDPDILETDFPASDMCDGASGVAQ 80
Cdd:pfam12772  19 PDFYNDDSWVEFIELDIEDSDEKNEGSDTDRLLGHDHLKSSNCLGAKDDDSGRASCYEPDIPETDFSASDTCDGTSDIAQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918140648  81 PQRLKGEADLLCLDQK-NQNNLPY-DASPATQQPS-TTLTEEDKPQPLLTSETESTHQLASMQISNPSSLANIDFYAQVS 157
Cdd:pfam12772  99 SKKLEKEADLLCLQPKdNETSLPSlERTPATEQPErPLQSEGNKPRPLLTDSTESTSPLVQTQLSNPQSLANTDFYAQVS 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1918140648 158 DITPAGSVVLSPGQKSKAGIPPCDiMHPEVISVCQANYNLDSAY 201
Cdd:pfam12772 179 DITPAGGVVLSPGQKLKAGESQSA-SERETQTKGKQNFVVDSAY 221
 
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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