ID   INS_ANAPL               Reviewed;          81 AA.
AC   P01333;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-DEC-2020, entry version 93.
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   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30 AND 61-81.
RX   PubMed=4763354; DOI=10.1111/j.1399-3011.1973.tb02317.x;
RA   Markussen J., Sundby F.;
RT   "Duck insulin: isolation, crystallization and amino acid sequence.";
RL   Int. J. Pept. Protein Res. 5:37-48(1973).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-58.
RX   PubMed=4715652; DOI=10.1111/j.1432-1033.1973.tb02772.x;
RA   Markussen J., Sundby F.;
RT   "Isolation and amino-acid sequence of the C-peptide of duck proinsulin.";
RL   Eur. J. Biochem. 34:401-408(1973).
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   -!- CAUTION: X's at positions 31-32 and 59-60 represent paired basic
CC       residues assumed by homology to be present in the precursor molecule.
CC       {ECO:0000305}.
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DR   PIR; A01600; IPDK.
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; Direct protein sequencing; Disulfide bond;
KW   Glucose metabolism; Hormone; Secreted.
FT   PEPTIDE         1..30
FT                   /note="Insulin B chain"
FT                   /evidence="ECO:0000269|PubMed:4763354"
FT                   /id="PRO_0000015746"
FT   PROPEP          33..58
FT                   /note="C peptide"
FT                   /id="PRO_0000015747"
FT   PEPTIDE         61..81
FT                   /note="Insulin A chain"
FT                   /evidence="ECO:0000269|PubMed:4763354"
FT                   /id="PRO_0000015748"
FT   DISULFID        7..67
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        19..80
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        66..71
SQ   SEQUENCE   81 AA;  9105 MW;  6EA8A271F099DA91 CRC64;
     AANQHLCGSH LVEALYLVCG ERGFFYSPKT XXDVEQPLVN GPLHGEVGEL PFQHEEYQXX
     GIVEQCCENP CSLYQLENYC N