SOMA_BOVIN
ID SOMA_BOVIN Reviewed; 217 AA.
AC P01246; A4GX96; Q28117; Q3LS73;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=GH1; Synonyms=GH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6893197; DOI=10.1016/s0021-9258(19)43855-6;
RA Miller W.L., Martial J.A., Baxter J.D.;
RT "Molecular cloning of DNA complementary to bovine growth hormone mRNA.";
RL J. Biol. Chem. 255:7521-7524(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6296767; DOI=10.1093/nar/10.22.7197;
RA Woychik R.P., Camper S.A., Lyons R.H., Horowitz S., Goodwin E.C.,
RA Rottman F.M.;
RT "Cloning and nucleotide sequencing of the bovine growth hormone gene.";
RL Nucleic Acids Res. 10:7197-7210(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6303731; DOI=10.1089/dna.1.1983.2.37;
RA Seeburg P.H., Sias S., Adelman J., de Boer H.A., Hayflick J., Jhurani P.,
RA Goeddel D.V., Heyneker H.L.;
RT "Efficient bacterial expression of bovine and porcine growth hormones.";
RL DNA 2:37-45(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=6357899; DOI=10.1016/0303-7207(83)90058-8;
RA Gordon D.F., Quick D.P., Erwin C.R., Donelson J.E., Maurer R.A.;
RT "Nucleotide sequence of the bovine growth hormone chromosomal gene.";
RL Mol. Cell. Endocrinol. 33:81-95(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rubtsov P.M., Chernov B.K., Gorbulev V.G., Parsadanyan A.S.,
RA Sverdlova P.S., Chupeeva V.V., Golova Y.B., Batchikova N.V.,
RA Zhvirblis G.S., Skryabin K.G., Baev A.A.;
RT "Genetic engineering of peptide hormones.";
RL Mol. Biol. (Mosk.) 19:226-235(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Nelore; TISSUE=Pituitary;
RA Mauro S.M.Z., Ferro M.I.T., Macari M., Ferro J.A.;
RT "The complete sequence of a cDNA encoding the bovine growth hormone.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Javadmanesh A., Nassiry M., Eftekhari Shahrudi F., Basami M.;
RT "Cloning the cDNA of bovine growth hormone gene in E. coli.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Shiwal, and Tharri malir; TISSUE=Pituitary;
RA Mahmood S.F., Awan I.N., Khan M.J., Shahzad M.I., Khanum A.;
RT "Cloning and sequencing of the growth hormone gene of Pakistani cow breeds
RT (Bos taurus).";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 27-217, AND VARIANT VAL-153.
RX PubMed=4584625; DOI=10.1016/0014-5793(73)80566-6;
RA Wallis M.;
RT "The primary structure of bovine growth hormone.";
RL FEBS Lett. 35:11-14(1973).
RN [10]
RP PROTEIN SEQUENCE OF 27-217.
RX PubMed=4580883; DOI=10.1111/j.1432-1033.1973.tb02971.x;
RA Santome J.A., Dellacha J.M., Paladini A.C., Pena C., Biscoglio M.J.,
RA Daurat S.T., Poskus E., Wolfenstein C.E.M.;
RT "Primary structure of bovine growth hormone.";
RL Eur. J. Biochem. 37:164-170(1973).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-49.
RX PubMed=3899556; DOI=10.1089/dna.1985.4.273;
RA George H.J., L'Italien J.J., Pilacinski W.P., Glassman D.L., Krzyzek R.A.;
RT "High-level expression in Escherichia coli of biologically active bovine
RT growth hormone.";
RL DNA 4:273-281(1985).
RN [12]
RP PROTEIN SEQUENCE OF 91-96 AND 104-121.
RX PubMed=4856718; DOI=10.1016/s0006-291x(74)80330-x;
RA Graf L., Li C.H.;
RT "On the primary structure of pituitary bovine growth hormone.";
RL Biochem. Biophys. Res. Commun. 56:168-176(1974).
RN [13]
RP EVIDENCE FOR TWO ALLELIC CHAINS.
RX PubMed=5579941; DOI=10.1016/s0006-291x(71)80105-5;
RA Seavey B.K., Singh R.N.P., Lewis U.J., Geschwind I.I.;
RT "Bovine growth hormone: evidence for two allelic forms.";
RL Biochem. Biophys. Res. Commun. 43:189-195(1971).
RN [14]
RP CHARACTERIZATION.
RX PubMed=1123321; DOI=10.1016/s0021-9258(19)41630-x;
RA Yamasaki N., Shimanaka J., Sonenburg M.;
RT "Studies on the common active site of growth hormone. Revision of the amino
RT acid sequence of an active fragment of bovine growth hormone.";
RL J. Biol. Chem. 250:2510-2514(1975).
RN [15]
RP 3D-STRUCTURE MODELING.
RX PubMed=2021631; DOI=10.1021/bi00232a004;
RA Carlacci L., Chou K.-C., Maggiora G.M.;
RT "A heuristic approach to predicting the tertiary structure of bovine
RT somatotropin.";
RL Biochemistry 30:4389-4398(1991).
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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000305}.
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DR EMBL; V00111; CAA23445.1; -; mRNA.
DR EMBL; J00008; AAA30542.1; -; Genomic_DNA.
DR EMBL; M27325; AAA30543.1; -; mRNA.
DR EMBL; M57764; AAA30544.1; -; Genomic_DNA.
DR EMBL; M23813; AAA30556.1; -; mRNA.
DR EMBL; AF034386; AAB92549.1; -; mRNA.
DR EMBL; DQ184480; ABA26924.1; -; mRNA.
DR EMBL; EF451795; ABO21739.1; -; mRNA.
DR EMBL; EF451796; ABO21740.1; -; mRNA.
DR EMBL; M11558; AAA30545.1; -; mRNA.
DR PIR; I45900; STBO.
DR RefSeq; NP_851339.1; NM_180996.1.
DR AlphaFoldDB; P01246; -.
DR BMRB; P01246; -.
DR SMR; P01246; -.
DR STRING; 9913.ENSBTAP00000022885; -.
DR MetOSite; P01246; -.
DR PaxDb; P01246; -.
DR PRIDE; P01246; -.
DR GeneID; 280804; -.
DR KEGG; bta:280804; -.
DR CTD; 2688; -.
DR eggNOG; ENOG502R5GJ; Eukaryota.
DR HOGENOM; CLU_088274_2_1_1; -.
DR InParanoid; P01246; -.
DR OrthoDB; 1190548at2759; -.
DR TreeFam; TF332592; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IDA:AgBase.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IDA:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:AgBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:AgBase.
DR GO; GO:1901984; P:negative regulation of protein acetylation; IMP:AgBase.
DR GO; GO:2000844; P:negative regulation of testosterone secretion; IMP:AgBase.
DR GO; GO:0035811; P:negative regulation of urine volume; IDA:AgBase.
DR GO; GO:2000860; P:positive regulation of aldosterone secretion; IDA:AgBase.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IDA:GO_Central.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:AgBase.
DR GO; GO:1900482; P:positive regulation of diacylglycerol biosynthetic process; IDA:GO_Central.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:GO_Central.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IDA:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR GO; GO:0045927; P:positive regulation of growth; IBA:GO_Central.
DR GO; GO:1903489; P:positive regulation of lactation; IDA:AgBase.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IDA:AgBase.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:AgBase.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:AgBase.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:AgBase.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IDA:GO_Central.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:2000833; P:positive regulation of steroid hormone secretion; IMP:AgBase.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:AgBase.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:GO_Central.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IDA:AgBase.
DR GO; GO:0033143; P:regulation of intracellular steroid hormone receptor signaling pathway; IDA:MGI.
DR GO; GO:0070294; P:renal sodium ion absorption; IDA:AgBase.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
DR GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
DR GO; GO:0031667; P:response to nutrient levels; IDA: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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hormone; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:4580883,
FT ECO:0000269|PubMed:4584625"
FT CHAIN 27..217
FT /note="Somatotropin"
FT /id="PRO_0000032974"
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:0000269|PubMed:4584625"
FT DISULFID 207..215
FT /evidence="ECO:0000269|PubMed:4584625"
FT VARIANT 153
FT /note="L -> V (in 30% of the molecules)"
FT /evidence="ECO:0000269|PubMed:4584625"
FT CONFLICT 95
FT /note="Q -> E (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..120
FT /note="QSWLGPLQFLS -> SQWLQPGFL (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="D -> N (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
