ID   SOMA_PIG                Reviewed;         216 AA.
AC   P01248; Q28958; Q29045;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=GH1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3666458; DOI=10.1016/0378-1119(87)90294-0;
RA   Vize P.D., Wells J.R.E.;
RT   "Isolation and characterization of the porcine growth hormone gene.";
RL   Gene 55:339-344(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2182128; DOI=10.1016/0167-4781(90)90069-e;
RA   Kato Y., Shimokawa N., Kato T., Hirai T., Yoshihama K., Kawai H.,
RA   Hattori M.A., Ezashi T., Shimogori Y., Wakabayashi K.;
RT   "Porcine growth hormone: molecular cloning of cDNA and expression in
RT   bacterial and mammalian cells.";
RL   Biochim. Biophys. Acta 1048:290-293(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pituitary;
RX   PubMed=2491309;
RA   Qi S.Z., Wang X.Z., Zhou S.W., Jia F., Wang H.Y., Xia L.I., Li J.;
RT   "Sequencing of porcine growth hormone cDNA.";
RL   Chin. J. Biotechnol. 5:27-32(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 27-30 AND 149-216, AND DISULFIDE BOND.
RX   PubMed=4918150; DOI=10.1016/s0021-9258(18)63011-x;
RA   Mills J.B., Howard S.C., Scapa S., Wilhelmi A.E.;
RT   "Cyanogen bromide cleavage and partial amino acid sequence of porcine
RT   growth hormone.";
RL   J. Biol. Chem. 245:3407-3415(1970).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-216.
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   [6]
RP   NUCLEOTIDE SEQUENCE OF 97-158.
RX   PubMed=1343826;
RA   Yang Q., Zhu B., Zhou S., Qi S.;
RT   "Cloning and partial sequencing of the porcine growth hormone (pGH) gene
RT   from pituitary gland.";
RL   Chin. J. Biotechnol. 8:227-233(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 5-57.
RA   Jiang Z.H., Rottmann O.J., Pirchner F.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA73478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X53325; CAA37411.1; -; mRNA.
DR   EMBL; M17704; AAA31044.1; -; Genomic_DNA.
DR   EMBL; U19788; AAA73478.1; ALT_INIT; mRNA.
DR   EMBL; M27326; AAA31045.1; -; mRNA.
DR   EMBL; S72386; AAB29947.2; -; Genomic_DNA.
DR   EMBL; U73464; AAB17619.1; -; Genomic_DNA.
DR   PIR; JW0015; STPG.
DR   AlphaFoldDB; P01248; -.
DR   SMR; P01248; -.
DR   STRING; 9823.ENSSSCP00000018314; -.
DR   PaxDb; P01248; -.
DR   Ensembl; ENSSSCT00035001704; ENSSSCP00035000543; ENSSSCG00035001304.
DR   Ensembl; ENSSSCT00055043259; ENSSSCP00055034420; ENSSSCG00055021962.
DR   eggNOG; ENOG502R5GJ; Eukaryota.
DR   InParanoid; P01248; -.
DR   OMA; QTAFCFS; -.
DR   Reactome; R-SSC-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   Reactome; R-SSC-982772; Growth hormone receptor signaling.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
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:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0045927; P:positive regulation of growth; IBA:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR   GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
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:4918150"
FT   CHAIN           27..216
FT                   /note="Somatotropin"
FT                   /id="PRO_0000032995"
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:0000269|PubMed:4918150"
FT   CONFLICT        9
FT                   /note="A -> V (in Ref. 5; AAA31045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        22
FT                   /note="R -> Q (in Ref. 5; AAA31045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78
FT                   /note="C -> F (in Ref. 3; AAA73478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="Q -> T (in Ref. 3; AAA73478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="H -> N (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203
FT                   /note="V -> L (in Ref. 3; AAA73478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="C -> S (in Ref. 3; AAA73478)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  24429 MW;  0216931D6BE76D14 CRC64;
     MAAGPRTSAL LAFALLCLPW TREVGAFPAM PLSSLFANAV LRAQHLHQLA ADTYKEFERA
     YIPEGQRYSI QNAQAAFCFS ETIPAPTGKD EAQQRSDVEL LRFSLLLIQS WLGPVQFLSR
     VFTNSLVFGT SDRVYEKLKD LEEGIQALMR ELEDGSPRAG QILKQTYDKF DTNLRSDDAL
     LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF