INS_BOVIN
ID INS_BOVIN Reviewed; 105 AA.
AC P01317;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 187.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2456452; DOI=10.1210/mend-1-4-327;
RA D'Agostino J., Younes M.A., White J.W., Besch P.K., Field J.B.,
RA Frazier M.L.;
RT "Cloning and nucleotide sequence analysis of complementary deoxyribonucleic
RT acid for bovine preproinsulin.";
RL Mol. Endocrinol. 1:327-331(1987).
RN [2]
RP PROTEIN SEQUENCE OF 25-105.
RX PubMed=4928892; DOI=10.1016/s0021-9258(18)62252-5;
RA Nolan C., Margoliash E., Peterson J.D., Steiner D.F.;
RT "The structure of bovine proinsulin.";
RL J. Biol. Chem. 246:2780-2795(1971).
RN [3]
RP PROTEIN SEQUENCE OF 25-54.
RX PubMed=14886311; DOI=10.1042/bj0490481;
RA Sanger F., Tuppy H.;
RT "The amino-acid sequence in the phenylalanyl chain of insulin. 2. The
RT investigation of peptides from enzymic hydrolysates.";
RL Biochem. J. 49:481-490(1951).
RN [4]
RP PROTEIN SEQUENCE OF 57-82.
RX PubMed=5545080; DOI=10.1016/s0021-9258(19)76983-x;
RA Steiner D.F., Cho S., Oyer P.E., Terris S., Peterson J.D., Rubenstein A.H.;
RT "Isolation and characterization of proinsulin C-peptide from bovine
RT pancreas.";
RL J. Biol. Chem. 246:1365-1374(1971).
RN [5]
RP PROTEIN SEQUENCE OF 57-82.
RX PubMed=5105368; DOI=10.1111/j.1432-1033.1971.tb01377.x;
RA Salokangas A., Smyth D.G., Markussen J., Sundby F.;
RT "Bovine proinsulin: amino acid sequence of the C-peptide isolated from
RT pancreas.";
RL Eur. J. Biochem. 20:183-189(1971).
RN [6]
RP PROTEIN SEQUENCE OF 85-105.
RX PubMed=13032079; DOI=10.1042/bj0530366;
RA Sanger F., Thompson E.O.P.;
RT "The amino-acid sequence in the glycyl chain of insulin. 2. The
RT investigation of peptides from enzymic hydrolysates.";
RL Biochem. J. 53:366-374(1953).
RN [7]
RP PROTEIN SEQUENCE OF 25-54 AND 85-105, AND DISULFIDE BONDS.
RX PubMed=13249947; DOI=10.1042/bj0600541;
RA Ryle A.P., Sanger F., Smith L.F., Kitai R.;
RT "The disulphide bonds of insulin.";
RL Biochem. J. 60:541-556(1955).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-54.
RA Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G.,
RA Reynolds C.D.;
RT "The structure of des-Phe b1 bovine insulin.";
RL Acta Crystallogr. B 38:3028-3032(1982).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-49.
RX PubMed=9141131;
RX DOI=10.1002/(sici)1097-0134(199704)27:4<507::aid-prot4>3.0.co;2-7;
RA Brange J., Dodson G.G., Edwards D.J., Holden P.H., Whittingham J.L.;
RT "A model of insulin fibrils derived from the X-ray crystal structure of a
RT monomeric insulin (despentapeptide insulin).";
RL Proteins 27:507-516(1997).
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:0000269|PubMed:13249947}.
CC -!- INTERACTION:
CC P01317; P01317: INS; NbExp=6; IntAct=EBI-3989070, EBI-3989070;
CC P01317; P08069: IGF1R; Xeno; NbExp=4; IntAct=EBI-3989070, EBI-475981;
CC P01317; P06213: INSR; Xeno; NbExp=5; IntAct=EBI-3989070, EBI-475899;
CC P01317; P06213-2: INSR; Xeno; NbExp=2; IntAct=EBI-3989070, EBI-9984921;
CC P01317; A1S3N8: Sama_0787; Xeno; NbExp=2; IntAct=EBI-3989070, EBI-7016414;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th century
CC - Issue 9 of April 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/009";
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DR EMBL; M54979; AAA30722.1; -; mRNA.
DR PIR; A40909; IPBO.
DR PDB; 1APH; X-ray; 2.00 A; A=85-105, B=25-54.
DR PDB; 1BPH; X-ray; 2.00 A; A=85-105, B=25-54.
DR PDB; 1CPH; X-ray; 1.90 A; A=85-105, B=25-54.
DR PDB; 1DPH; X-ray; 1.90 A; A=85-105, B=25-54.
DR PDB; 1HO0; NMR; -; A=25-54.
DR PDB; 1PID; X-ray; 1.30 A; A/C=85-105, B/D=25-49.
DR PDB; 2A3G; X-ray; 2.25 A; A/C=85-105, B/D=25-54.
DR PDB; 2BN1; X-ray; 1.40 A; A=85-105, B=25-54.
DR PDB; 2BN3; X-ray; 1.40 A; A=85-105, B=25-54.
DR PDB; 2INS; X-ray; 2.50 A; A/C=85-105, B/D=26-54.
