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