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SOMA_MOUSE
ID   SOMA_MOUSE              Reviewed;         216 AA.
AC   P06880; Q544X1;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=Gh1; Synonyms=Gh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2991252; DOI=10.1016/s0021-9258(17)39273-6;
RA   Linzer D.I.H., Talamantes F.;
RT   "Nucleotide sequence of mouse prolactin and growth hormone mRNAs and
RT   expression of these mRNAs during pregnancy.";
RL   J. Biol. Chem. 260:9574-9579(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FZTDU; TISSUE=Liver;
RX   PubMed=8647448; DOI=10.1016/0378-1119(95)00815-2;
RA   Das P., Meyer L., Seyfert H.-M., Brockmann G., Schwerin M.;
RT   "Structure of the growth hormone-encoding gene and its promoter in mice.";
RL   Gene 169:209-213(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; X02891; CAA26650.1; -; mRNA.
DR   EMBL; Z46663; CAA86658.1; -; Genomic_DNA.
DR   EMBL; AK019952; BAB31931.1; -; mRNA.
DR   EMBL; AK019954; BAB31932.1; -; mRNA.
DR   EMBL; AK019956; BAB31933.1; -; mRNA.
DR   EMBL; AK019959; BAB31935.1; -; mRNA.
DR   EMBL; AK019961; BAB31937.1; -; mRNA.
DR   EMBL; AK030715; BAC27096.1; -; mRNA.
DR   EMBL; BC061157; AAH61157.1; -; mRNA.
DR   CCDS; CCDS25554.1; -.
DR   PIR; B23911; STMS.
DR   RefSeq; NP_032143.1; NM_008117.3.
DR   AlphaFoldDB; P06880; -.
DR   SMR; P06880; -.
DR   BioGRID; 199914; 2.
DR   STRING; 10090.ENSMUSP00000099360; -.
DR   iPTMnet; P06880; -.
DR   PhosphoSitePlus; P06880; -.
DR   MaxQB; P06880; -.
DR   PaxDb; P06880; -.
DR   PeptideAtlas; P06880; -.
DR   PRIDE; P06880; -.
DR   ProteomicsDB; 261603; -.
DR   DNASU; 14599; -.
DR   Ensembl; ENSMUST00000103071; ENSMUSP00000099360; ENSMUSG00000020713.
DR   GeneID; 14599; -.
DR   KEGG; mmu:14599; -.
DR   UCSC; uc007lys.2; mouse.
DR   CTD; 14599; -.
DR   MGI; MGI:95707; Gh.
DR   VEuPathDB; HostDB:ENSMUSG00000020713; -.
DR   eggNOG; ENOG502R5GJ; Eukaryota.
DR   GeneTree; ENSGT00950000182818; -.
DR   HOGENOM; CLU_088274_2_1_1; -.
DR   InParanoid; P06880; -.
DR   OMA; QTAFCFS; -.
DR   OrthoDB; 1190548at2759; -.
DR   PhylomeDB; P06880; -.
DR   TreeFam; TF332592; -.
DR   Reactome; R-MMU-1170546; Prolactin receptor signaling.
DR   Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   Reactome; R-MMU-982772; Growth hormone receptor signaling.
DR   BioGRID-ORCS; 14599; 7 hits in 73 CRISPR screens.
DR   ChiTaRS; Gh; mouse.
DR   PRO; PR:P06880; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P06880; protein.
DR   Bgee; ENSMUSG00000020713; Expressed in pituitary gland and 68 other tissues.
DR   ExpressionAtlas; P06880; baseline and differential.
DR   Genevisible; P06880; MM.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0070195; C:growth hormone receptor complex; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR   GO; GO:0005131; F:growth hormone receptor binding; IPI:MGI.
DR   GO; GO:0005179; F:hormone activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005148; F:prolactin receptor binding; ISO:MGI.
DR   GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:Ensembl.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
DR   GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0060396; P:growth hormone receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0048286; P:lung alveolus development; ISO:MGI.
DR   GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR   GO; GO:0007405; P:neuroblast proliferation; ISO:MGI.
DR   GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:MGI.
DR   GO; GO:0045927; P:positive regulation of growth; ISO:MGI.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:MGI.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; ISO:MGI.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR   GO; GO:0033143; P:regulation of intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR   GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IDA:MGI.
DR   GO; GO:0009416; P:response to light stimulus; ISO:MGI.
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   2: Evidence at transcript 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_0000032992"
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:0000250"
SQ   SEQUENCE   216 AA;  24716 MW;  98666A3AE25D65FC CRC64;
     MATDSRTSWL LTVSLLCLLW PQEASAFPAM PLSSLFSNAV LRAQHLHQLA ADTYKEFERA
     YIPEGQRYSI QNAQAAFCFS ETIPAPTGKE EAQQRTDMEL LRFSLLLIQS WLGPVQFLSR
     IFTNSLMFGT SDRVYEKLKD LEEGIQALMQ ELEDGSPRVG QILKQTYDKF DANMRSDDAL
     LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF
 
 
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