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Conserved domains on  [gi|1819749297|gb|QII57687|]
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growth hormone receptor, partial [Crocidura sp. dark-lea]

Protein Classification

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 ...
 1-188 2.37e-85

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: 253.65  E-value: 2.37e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819749297   1 TSCYEPDILETDFHASDTCDGTSELEQPQRLKEEAVLLCLEKKQNHSLSNDTLSSI--PQPSV-TLAQESKSRPLVIGGT 77
Cdd:pfam12772  72 ASCYEPDIPETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKDNETSLPSLERTPatEQPERpLQSEGNKPRPLLTDST 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819749297  78 ESTHPTIHTQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKMKAGMVNFDIHPEAVSLSQSNFIMDNAYFCEADAKKCI 157
Cdd:pfam12772 152 ESTSPLVQTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCI 231

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1819749297 158 TAGPHLEVQSRAEPSFNQEDIYITTESLTTT 188
Cdd:pfam12772 232 AVTPPSEAEPGVGYQTNNEDPYITTESLTTT 262
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 1-188 2.37e-85

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: 253.65  E-value: 2.37e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819749297   1 TSCYEPDILETDFHASDTCDGTSELEQPQRLKEEAVLLCLEKKQNHSLSNDTLSSI--PQPSV-TLAQESKSRPLVIGGT 77
Cdd:pfam12772  72 ASCYEPDIPETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKDNETSLPSLERTPatEQPERpLQSEGNKPRPLLTDST 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819749297  78 ESTHPTIHTQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKMKAGMVNFDIHPEAVSLSQSNFIMDNAYFCEADAKKCI 157
Cdd:pfam12772 152 ESTSPLVQTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCI 231

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1819749297 158 TAGPHLEVQSRAEPSFNQEDIYITTESLTTT 188
Cdd:pfam12772 232 AVTPPSEAEPGVGYQTNNEDPYITTESLTTT 262
 
Name Accession Description Interval E-value
GHBP pfam12772
Growth hormone receptor binding; Growth hormone receptor binding protein is produced either by ...
 1-188 2.37e-85

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: 253.65  E-value: 2.37e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819749297   1 TSCYEPDILETDFHASDTCDGTSELEQPQRLKEEAVLLCLEKKQNHSLSNDTLSSI--PQPSV-TLAQESKSRPLVIGGT 77
Cdd:pfam12772  72 ASCYEPDIPETDFSASDTCDGTSDIAQSKKLEKEADLLCLQPKDNETSLPSLERTPatEQPERpLQSEGNKPRPLLTDST 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819749297  78 ESTHPTIHTQLSNPSSLANIDFYAQVSDITPAGSVVLSPGQKMKAGMVNFDIHPEAVSLSQSNFIMDNAYFCEADAKKCI 157
Cdd:pfam12772 152 ESTSPLVQTQLSNPQSLANTDFYAQVSDITPAGGVVLSPGQKLKAGESQSASERETQTKGKQNFVVDSAYFCEADVKKCI 231

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1819749297 158 TAGPHLEVQSRAEPSFNQEDIYITTESLTTT 188
Cdd:pfam12772 232 AVTPPSEAEPGVGYQTNNEDPYITTESLTTT 262
 
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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