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