ID   SOMA_CAMDR              Reviewed;         216 AA.
AC   Q7YRR6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=GH1; Synonyms=GH;
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
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; AJ575419; CAE01391.1; -; Genomic_DNA.
DR   RefSeq; XP_010979998.1; XM_010981696.1.
DR   AlphaFoldDB; Q7YRR6; -.
DR   SMR; Q7YRR6; -.
DR   STRING; 9838.ENSCDRP00005030867; -.
DR   Ensembl; ENSCDRT00005033980; ENSCDRP00005030867; ENSCDRG00005021034.
DR   GeneID; 105090400; -.
DR   KEGG; cdk:105090400; -.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR   GO; GO:0005131; F:growth hormone receptor binding; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IEA:Ensembl.
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..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..216
FT                   /note="Somatotropin"
FT                   /id="PRO_0000032977"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01241"
FT   DISULFID        78..189
FT                   /evidence="ECO:0000250"
FT   DISULFID        206..214
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24485 MW;  5810D2C02C2DACF5 CRC64;
     MAAGPRTSVL LAFTLLCLPW PQEAGAFPAM PLSSLFANAV LRAQHLHQLA ADTYKEFERT
     YIPEGQRYSI QNAQAAFCFS ETIPAPTGKD EAQQRSDVEL LRFSLLLIQS WLGPVQFLSR
     VFTNSLVFGT SDRVYEKLKD LEEGIQALMR ELEDGSPRAG QILRQTYDKF DTNLRSDDAL
     LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF