SOMA_RAT
ID SOMA_RAT Reviewed; 216 AA.
AC P01244;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=Gh1; Synonyms=Gh;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272224; DOI=10.1093/nar/9.9.2087;
RA Page G.S., Smith S., Goodman H.M.;
RT "DNA sequence of the rat growth hormone gene: location of the 5' terminus
RT of the growth hormone mRNA and identification of an internal transposon-
RT like element.";
RL Nucleic Acids Res. 9:2087-2104(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=339105; DOI=10.1038/270486a0;
RA Seeburg P.H., Shine J., Martial J.A., Baxter J.D., Goodman H.M.;
RT "Nucleotide sequence and amplification in bacteria of structural gene for
RT rat growth hormone.";
RL Nature 270:486-494(1977).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISULFIDE BONDS.
RC TISSUE=Liver;
RX PubMed=6946433; DOI=10.1073/pnas.78.8.4867;
RA Barta A., Richards R.I., Baxter J.D., Shine J.;
RT "Primary structure and evolution of rat growth hormone gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4867-4871(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8521139; DOI=10.1159/000096879;
RA Rohn W.M., Weigent D.A.;
RT "Cloning and nucleotide sequencing of rat lymphocyte growth hormone cDNA.";
RL Neuroimmunomodulation 2:108-114(1995).
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; V01238; CAA24548.1; -; Genomic_DNA.
DR EMBL; V01237; CAA24547.1; -; mRNA.
DR EMBL; V01239; CAA24549.1; -; Genomic_DNA.
DR EMBL; U62779; AAB04025.1; -; mRNA.
DR PIR; A93725; STRT.
DR RefSeq; NP_001030020.2; NM_001034848.2.
DR AlphaFoldDB; P01244; -.
DR SMR; P01244; -.
DR BioGRID; 246561; 1.
DR STRING; 10116.ENSRNOP00000015818; -.
DR PaxDb; P01244; -.
DR Ensembl; ENSRNOT00000015818; ENSRNOP00000015818; ENSRNOG00000011207.
DR GeneID; 24391; -.
DR KEGG; rno:24391; -.
DR UCSC; RGD:2686; rat.
DR CTD; 2688; -.
DR RGD; 2686; Gh1.
DR eggNOG; ENOG502R5GJ; Eukaryota.
DR GeneTree; ENSGT00950000182818; -.
DR HOGENOM; CLU_088274_2_1_1; -.
DR InParanoid; P01244; -.
DR OMA; QTAFCFS; -.
DR OrthoDB; 1190548at2759; -.
DR PhylomeDB; P01244; -.
DR TreeFam; TF332592; -.
DR Reactome; R-RNO-1170546; Prolactin receptor signaling.
DR Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Reactome; R-RNO-982772; Growth hormone receptor signaling.
DR PRO; PR:P01244; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011207; Expressed in quadriceps femoris and 2 other tissues.
DR ExpressionAtlas; P01244; baseline and differential.
DR Genevisible; P01244; RN.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0070195; C:growth hormone receptor complex; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; ISO:RGD.
DR GO; GO:0005131; F:growth hormone receptor binding; ISO:RGD.
DR GO; GO:0005179; F:hormone activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005148; F:prolactin receptor binding; ISO:RGD.
DR GO; GO:0048513; P:animal organ development; IEP:RGD.
DR GO; GO:0070977; P:bone maturation; ISO:RGD.
DR GO; GO:0071469; P:cellular response to alkaline pH; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; IMP:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
DR GO; GO:0007405; P:neuroblast proliferation; IDA:RGD.
DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; ISO:RGD.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:RGD.
DR GO; GO:0045927; P:positive regulation of growth; IMP:RGD.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IDA:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032094; P:response to food; ISO:RGD.
DR GO; GO:0009416; P:response to light stimulus; IDA:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
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 Disulfide bond; Hormone; Metal-binding; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..216
FT /note="Somatotropin"
FT /id="PRO_0000032998"
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:0000269|PubMed:6946433"
FT DISULFID 206..214
FT /evidence="ECO:0000269|PubMed:6946433"
FT CONFLICT 27
FT /note="F -> L (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24656 MW; CABF49DC0B2A226C CRC64;
MAADSQTPWL LTFSLLCLLW PQEAGAFPAM PLSSLFANAV LRAQHLHQLA ADTYKEFERA
YIPEGQRYSI QNAQAAFCFS ETIPAPTGKE EAQQRTDMEL LRFSLLLIQS WLGPVQFLSR
IFTNSLMFGT SDRVYEKLKD LEEGIQALMQ ELEDGSPRIG QILKQTYDKF DANMRSDDAL
LKNYGLLSCF KKDLHKAETY LRVMKCRRFA ESSCAF
