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Somatotropin (Growth hormone)

 SOMA_BOVIN              Reviewed;         217 AA.
P01246; A4GX96; Q28117; Q3LS73;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 142.
RecName: Full=Somatotropin;
AltName: Full=Growth hormone;
Flags: Precursor;
Name=GH1; Synonyms=GH;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6893197;
Miller W.L., Martial J.A., Baxter J.D.;
"Molecular cloning of DNA complementary to bovine growth hormone
mRNA.";
J. Biol. Chem. 255:7521-7524(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6296767; DOI=10.1093/nar/10.22.7197;
Woychik R.P., Camper S.A., Lyons R.H., Horowitz S., Goodwin E.C.,
Rottman F.M.;
"Cloning and nucleotide sequencing of the bovine growth hormone
gene.";
Nucleic Acids Res. 10:7197-7210(1982).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6303731; DOI=10.1089/dna.1.1983.2.37;
Seeburg P.H., Sias S., Adelman J., de Boer H.A., Hayflick J.,
Jhurani P., Goeddel D.V., Heyneker H.L.;
"Efficient bacterial expression of bovine and porcine growth
hormones.";
DNA 2:37-45(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=6357899; DOI=10.1016/0303-7207(83)90058-8;
Gordon D.F., Quick D.P., Erwin C.R., Donelson J.E., Maurer R.A.;
"Nucleotide sequence of the bovine growth hormone chromosomal gene.";
Mol. Cell. Endocrinol. 33:81-95(1983).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,
Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,
Zhvirblis G.S., Skryabin K.G., Baev A.A.;
"Genetic engineering of peptide hormones.";
Mol. Biol. (Mosk.) 19:226-235(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Nelore; TISSUE=Pituitary;
Mauro S.M.Z., Ferro M.I.T., Macari M., Ferro J.A.;
"The complete sequence of a cDNA encoding the bovine growth hormone.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
Javadmanesh A., Nassiry M., Eftekhari Shahrudi F., Basami M.;
"Cloning the cDNA of bovine growth hormone gene in E. coli.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Shiwal, and Tharri malir; TISSUE=Pituitary;
Mahmood S.F., Awan I.N., Khan M.J., Shahzad M.I., Khanum A.;
"Cloning and sequencing of the growth hormone gene of Pakistani cow
breeds (Bos taurus).";
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 27-217, AND VARIANT VAL-153.
PubMed=4584625; DOI=10.1016/0014-5793(73)80566-6;
Wallis M.;
"The primary structure of bovine growth hormone.";
FEBS Lett. 35:11-14(1973).
[10]
PROTEIN SEQUENCE OF 27-217.
PubMed=4580883; DOI=10.1111/j.1432-1033.1973.tb02971.x;
Santome J.A., Dellacha J.M., Paladini A.C., Pena C., Biscoglio M.J.,
Daurat S.T., Poskus E., Wolfenstein C.E.M.;
"Primary structure of bovine growth hormone.";
Eur. J. Biochem. 37:164-170(1973).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 27-49.
PubMed=3899556;
George H.J., L'Italien J.J., Pilacinski W.P., Glassman D.L.,
Krzyzek R.A.;
"High-level expression in Escherichia coli of biologically active
bovine growth hormone.";
DNA 4:273-281(1985).
[12]
PROTEIN SEQUENCE OF 91-96 AND 104-121.
PubMed=4856718; DOI=10.1016/S0006-291X(74)80330-X;
Graf L., Li C.H.;
"On the primary structure of pituitary bovine growth hormone.";
Biochem. Biophys. Res. Commun. 56:168-176(1974).
[13]
EVIDENCE FOR TWO ALLELIC CHAINS.
PubMed=5579941; DOI=10.1016/S0006-291X(71)80105-5;
Seavey B.K., Singh R.N.P., Lewis U.J., Geschwind I.I.;
"Bovine growth hormone: evidence for two allelic forms.";
Biochem. Biophys. Res. Commun. 43:189-195(1971).
[14]
CHARACTERIZATION.
PubMed=1123321;
Yamasaki N., Shimanaka J., Sonenburg M.;
"Studies on the common active site of growth hormone. Revision of the
amino acid sequence of an active fragment of bovine growth hormone.";
J. Biol. Chem. 250:2510-2514(1975).
[15]
3D-STRUCTURE MODELING.
PubMed=2021631; DOI=10.1021/bi00232a004;
Carlacci L., Chou K.-C., Maggiora G.M.;
"A heuristic approach to predicting the tertiary structure of bovine
somatotropin.";
Biochemistry 30:4389-4398(1991).
-!- 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; V00111; CAA23445.1; -; mRNA.
EMBL; J00008; AAA30542.1; -; Genomic_DNA.
EMBL; M27325; AAA30543.1; -; mRNA.
EMBL; M57764; AAA30544.1; -; Genomic_DNA.
EMBL; M23813; AAA30556.1; -; mRNA.
EMBL; AF034386; AAB92549.1; -; mRNA.
EMBL; DQ184480; ABA26924.1; -; mRNA.
EMBL; EF451795; ABO21739.1; -; mRNA.
EMBL; EF451796; ABO21740.1; -; mRNA.
EMBL; M11558; AAA30545.1; -; mRNA.
PIR; I45900; STBO.
RefSeq; NP_851339.1; NM_180996.1.
UniGene; Bt.28019; -.
PDB; 1BST; Model; -; A=27-217.
PDBsum; 1BST; -.
ProteinModelPortal; P01246; -.
SMR; P01246; -.
STRING; 9913.ENSBTAP00000022885; -.
PaxDb; P01246; -.
PRIDE; P01246; -.
Ensembl; ENSBTAT00000022885; ENSBTAP00000022885; ENSBTAG00000017220.
GeneID; 280804; -.
KEGG; bta:280804; -.
CTD; 2688; -.
eggNOG; ENOG410IFR6; Eukaryota.
eggNOG; ENOG4111HU8; LUCA.
GeneTree; ENSGT00730000111012; -.
HOGENOM; HOG000068443; -.
HOVERGEN; HBG011318; -.
InParanoid; P01246; -.
KO; K05438; -.
OMA; TYLRVMK; -.
OrthoDB; EOG091G0KPU; -.
TreeFam; TF332592; -.
Reactome; R-BTA-1170546; Prolactin receptor signaling.
Reactome; R-BTA-422085; Synthesis, secretion, and deacylation of Ghrelin.
Reactome; R-BTA-982772; Growth hormone receptor signaling.
Proteomes; UP000009136; Chromosome 19.
Bgee; ENSBTAG00000017220; -.
ExpressionAtlas; P01246; baseline.
GO; GO:0005615; C:extracellular space; IDA: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; IDA:MGI.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IDA:AgBase.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; IDA:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:AgBase.
GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase.
GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:AgBase.
GO; GO:1901984; P:negative regulation of protein acetylation; IMP:AgBase.
GO; GO:2000844; P:negative regulation of testosterone secretion; IMP:AgBase.
GO; GO:0035811; P:negative regulation of urine volume; IDA:AgBase.
GO; GO:2000860; P:positive regulation of aldosterone secretion; IDA:AgBase.
GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IDA:AgBase.
GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:AgBase.
GO; GO:1900482; P:positive regulation of diacylglycerol biosynthetic process; IDA:AgBase.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:AgBase.
GO; GO:2000253; P:positive regulation of feeding behavior; IDA:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
GO; GO:1903489; P:positive regulation of lactation; IDA:AgBase.
GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:AgBase.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:AgBase.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:AgBase.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:AgBase.
GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IDA:AgBase.
GO; GO:2000833; P:positive regulation of steroid hormone secretion; IMP:AgBase.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:AgBase.
GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:AgBase.
GO; GO:0009306; P:protein secretion; IDA:AgBase.
GO; GO:0033143; P:regulation of intracellular steroid hormone receptor signaling pathway; IDA:MGI.
GO; GO:0070294; P:renal sodium ion absorption; IDA:AgBase.
GO; GO:0032094; P:response to food; IDA:AgBase.
GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
GO; GO:0031667; P:response to nutrient levels; IDA: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:SF53; PTHR11417:SF53; 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;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Hormone; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 26 {ECO:0000269|PubMed:4580883,
ECO:0000269|PubMed:4584625}.
CHAIN 27 217 Somatotropin.
/FTId=PRO_0000032974.
METAL 46 46 Zinc. {ECO:0000250}.
METAL 199 199 Zinc. {ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P01241}.
DISULFID 79 190 {ECO:0000269|PubMed:4584625}.
DISULFID 207 215 {ECO:0000269|PubMed:4584625}.
VARIANT 153 153 L -> V (in 30% of the molecules).
{ECO:0000269|PubMed:4584625}.
CONFLICT 95 95 Q -> E (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 110 120 QSWLGPLQFLS -> SQWLQPGFL (in Ref. 10; AA
sequence). {ECO:0000305}.
CONFLICT 194 194 D -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
SEQUENCE 217 AA; 24558 MW; 99ED8D01B852EF89 CRC64;
MMAAGPRTSL LLAFALLCLP WTQVVGAFPA MSLSGLFANA VLRAQHLHQL AADTFKEFER
TYIPEGQRYS IQNTQVAFCF SETIPAPTGK NEAQQKSDLE LLRISLLLIQ SWLGPLQFLS
RVFTNSLVFG TSDRVYEKLK DLEEGILALM RELEDGTPRA GQILKQTYDK FDTNMRSDDA
LLKNYGLLSC FRKDLHKTET YLRVMKCRRF GEASCAF


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