ID   INS_ANGAN               Reviewed;          53 AA.
AC   P41522;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-JUN-2021, entry version 75.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor; Fragment;
GN   Name=ins;
OS   Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30.
RC   TISSUE=Pancreas;
RX   PubMed=2776429; DOI=10.1016/0305-0491(89)90092-8;
RA   Conlon J.M., Thim L.;
RT   "Isolation and primary structure of the C-peptide of proinsulin from the
RT   European eel (Anguilla anguilla).";
RL   Comp. Biochem. Physiol. 93B:359-362(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-53.
RC   TISSUE=Pancreas;
RX   PubMed=1874385; DOI=10.1016/0016-6480(91)90292-e;
RA   Conlon J.M., Andrews P.C., Thim L., Moon T.W.;
RT   "The primary structure of glucagon-like peptide but not insulin has been
RT   conserved between the American eel, Anguilla rostrata and the European eel,
RT   Anguilla anguilla.";
RL   Gen. Comp. Endocrinol. 82:23-32(1991).
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; JL0099; JL0099.
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   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   Pfam; PF00049; Insulin; 1.
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   PROPEP          1..30
FT                   /note="C peptide"
FT                   /id="PRO_0000015749"
FT   PEPTIDE         33..53
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015750"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        38..43
FT   NON_TER         1
SQ   SEQUENCE   53 AA;  5955 MW;  DDD3F00B33144EAD CRC64;
     DVEPLLGFLS PKSGQENEVD DFPYKGQGEL XXGIVEQCCH KPCNIFDLQN YCN