ID   INS_CANFA               Reviewed;         110 AA.
AC   P01321;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-NOV-2009, entry version 76.
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   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=83109071; PubMed=6296142;
RA   Kwok S.C.M., Chan S.J., Steiner D.F.;
RT   "Cloning and nucleotide sequence analysis of the dog insulin gene.
RT   Coded amino acid sequence of canine preproinsulin predicts an
RT   additional C-peptide fragment.";
RL   J. Biol. Chem. 258:2357-2363(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   MEDLINE=66160119; PubMed=5949593; DOI=10.1016/0002-9343(66)90145-8;
RA   Smith L.F.;
RT   "Species variation in the amino acid sequence of insulin.";
RL   Am. J. Med. 40:662-666(1966).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen 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.
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DR   EMBL; V00179; CAA23475.1; -; Genomic_DNA.
DR   PIR; A92413; IPDG.
DR   RefSeq; NP_001123565.1; -.
DR   UniGene; Cfa.18796; -.
DR   HSSP; P01317; 1APH.
DR   SMR; P01321; 25-84.
DR   STRING; P01321; -.
DR   Ensembl; ENSCAFT00000016041; ENSCAFP00000014836; ENSCAFG00000010092; Canis familiaris.
DR   GeneID; 483665; -.
DR   KEGG; cfa:483665; -.
DR   CTD; 483665; -.
DR   HOVERGEN; P01321; -.
DR   OMA; PAPAFVN; -.
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   InterPro; IPR004825; Ins/IGF/relaxin.
DR   InterPro; IPR016179; Insulin-like.
DR   Gene3D; G3DSA:1.10.100.10; Ins/IGF/relaxin; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULINB.
DR   ProDom; PD015667; Mollusc_ins; 1.
DR   SMART; SM00078; IlGF; 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;
KW   Hormone; Secreted; Signal.
FT   SIGNAL        1     24
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015777.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015778.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015779.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
SQ   SEQUENCE   110 AA;  12190 MW;  A574791864A4FB98 CRC64;
     MALWMRLLPL LALLALWAPA PTRAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVED
     LQVRDVELAG APGEGGLQPL ALEGALQKRG IVEQCCTSIC SLYQLENYCN
//