ID   INS_RABIT               Reviewed;         110 AA.
AC   P01311;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 123.
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Pancreas;
RX   PubMed=8132571; DOI=10.1016/s0021-9258(17)37214-9;
RA   Devaskar S.U., Giddings S.J., Rajakumar P.A., Carnaghi L.R., Menon R.K.,
RA   Zahm D.S.;
RT   "Insulin gene expression and insulin synthesis in mammalian neuronal
RT   cells.";
RL   J. Biol. Chem. 269:8445-8454(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-110.
RA   Giddings S.J., Carnaghi L.R., Devaskar S.U.;
RL   Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
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; U03610; AAA19033.1; -; mRNA.
DR   EMBL; M61153; AAA17540.1; -; mRNA.
DR   PIR; A53438; INRB.
DR   RefSeq; NP_001075804.1; NM_001082335.1.
DR   AlphaFoldDB; P01311; -.
DR   BMRB; P01311; -.
DR   SMR; P01311; -.
DR   STRING; 9986.ENSOCUP00000020463; -.
DR   GeneID; 100009181; -.
DR   KEGG; ocu:100009181; -.
DR   CTD; 3630; -.
DR   eggNOG; ENOG502S5P5; Eukaryota.
DR   InParanoid; P01311; -.
DR   OrthoDB; 1644517at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:5949593"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /evidence="ECO:0000269|PubMed:8132571"
FT                   /id="PRO_0000015892"
FT   PROPEP          57..87
FT                   /note="C peptide"
FT                   /id="PRO_0000015893"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:8132571"
FT                   /id="PRO_0000015894"
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"
FT   CONFLICT        83
FT                   /note="E -> Y (in Ref. 3; AAA17540)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  11838 MW;  82D2975B85D77FA8 CRC64;
     MASLAALLPL LALLVLCRLD PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKSRREVEE
     LQVGQAELGG GPGAGGLQPS ALELALQKRG IVEQCCTSIC SLYQLENYCN