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INS_VERMO
ID   INS_VERMO               Reviewed;         115 AA.
AC   Q9W7R2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 78.
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   Verasper moseri (Barfin flounder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae; Verasper.
OX   NCBI_TaxID=98923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Andoh T., Nagasawa H.;
RT   "Two molecular forms of insulin from barfin flounder, Verasper moseri, are
RT   derived from a single gene.";
RL   Zool. Sci. 15:931-937(1998).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AB029318; BAA82315.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9W7R2; -.
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..22
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         23..53
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015926"
FT   PROPEP          56..92
FT                   /note="C peptide"
FT                   /id="PRO_0000015927"
FT   PEPTIDE         95..115
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015928"
FT   DISULFID        32..101
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..114
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        100..105
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   115 AA;  12608 MW;  7EA2A5B568DEDDBB CRC64;
     MAALWLQSVS LLVLMLVSWS GSQAVLPPQH LCGAHLVDAL YLVCGERGFF YTPKRDVDPL
     LGFLPAKSGG AAAGGENEVA EFAFKDQMEM MVKRGIVEQC CHKPCNIFDL QNYCN
 
 
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