ID   INS_TORMA               Reviewed;          70 AA.
AC   P12705;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   02-DEC-2020, entry version 92.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor; Fragments;
GN   Name=ins;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3549433; DOI=10.1016/0016-6480(86)90004-3;
RA   Conlon J.M., Thim L.;
RT   "Primary structure of insulin and a truncated C-peptide from an
RT   elasmobranchian fish, Torpedo marmorata.";
RL   Gen. Comp. Endocrinol. 64:199-205(1986).
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 represent paired basic residues assumed
CC       by homology to be present in the precursor molecule. {ECO:0000305}.
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DR   PIR; S07212; IPRYM.
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; 2.
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_0000015921"
FT   PROPEP          33..>49
FT                   /note="C peptide"
FT                   /id="PRO_0000015922"
FT   PEPTIDE         50..70
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015923"
FT   DISULFID        7..56
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        19..69
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        55..60
FT   NON_CONS        49..50
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   70 AA;  7663 MW;  049C833B36146A9C CRC64;
     LPSQHLCGSH LVEALYFVCG PKGFYYLPKA XXFVDSLAGY SKHQNGGISG IVEHCCHNTC
     SLFDLEGYCN