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INS_HORSE
ID   INS_HORSE               Reviewed;          86 AA.
AC   P01310;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 108.
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   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-30 AND 66-86.
RX   PubMed=13373434; DOI=10.1016/0003-9861(56)90203-x;
RA   Harris J.I., Sanger F., Naughton M.A.;
RT   "Species differences in insulin.";
RL   Arch. Biochem. Biophys. 65:427-438(1956).
RN   [2]
RP   PROTEIN SEQUENCE OF 33-63.
RX   PubMed=4640931; DOI=10.1016/s0021-9258(20)81791-8;
RA   Tager H.S., Steiner D.F.;
RT   "Primary structures of the proinsulin connecting peptides of the rat and
RT   the horse.";
RL   J. Biol. Chem. 247:7936-7940(1972).
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. {ECO:0000250|UniProtKB:P01308}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- CAUTION: X's at positions 31-32 and 64-65 represent paired basic
CC       residues assumed by homology to be present in the precursor molecule.
CC       {ECO:0000305}.
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DR   PIR; A01580; IPHO.
DR   BMRB; P01310; -.
DR   STRING; 9796.ENSECAP00000022114; -.
DR   PRIDE; P01310; -.
DR   InParanoid; P01310; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IBA:GO_Central.
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; Reference proteome; Secreted.
FT   PEPTIDE         1..30
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015816"
FT   PROPEP          33..63
FT                   /note="C peptide"
FT                   /id="PRO_0000015817"
FT   PEPTIDE         66..86
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015818"
FT   DISULFID        7..72
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
FT   DISULFID        19..85
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
FT   DISULFID        71..76
FT                   /evidence="ECO:0000250|UniProtKB:P01308"
SQ   SEQUENCE   86 AA;  9147 MW;  A3E1E822711BDB46 CRC64;
     FVNQHLCGSH LVEALYLVCG ERGFFYTPKA XXEAEDPQVG EVELGGGPGL GGLQPLALAG
     PQQXXGIVEQ CCTGICSLYQ LENYCN
 
 
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