SOMA_CEREL
ID SOMA_CEREL Reviewed; 217 AA.
AC P56437;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=GH1;
OS Cervus elaphus (Red deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=9860;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Tongue;
RX PubMed=9460647; DOI=10.1677/jme.0.0190259;
RA Lioupis A., Wallis O.C., Wallis M.;
RT "Cloning and characterisation of the gene encoding red deer (Cervus
RT elaphus) growth hormone: implications for the molecular evolution of growth
RT hormone in artiodactyls.";
RL J. Mol. Endocrinol. 19:259-266(1997).
CC -!- FUNCTION: Plays an important role in growth control. Its major role in
CC stimulating body growth is to stimulate the liver and other tissues to
CC secrete IGF-1. It stimulates both the differentiation and proliferation
CC of myoblasts. It also stimulates amino acid uptake and protein
CC synthesis in muscle and other tissues (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000305}.
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DR EMBL; Y12578; CAA73158.1; -; Genomic_DNA.
DR AlphaFoldDB; P56437; -.
DR BMRB; P56437; -.
DR SMR; P56437; -.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005131; F:growth hormone receptor binding; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030073; P:insulin secretion; ISS:AgBase.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR034975; Somatotropin.
DR InterPro; IPR001400; Somatotropin/Prolactin.
DR InterPro; IPR018116; Somatotropin_CS.
DR PANTHER; PTHR11417; PTHR11417; 1.
DR PANTHER; PTHR11417:SF2; PTHR11417:SF2; 1.
DR Pfam; PF00103; Hormone_1; 1.
DR PRINTS; PR00836; SOMATOTROPIN.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hormone; Metal-binding; Phosphoprotein; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..217
FT /note="Somatotropin"
FT /id="PRO_0000032981"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01241"
FT DISULFID 79..190
FT /evidence="ECO:0000250"
FT DISULFID 207..215
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 24558 MW; 6F22D5241468B7AD CRC64;
MMAAGPRASL LLAFALLCLP WTQEVGAFPA MSLSGLFANA VLRAQHLHQL AADTFKEFER
TYIPEGQRYS IQNTQVAFCF SETIPAPTGK NEAQQKSDLE LLRISLLLIQ SWLGPLQFLS
RVFTNSLVFG TSDRVYEKLK DLEEGILALM RELEDGTPRA GQILKQTYDK FDTNMRSDDA
LLKNYGLLSC FRKDLHKTET YLRVMKCRRF GEASCAF