ID   INS_CYPCA               Reviewed;         108 AA.
AC   P01335;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6306593; DOI=10.1093/nar/11.13.4541;
RA   Hahn V., Winkler J., Rapoport T.A., Liebscher D.-H., Coutelle C.,
RA   Rosenthal S.;
RT   "Carp preproinsulin cDNA sequence and evolution of insulin genes.";
RL   Nucleic Acids Res. 11:4541-4552(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-108.
RX   PubMed=7037403; DOI=10.1111/j.1432-1033.1982.tb05886.x;
RA   Makower A., Dettmer R., Rapoport T.A., Knospe S., Behlke J., Prehn S.,
RA   Franke P., Etzold G., Rosenthal S.;
RT   "Carp insulin: amino acid sequence, biological activity and structural
RT   properties.";
RL   Eur. J. Biochem. 122:339-345(1982).
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; X00989; CAA25496.1; -; mRNA.
DR   PIR; A01602; IPCA.
DR   AlphaFoldDB; P01335; -.
DR   Proteomes; UP000694384; Unplaced.
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   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:7037403"
FT   PEPTIDE         22..51
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015802"
FT   PROPEP          54..85
FT                   /note="C peptide"
FT                   /id="PRO_0000015803"
FT   PEPTIDE         88..108
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:6306593"
FT                   /id="PRO_0000015804"
FT   DISULFID        30..94
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        42..107
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        93..98
SQ   SEQUENCE   108 AA;  11821 MW;  8656D5A50B862C42 CRC64;
     MAVWIQAGAL LFLLAVSSVN ANAGAPQHLC GSHLVDALYL VCGPTGFFYN PKRDVDPPLG
     FLPPKSAQET EVADFAFKDH AEVIRKRGIV EQCCHKPCSI FELQNYCN