ID   INS_BALPH               Reviewed;          51 AA.
AC   P67973; P01312;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
GN   Name=INS;
OS   Balaenoptera physalus (Fin whale) (Balaena physalus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=9770;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=14228503; DOI=10.1093/oxfordjournals.jbchem.a127991;
RA   Hama H., Titani K., Sakaki S., Narita K.;
RT   "The amino acid sequence in fin-whale insulin.";
RL   J. Biochem. 56:285-293(1964).
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   PIR; A91918; INWHF.
DR   PDB; 1BZV; NMR; -; A=31-51.
DR   PDBsum; 1BZV; -.
DR   AlphaFoldDB; P67973; -.
DR   SMR; P67973; -.
DR   EvolutionaryTrace; P67973; -.
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   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE         1..30
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015760"
FT   PEPTIDE         31..51
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015761"
FT   DISULFID        7..37
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        19..50
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        36..41
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000305"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:1BZV"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1BZV"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:1BZV"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:1BZV"
SQ   SEQUENCE   51 AA;  5766 MW;  9007B514691A7CDD CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA GIVEQCCTSI CSLYQLENYC N