ID   SOMA_GIRCA              Reviewed;         217 AA.
AC   Q7YQD2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-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;
GN   and
GN   Name=GH2;
OS   Giraffa camelopardalis (Giraffe).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Giraffidae;
OC   Giraffa.
OX   NCBI_TaxID=9894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15461431; DOI=10.1007/s00239-004-2595-x;
RA   Maniou Z., Wallis O.C., Wallis M.;
RT   "Episodic molecular evolution of pituitary growth hormone in
RT   Cetartiodactyla.";
RL   J. Mol. Evol. 58:743-753(2004).
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; AJ575420; CAE01392.1; -; Genomic_DNA.
DR   EMBL; AJ575421; CAE01393.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YQD2; -.
DR   SMR; Q7YQD2; -.
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_0000032985"
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;  24576 MW;  C5166A0D52EB6BDE CRC64;
     MMAAGPRTSL LLAFALLCLP WTQMVGAFPA MSLSGLFANA VLRAQHLHQL AADTFKEFER
     TYIPEGQRYS IQNTQVAFCF SETIPAPTGK NEAQQKSDLE LLRISLLLIQ SWLGPLQFLS
     RVFSNSLVFG TSDRVYEKLK DLEEGILALM RELEDGTPRA GQILKQTYDK FDTNMRSDDA
     LLKNYGLLSC FRKDLHKTET YLRVMKCRRF GEASCAF