ID   INS_CHICH               Reviewed;          86 AA.
AC   P01327;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   25-MAY-2022, entry version 98.
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   Chinchilla chinchilla (Short-tailed chinchilla) (Chinchilla brevicaudata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC   Chinchillidae; Chinchilla.
OX   NCBI_TaxID=10152;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30 AND 66-86.
RX   PubMed=1175610; DOI=10.1111/j.1432-1033.1975.tb02190.x;
RA   Wood S.P., Blundell T.L., Wollmer A., Lazarus N.R., Neville R.W.J.;
RT   "The relation of conformation and association of insulin to receptor
RT   binding; X-ray and circular-dichroism studies on bovine and hystricomorph
RT   insulins.";
RL   Eur. J. Biochem. 55:531-542(1975).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-63.
RX   PubMed=808541; DOI=10.1016/s0021-9258(19)41065-x;
RA   Snell C.R., Smyth D.G.;
RT   "Proinsulin: a proposed three-dimensional structure.";
RL   J. Biol. Chem. 250:6291-6295(1975).
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}.
CC   -!- CAUTION: X's at positions 31-32 and 64-65 represent paired basic
CC       residues assumed by homology to be present in the precursor molecule.
CC       {ECO:0000305}.
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DR   PIR; A01593; INCB.
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; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE         1..30
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015788"
FT   PROPEP          33..63
FT                   /note="C peptide"
FT                   /id="PRO_0000043180"
FT   PEPTIDE         66..86
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015789"
FT   DISULFID        7..72
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..85
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..76
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   86 AA;  9470 MW;  95A4DAA4C004B4E2 CRC64;
     FVNKHLCGSH LVDALYLVCG DRGFFYTPMA XXELEDPQVG QADPGVVPEA GRLQPLALEM
     TLQXXGIVDQ CCTSICTLYQ LENYCN