ID   INS_LOPAM               Reviewed;         116 AA.
AC   P69045; P01341;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 59.
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   Lophius americanus (American angler) (Anglerfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Lophiiformes; Lophiidae; Lophius.
OX   NCBI_TaxID=8073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7001633; DOI=10.1126/science.7001633;
RA   Hobart P.M., Shen L.-P., Crawford R., Pictet R.L., Rutter W.J.;
RT   "Comparison of the nucleic acid sequence of anglerfish and mammalian
RT   insulin mRNA's from cloned cDNA's.";
RL   Science 210:1360-1363(1980).
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; V00634; CAA23907.1; -; mRNA.
DR   PIR; A01608; IPAF.
DR   AlphaFoldDB; P69045; -.
DR   SMR; P69045; -.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL          1..24
FT   PEPTIDE         25..53
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015832"
FT   PROPEP          56..93
FT                   /note="C peptide"
FT                   /id="PRO_0000015833"
FT   PEPTIDE         96..116
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015834"
FT   DISULFID        32..102
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..115
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        101..106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   116 AA;  12737 MW;  C686F8EF8183BEFE CRC64;
     MAALWLQSFS LLVLLVVSWP GSQAVAPAQH LCGSHLVDAL YLVCGDRGFF YNPKRDVDQL
     LGFLPPKSGG AAAAGADNEV AEFAFKDQME MMVKRGIVEQ CCHRPCNIFD LQNYCN