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INS_PONPY
ID   INS_PONPY               Reviewed;         110 AA.
AC   Q8HXV2;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12952878; DOI=10.1101/gr.948003;
RA   Stead J.D.H., Hurles M.E., Jeffreys A.J.;
RT   "Global haplotype diversity in the human insulin gene region.";
RL   Genome Res. 13:2101-2111(2003).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It increases
CC       cell permeability to monosaccharides, amino acids and fatty acids. It
CC       accelerates glycolysis, the pentose phosphate cycle, and glycogen
CC       synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds. {ECO:0000250|UniProtKB:P01308}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AY137503; AAN06937.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8HXV2; -.
DR   BMRB; Q8HXV2; -.
DR   SMR; Q8HXV2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04367; IlGF_insulin_like; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR11454; PTHR11454; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015884"
FT   PROPEP          57..87
FT                   /note="C peptide"
FT                   /id="PRO_0000015885"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015886"
FT   DISULFID        31..96
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
FT   DISULFID        43..109
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
SQ   SEQUENCE   110 AA;  12038 MW;  22D2B32B94F520F8 CRC64;
     MALWMRLLPL LALLALWGPD PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
 
 
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