ID   INS_CALMI               Reviewed;          89 AA.
AC   P13190; O42485;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 104.
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   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-89.
RX   PubMed=9356216; DOI=10.1006/gcen.1997.6965;
RA   Gieseg M.A., Swarbrick P.A., Perko L., Powell R.J., Cutfield J.F.;
RT   "Elephantfish proinsulin possesses a monobasic processing site.";
RL   Gen. Comp. Endocrinol. 108:199-208(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-31 AND 69-89.
RX   PubMed=2690815; DOI=10.1042/bj2630261;
RA   Berks B.C., Marshall C.J., Carne A., Galloway S.M., Cutfield J.F.;
RT   "Isolation and structural characterization of insulin and glucagon from the
RT   holocephalan species Callorhynchus milii (elephantfish).";
RL   Biochem. J. 263:261-266(1989).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U82395; AAB64356.1; -; Genomic_DNA.
DR   PIR; S06128; INEN.
DR   AlphaFoldDB; P13190; -.
DR   SMR; P13190; -.
DR   STRING; 7868.ENSCMIP00000017634; -.
DR   Proteomes; UP000314986; Unassembled WGS sequence.
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.
FT   PEPTIDE         1..31
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015772"
FT   PROPEP          33..66
FT                   /note="C peptide"
FT                   /id="PRO_0000015773"
FT   PEPTIDE         69..89
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015774"
FT   DISULFID        7..75
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..88
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..79
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   89 AA;  10147 MW;  F2E8B0030BFCA7E3 CRC64;
     VPTQRLCGSH LVDALYFVCG ERGFFYSPKQ IRDVGPLSAF RDLEPPLDTE MEDRFPYRQQ
     LAGSKMKRGI VEQCCHNTCS LVNLEGYCN