ID   INS_CRILO               Reviewed;         110 AA.
AC   P01313;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   25-MAY-2022, entry version 100.
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   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6365663; DOI=10.2337/diab.33.3.297;
RA   Bell G.I., Sanchez-Pescador R.;
RT   "Sequence of a cDNA encoding Syrian hamster preproinsulin.";
RL   Diabetes 33:297-300(1984).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RA   Neelon F.A., Delcher H.K., Steinman H., Lebovitz H.E.;
RT   "Structure of hamster insulin: comparison with a tumor insulin.";
RL   Fed. Proc. 32:300-300(1973).
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; M26328; AAA37089.1; -; mRNA.
DR   AlphaFoldDB; P01313; -.
DR   BMRB; P01313; -.
DR   SMR; P01313; -.
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   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|Ref.2"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015797"
FT   PROPEP          57..87
FT                   /note="C peptide"
FT                   /id="PRO_0000015798"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015799"
FT   DISULFID        31..96
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        43..109
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        95..100
SQ   SEQUENCE   110 AA;  12268 MW;  219E92B85A535CEC CRC64;
     MTLWMRLLPL LTLLVLWEPN PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKSRRGVED
     PQVAQLELGG GPGADDLQTL ALEVAQQKRG IVDQCCTSIC SLYQLENYCN