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SOMA_PRIGL
ID   SOMA_PRIGL              Reviewed;         183 AA.
AC   P34006;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
GN   Name=gh;
OS   Prionace glauca (Blue shark) (Squalus glaucus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Carcharhinidae;
OC   Prionace.
OX   NCBI_TaxID=7815;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2707584; DOI=10.1016/0016-6480(89)90098-1;
RA   Yamaguchi K., Yasuda A., Lewis U.J., Yokoo Y., Kawauchi H.;
RT   "The complete amino acid sequence of growth hormone of an elasmobranch, the
RT   blue shark (Prionace glauca).";
RL   Gen. Comp. Endocrinol. 73:252-259(1989).
CC   -!- FUNCTION: Growth hormone plays an important role in growth control and
CC       is involved in the regulation of several anabolic processes. Implicated
CC       as an osmoregulatory substance important for seawater adaptation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   PIR; A60623; A60623.
DR   AlphaFoldDB; P34006; -.
DR   SMR; P34006; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005131; F:growth hormone receptor binding; IEA:InterPro.
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   Secreted; Zinc.
FT   CHAIN           1..183
FT                   /note="Somatotropin"
FT                   /id="PRO_0000181337"
FT   REGION          38..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..156
FT                   /evidence="ECO:0000250"
FT   DISULFID        173..181
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   183 AA;  21071 MW;  681E45B3D9D9B30D CRC64;
     YPLLPLSDLF AKAVHRAQHL HLVAAETTKD FERKYIPEEQ RHSHKSSPSA FCQSETIPAP
     TGKEDAQQRS DRELLLYSLL LIQSWLNPIQ NLSAFRTSDR VYDKLRDLEE GIFALMKTLE
     DGGSSQGFAW LKFSYERFDG NLSEEALMKN YGLLACFKKD MHKVETYLKV MNCKRFAESN
     CTV
 
 
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