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SOMA_OREMO
ID   SOMA_OREMO              Reviewed;         204 AA.
AC   P34746; Q9PRH7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Chen J.-Y., Chang C.-Y., Shen S.-C., Wang J.-I., Wu J.-L.;
RT   "Production of recombinant Oreochromis mossambicus growth hormone (GH)
RT   polypeptides in E. coli cells and characterization of the molecular
RT   structure of the GH gene.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 18-204, AND PYROGLUTAMATE FORMATION AT GLN-18.
RC   TISSUE=Pituitary;
RX   PubMed=2019405; DOI=10.1016/0016-6480(91)90017-z;
RA   Yamaguchi K., King D.S., Specker J.L., Nishioka R.S., Hirano T., Bern H.A.;
RT   "Amino acid sequence of growth hormone isolated from medium of incubated
RT   pituitary glands of tilapia (Oreochromis mossambicus).";
RL   Gen. Comp. Endocrinol. 81:323-331(1991).
CC   -!- FUNCTION: Growth hormone plays an important role in growth control and
CC       involved in the regulation of several anabolic processes.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   EMBL; AF033805; AAC77875.1; -; mRNA.
DR   EMBL; AF033806; AAC77876.1; -; Genomic_DNA.
DR   PIR; A61123; A61123.
DR   AlphaFoldDB; P34746; -.
DR   SMR; P34746; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005131; F:growth hormone receptor binding; IMP:AgBase.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Pyrrolidone carboxylic acid; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:2019405"
FT   CHAIN           18..204
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033042"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2019405"
FT   DISULFID        69..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..202
FT                   /evidence="ECO:0000250"
FT   CONFLICT        38
FT                   /note="Y -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  23151 MW;  8B83CABC0ADFC329 CRC64;
     MNSVVLQLSV VCLGVSSQQI TDSQRLFSIA VNRVTHLYLL AQRLFSDFES SLQTEEQRQL
     NKIFLQDFCN SDYIISPIDK HETQRSSVLK LLSISYGLVE SWEFPSRSLS GGSSLRNQIS
     PRLSELKTGI LLLIRANQDE AENYPDTDTL QHAPYGNYYQ SLGGNESLRQ TYELLACFKK
     DMHKVETYLT VAKCRLSPEA NCTL
 
 
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