ID   INS_CHLAE               Reviewed;         110 AA.
AC   P30407; P01309;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 91.
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   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1560757; DOI=10.1093/oxfordjournals.molbev.a040713;
RA   Seino S., Bell G.I., Li W.;
RT   "Sequences of primate insulin genes support the hypothesis of a slower rate
RT   of molecular evolution in humans and apes than in monkeys.";
RL   Mol. Biol. Evol. 9:193-203(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=4626369; DOI=10.1016/s0021-9258(19)44991-0;
RA   Peterson J.D., Nehrlich S., Oyer P.E., Steiner D.F.;
RT   "Determination of the amino acid sequence of the monkey, sheep, and dog
RT   proinsulin C-peptides by a semi-micro Edman degradation procedure.";
RL   J. Biol. Chem. 247:4866-4871(1972).
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; X61092; CAA43405.1; -; Genomic_DNA.
DR   PIR; B42179; B42179.
DR   AlphaFoldDB; P30407; -.
DR   BMRB; P30407; -.
DR   SMR; P30407; -.
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   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015785"
FT   PROPEP          57..87
FT                   /note="C peptide"
FT                   /id="PRO_0000015786"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015787"
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;  12019 MW;  95A1F54BE7B247F9 CRC64;
     MALWMRLLPL LALLALWGPD PVPAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     PQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN