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SOMA_HORSE
ID   SOMA_HORSE              Reviewed;         216 AA.
AC   P01245;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=GH1;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=8206392; DOI=10.1016/0378-1119(94)90115-5;
RA   Ascacio-Martinez J.A., Barrera-Saldana H.A.;
RT   "Sequence of a cDNA encoding horse growth hormone.";
RL   Gene 143:299-300(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-216.
RX   PubMed=965151; DOI=10.1111/j.1399-3011.1976.tb02523.x;
RA   Zakin M.M., Poskus E., Langton A.A., Ferrara P., Santome J.A.,
RA   Dellacha J.M., Paladini A.C.;
RT   "Primary structure of equine growth hormone.";
RL   Int. J. Pept. Protein Res. 8:435-444(1976).
RN   [3]
RP   PRELIMINARY PROTEIN SEQUENCE OF 27-216.
RX   PubMed=4747849; DOI=10.1016/0014-5793(73)80829-4;
RA   Zakin M.M., Poskus E., Dellacha J.M., Paladini A.C., Santome J.A.;
RT   "The amino acid sequence of equine growth hormone.";
RL   FEBS Lett. 34:353-355(1973).
RN   [4]
RP   PROTEIN SEQUENCE OF 68-95 AND 183-216.
RX   PubMed=11946725; DOI=10.1016/0014-5793(72)80458-7;
RA   Zakin M.M., Poskus E., Dellacha J.M., Paladini A.C., Santome J.A.;
RT   "Amino acid sequences around the cystine residues in equine growth
RT   hormone.";
RL   FEBS Lett. 25:77-82(1972).
RN   [5]
RP   PROTEIN SEQUENCE OF 202-216.
RX   PubMed=4876100; DOI=10.1042/bj1090019;
RA   Oliver L., Hartree A.S.;
RT   "Amino acid sequences around the cystine residues in horse growth
RT   hormone.";
RL   Biochem. J. 109:19-24(1968).
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; U02929; AAA21027.1; -; mRNA.
DR   PIR; A91772; STHO.
DR   RefSeq; NP_001075417.1; NM_001081948.1.
DR   AlphaFoldDB; P01245; -.
DR   SMR; P01245; -.
DR   STRING; 9796.ENSECAP00000007142; -.
DR   PaxDb; P01245; -.
DR   GeneID; 100034180; -.
DR   KEGG; ecb:100034180; -.
DR   CTD; 2688; -.
DR   InParanoid; P01245; -.
DR   OrthoDB; 1190548at2759; -.
DR   Proteomes; UP000002281; 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; IBA:GO_Central.
DR   GO; GO:0045927; P:positive regulation of growth; IBA:GO_Central.
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; IBA:GO_Central.
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:965151"
FT   CHAIN           27..216
FT                   /note="Somatotropin"
FT                   /id="PRO_0000032987"
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   DISULFID        206..214
SQ   SEQUENCE   216 AA;  24423 MW;  37AB3173834D11AC CRC64;
     MAAGPRTSVL LAFGLLCLPW PQDVGAFPAM PLSSLFANAV LRAQHLHQLA ADTYKEFERA
     YIPEGQRYSI QNAQAAFCFS ETIPAPTGKD EAQQRSDMEL LRFSLLLIQS WLGPVQLLSR
     VFTNSLVFGT SDRVYEKLRD LEEGIQALMR ELEDGSPRAG QILKQTYDKF DTNLRSDDAL
     LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF
 
 
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