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Somatotropin (Growth hormone)

 SOMA_MOUSE              Reviewed;         216 AA.
P06880; Q544X1;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
12-SEP-2018, entry version 160.
RecName: Full=Somatotropin;
AltName: Full=Growth hormone;
Flags: Precursor;
Name=Gh1; Synonyms=Gh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2991252;
Linzer D.I.H., Talamantes F.;
"Nucleotide sequence of mouse prolactin and growth hormone mRNAs and
expression of these mRNAs during pregnancy.";
J. Biol. Chem. 260:9574-9579(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=FZTDU; TISSUE=Liver;
PubMed=8647448; DOI=10.1016/0378-1119(95)00815-2;
Das P., Meyer L., Seyfert H.-M., Brockmann G., Schwerin M.;
"Structure of the growth hormone-encoding gene and its promoter in
mice.";
Gene 169:209-213(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- 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; X02891; CAA26650.1; -; mRNA.
EMBL; Z46663; CAA86658.1; -; Genomic_DNA.
EMBL; AK019952; BAB31931.1; -; mRNA.
EMBL; AK019954; BAB31932.1; -; mRNA.
EMBL; AK019956; BAB31933.1; -; mRNA.
EMBL; AK019959; BAB31935.1; -; mRNA.
EMBL; AK019961; BAB31937.1; -; mRNA.
EMBL; AK030715; BAC27096.1; -; mRNA.
EMBL; BC061157; AAH61157.1; -; mRNA.
CCDS; CCDS25554.1; -.
PIR; B23911; STMS.
RefSeq; NP_032143.1; NM_008117.3.
UniGene; Mm.343934; -.
ProteinModelPortal; P06880; -.
BioGrid; 199914; 2.
IntAct; P06880; 1.
MINT; P06880; -.
STRING; 10090.ENSMUSP00000099360; -.
iPTMnet; P06880; -.
PhosphoSitePlus; P06880; -.
MaxQB; P06880; -.
PaxDb; P06880; -.
PeptideAtlas; P06880; -.
PRIDE; P06880; -.
Ensembl; ENSMUST00000103071; ENSMUSP00000099360; ENSMUSG00000020713.
GeneID; 14599; -.
KEGG; mmu:14599; -.
UCSC; uc007lys.2; mouse.
CTD; 14599; -.
MGI; MGI:95707; Gh.
eggNOG; ENOG410IFR6; Eukaryota.
eggNOG; ENOG4111HU8; LUCA.
GeneTree; ENSGT00730000111012; -.
HOGENOM; HOG000068443; -.
HOVERGEN; HBG011318; -.
InParanoid; P06880; -.
KO; K05438; -.
OMA; TYLRVMK; -.
OrthoDB; EOG091G0KPU; -.
PhylomeDB; P06880; -.
TreeFam; TF332592; -.
Reactome; R-MMU-1170546; Prolactin receptor signaling.
Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
ChiTaRS; Gh; mouse.
PRO; PR:P06880; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020713; Expressed in 101 organ(s), highest expression level in pituitary gland.
CleanEx; MM_GH; -.
ExpressionAtlas; P06880; baseline and differential.
Genevisible; P06880; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0005131; F:growth hormone receptor binding; IPI:MGI.
GO; GO:0005179; F:hormone activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071469; P:cellular response to alkaline pH; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0048286; P:lung alveolus development; ISO:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0007405; P:neuroblast proliferation; ISO:MGI.
GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:MGI.
GO; GO:0045927; P:positive regulation of growth; ISO:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:MGI.
GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; ISO:MGI.
GO; GO:0033143; P:regulation of intracellular steroid hormone receptor signaling pathway; ISO:MGI.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0032094; P:response to food; IDA:MGI.
GO; GO:0009416; P:response to light stimulus; ISO:MGI.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR034975; Somatotropin.
InterPro; IPR001400; Somatotropin/Prolactin.
InterPro; IPR018116; Somatotropin_CS.
PANTHER; PTHR11417; PTHR11417; 1.
PANTHER; PTHR11417:SF2; PTHR11417:SF2; 1.
Pfam; PF00103; Hormone_1; 1.
PRINTS; PR00836; SOMATOTROPIN.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00266; SOMATOTROPIN_1; 1.
PROSITE; PS00338; SOMATOTROPIN_2; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Hormone; Metal-binding;
Phosphoprotein; Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 26 {ECO:0000250}.
CHAIN 27 216 Somatotropin.
/FTId=PRO_0000032992.
METAL 45 45 Zinc. {ECO:0000250}.
METAL 198 198 Zinc. {ECO:0000250}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000250|UniProtKB:P01241}.
DISULFID 78 189 {ECO:0000250}.
DISULFID 206 214 {ECO:0000250}.
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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