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Somatotropin (Growth hormone)

 SOMA_SHEEP              Reviewed;         217 AA.
P67930; P01247; P07289; Q29404;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
25-OCT-2017, entry version 69.
RecName: Full=Somatotropin;
AltName: Full=Growth hormone;
Flags: Precursor;
Name=GH1;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3453044;
Byrne C.R., Wilson B.W., Ward K.A.;
"The isolation and characterisation of the ovine growth hormone
gene.";
Aust. J. Biol. Sci. 40:459-468(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3174441; DOI=10.1093/nar/16.18.9046;
Orian J.M., O'Mahoney J.V., Brandon M.R.;
"Cloning and sequencing of the ovine growth hormone gene.";
Nucleic Acids Res. 16:9046-9046(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2660907; DOI=10.1016/0167-4781(80)90016-0;
Warwick J.M., Wallis O.C., Wallis M.;
"Cloning, sequence and expression in Escherichia coli of cDNA for
ovine pregrowth hormone.";
Biochim. Biophys. Acta 1008:247-250(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
PubMed=1459643;
Guron C., Rao K.B., Jain S.K., Totey S.M., Talwar G.P.;
"Cloning and nucleotide sequencing of sheep growth hormone cDNA.";
Indian J. Exp. Biol. 30:659-663(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Awassi;
PubMed=9321473; DOI=10.1007/s003359900563;
Ofir R., Gootwine E.;
"Ovine growth hormone gene duplication -- structural and evolutionary
implications.";
Mamm. Genome 8:770-772(1997).
[6]
PROTEIN SEQUENCE OF 28-217.
PubMed=4736985; DOI=10.1016/0003-9861(73)90299-3;
Li C.H., Gordon D., Knorr J.;
"The primary structure of sheep pituitary growth hormone.";
Arch. Biochem. Biophys. 156:493-508(1973).
[7]
PROTEIN SEQUENCE OF 150-217.
PubMed=5062423; DOI=10.1016/S0006-291X(72)80091-3;
Bellair J.T.;
"Ovine growth hormone. Sequence of the C-terminal 68 amino acids.";
Biochem. Biophys. Res. Commun. 46:1128-1134(1972).
-!- FUNCTION: Plays an important role in growth control. Its major
role in stimulating body growth is to stimulate the liver and
other tissues to secrete IGF-1. It stimulates both the
differentiation and proliferation of myoblasts. It also stimulates
amino acid uptake and protein synthesis in muscle and other
tissues.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the somatotropin/prolactin family.
{ECO:0000305}.
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EMBL; M37310; AAA31527.1; -; Genomic_DNA.
EMBL; X12546; CAA31063.1; -; Genomic_DNA.
EMBL; X15976; CAA34098.1; -; mRNA.
EMBL; S50877; AAB24467.2; -; mRNA.
EMBL; AF002113; AAB63273.1; -; Genomic_DNA.
EMBL; AF002111; AAB63273.1; JOINED; Genomic_DNA.
EMBL; AF002112; AAB63273.1; JOINED; Genomic_DNA.
PIR; S02225; STSH.
RefSeq; NP_001009315.2; NM_001009315.3.
UniGene; Oar.641; -.
ProteinModelPortal; P67930; -.
Ensembl; ENSOART00000015172; ENSOARP00000014952; ENSOARG00000013932.
GeneID; 443329; -.
KEGG; oas:443329; -.
CTD; 14599; -.
GeneTree; ENSGT00730000111012; -.
HOVERGEN; HBG011318; -.
KO; K05438; -.
OMA; TYLRVMK; -.
OrthoDB; EOG091G0KPU; -.
Proteomes; UP000002356; Chromosome 11.
ExpressionAtlas; P67930; baseline.
GO; GO:0005615; C:extracellular space; ISS:AgBase.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0005131; F:growth hormone receptor binding; IEA:Ensembl.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0055074; P:calcium ion homeostasis; IMP:AgBase.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0042538; P:hyperosmotic salinity response; IMP:AgBase.
GO; GO:0030073; P:insulin secretion; ISS:AgBase.
GO; GO:0010960; P:magnesium ion homeostasis; IMP:AgBase.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:1903408; P:positive regulation of sodium:potassium-exchanging ATPase activity; IMP:AgBase.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:AgBase.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0055078; P:sodium ion homeostasis; IMP:AgBase.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR034975; Somatotropin.
InterPro; IPR001400; Somatotropin/Prolactin.
InterPro; IPR018116; Somatotropin_CS.
PANTHER; PTHR11417; PTHR11417; 1.
PANTHER; PTHR11417:SF2; PTHR11417:SF2; 1.
Pfam; PF00103; Hormone_1; 1.
PRINTS; PR00836; SOMATOTROPIN.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00266; SOMATOTROPIN_1; 1.
PROSITE; PS00338; SOMATOTROPIN_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond; Hormone;
Metal-binding; Phosphoprotein; Reference proteome; Secreted; Signal;
Zinc.
SIGNAL 1 27 {ECO:0000269|PubMed:4736985}.
CHAIN 28 217 Somatotropin.
/FTId=PRO_0000033000.
METAL 46 46 Zinc. {ECO:0000250}.
METAL 199 199 Zinc. {ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P01241}.
DISULFID 79 190
DISULFID 207 215
CONFLICT 89 89 G -> S (in Ref. 1; AAA31527).
{ECO:0000305}.
CONFLICT 125 125 N -> D (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 134 134 R -> L (in Ref. 1; AAA31527).
{ECO:0000305}.
CONFLICT 173 173 T -> R (in Ref. 4; AAB24467).
{ECO:0000305}.
SEQUENCE 217 AA; 24631 MW; 77EC37A102584429 CRC64;
MMAAGPRTSL LLAFTLLCLP WTQVVGAFPA MSLSGLFANA VLRAQHLHQL AADTFKEFER
TYIPEGQRYS IQNTQVAFCF SETIPAPTGK NEAQQKSDLE LLRISLLLIQ SWLGPLQFLS
RVFTNSLVFG TSDRVYEKLK DLEEGILALM RELEDVTPRA GQILKQTYDK FDTNMRSDDA
LLKNYGLLSC FRKDLHKTET YLRVMKCRRF GEASCAF


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