ID   INS_HYDCO               Reviewed;          59 AA.
AC   P68992; P09536;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=ins;
OS   Hydrolagus colliei (Spotted ratfish) (Chimaera colliei).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Chimaeridae; Hydrolagus.
OX   NCBI_TaxID=7873;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3780981; DOI=10.1016/0014-5793(86)81066-3;
RA   Conlon J.M., Dafgard E., Falkmer S., Thim L.;
RT   "The primary structure of ratfish insulin reveals an unusual mode of
RT   proinsulin processing.";
RL   FEBS Lett. 208:445-450(1986).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=2646172; DOI=10.1016/0016-6480(89)90064-6;
RA   Conlon J.M., Goeke R., Andrews P.C., Thim L.;
RT   "Multiple molecular forms of insulin and glucagon-like peptide from the
RT   Pacific ratfish (Hydrolagus colliei).";
RL   Gen. Comp. Endocrinol. 73:136-146(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   -!- MISCELLANEOUS: Due to a substitution of the Arg in position 31 by an
CC       Ile, this insulin B chain is longer than most other B chains and is
CC       processed differently.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   PIR; S06474; INFI.
DR   AlphaFoldDB; P68992; -.
DR   SMR; P68992; -.
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; 2.
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..38
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015822"
FT   PEPTIDE         39..59
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015823"
FT   DISULFID        7..45
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        19..58
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        44..49
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   59 AA;  6606 MW;  8827A57A9ED6D4AC CRC64;
     VPTQRLCGSH LVDALYFVCG ERGFFYSPKP IRELEPLLGI VEQCCHNTCS LANLEGYCN