ID   SOMA_BOSMU              Reviewed;         217 AA.
AC   Q864S7;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=GH1; Synonyms=GH;
OS   Bos mutus grunniens (Wild yak) (Bos grunniens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Ou J.T., Zhong J.C., Chen Z.H., Guo C.H., Zhao Y.X.;
RT   "Cloning, sequencing, and polymorphism analysis on entire growth hormone
RT   gene of Yak.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
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; AY271297; AAP06256.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q864S7; -.
DR   SMR; Q864S7; -.
DR   Proteomes; UP000694520; Unplaced.
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   GO; GO:0009893; P:positive regulation of metabolic process; IEA:UniProt.
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; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..217
FT                   /note="Somatotropin"
FT                   /id="PRO_0000032973"
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;  24486 MW;  ADFB98419A52EDA9 CRC64;
     MMAAGPRTSL LLAFALLCLP WTQVVGAFPA MSLSGLFANA VLRAQHLHQL AADTFKEFER
     TYIPGGQRYS IQNTQVAFCF SETIPAPTGK NEAQQKSDLE LLRISLLLIQ SWLGPLQFLS
     RVFTNSLVFG TSDRVYEKLK DLEEGILALM RELEDGTPRA GQILKQTYDK FDTNMRSDDA
     LLKNYGLLSC FRKDLHKTET YLRVMKCRRF GEASCAF