DR PDB; 2ZP6; X-ray; 2.56 A; A/C=85-105, B/D=25-54.
DR PDB; 4BS3; X-ray; 2.30 A; A=85-105, B=25-54.
DR PDB; 4E7T; X-ray; 1.40 A; A/C=85-105, B/D=25-54.
DR PDB; 4E7U; X-ray; 1.30 A; A/C=85-105, B/D=25-54.
DR PDB; 4E7V; X-ray; 1.80 A; 1/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y=85-105, 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z=25-54.
DR PDB; 4I5Y; X-ray; 1.80 A; A=85-105, B=25-54.
DR PDB; 4I5Z; X-ray; 1.80 A; A=85-105, B=25-54.
DR PDB; 4IDW; X-ray; 2.70 A; A/C=85-105, B/D=25-54.
DR PDB; 4IHN; X-ray; 1.16 A; A=85-105, B=25-54.
DR PDB; 4M4F; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR PDB; 4M4H; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR PDB; 4M4I; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR PDB; 4M4J; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
DR PDB; 4M4L; X-ray; 1.45 A; A/C=85-105, B/D=25-54.
DR PDB; 4M4M; X-ray; 1.50 A; A/C=85-105, B/D=25-54.
DR PDB; 5AZZ; X-ray; 1.45 A; A=85-105, B=25-54.
DR PDB; 5KQV; X-ray; 4.40 A; A/I=85-105, B/J=25-54.
DR PDB; 5MIZ; NMR; -; A=85-105, B=25-54.
DR PDB; 6KH8; NMR; -; A=85-105, B=25-54.
DR PDB; 6KH9; NMR; -; A=85-105, B=25-54.
DR PDB; 6KHA; NMR; -; A=85-105, B=25-54.
DR PDB; 6OR0; X-ray; 1.55 A; A=85-105, B=25-53.
DR PDB; 6Q8Q; X-ray; 2.00 A; A=85-105, B=25-54.
DR PDB; 6QQ7; X-ray; 1.65 A; A=85-105, B=25-54.
DR PDB; 6QQG; X-ray; 2.15 A; A=85-105, B=25-54.
DR PDB; 6QRH; X-ray; 2.15 A; A=85-105, B=25-54.
DR PDB; 6QRK; X-ray; 2.10 A; A=85-105, B=25-54.
DR PDB; 6ZHB; EM; 3.25 A; A/C=85-105, B/D=25-54.
DR PDB; 6ZI8; X-ray; 2.30 A; A/B/C/D=1-105.
DR PDB; 7ELJ; NMR; -; A=85-105, B=25-54.
DR PDBsum; 1APH; -.
DR PDBsum; 1BPH; -.
DR PDBsum; 1CPH; -.
DR PDBsum; 1DPH; -.
DR PDBsum; 1HO0; -.
DR PDBsum; 1PID; -.
DR PDBsum; 2A3G; -.
DR PDBsum; 2BN1; -.
DR PDBsum; 2BN3; -.
DR PDBsum; 2INS; -.
DR PDBsum; 2ZP6; -.
DR PDBsum; 4BS3; -.
DR PDBsum; 4E7T; -.
DR PDBsum; 4E7U; -.
DR PDBsum; 4E7V; -.
DR PDBsum; 4I5Y; -.
DR PDBsum; 4I5Z; -.
DR PDBsum; 4IDW; -.
DR PDBsum; 4IHN; -.
DR PDBsum; 4M4F; -.
DR PDBsum; 4M4H; -.
DR PDBsum; 4M4I; -.
DR PDBsum; 4M4J; -.
DR PDBsum; 4M4L; -.
DR PDBsum; 4M4M; -.
DR PDBsum; 5AZZ; -.
DR PDBsum; 5KQV; -.
DR PDBsum; 5MIZ; -.
DR PDBsum; 6KH8; -.
DR PDBsum; 6KH9; -.
DR PDBsum; 6KHA; -.
DR PDBsum; 6OR0; -.
DR PDBsum; 6Q8Q; -.
DR PDBsum; 6QQ7; -.
DR PDBsum; 6QQG; -.
DR PDBsum; 6QRH; -.
DR PDBsum; 6QRK; -.
DR PDBsum; 6ZHB; -.
DR PDBsum; 6ZI8; -.
DR PDBsum; 7ELJ; -.
DR AlphaFoldDB; P01317; -.
DR BMRB; P01317; -.
DR SMR; P01317; -.
DR DIP; DIP-52901N; -.
DR IntAct; P01317; 5.
DR MINT; P01317; -.
DR STRING; 9913.ENSBTAP00000017289; -.
DR Allergome; 2118; Bos d Insulin.
DR CarbonylDB; P01317; -.
DR PaxDb; P01317; -.
DR PRIDE; P01317; -.
DR ABCD; P01317; 4 sequenced antibodies.
DR eggNOG; ENOG502S5P5; Eukaryota.
DR InParanoid; P01317; -.
DR OrthoDB; 1644517at2759; -.
DR EvolutionaryTrace; P01317; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005158; F:insulin receptor binding; IDA:AgBase.
DR GO; GO:0035938; P:estradiol secretion; IDA:AgBase.
DR GO; GO:0007631; P:feeding behavior; IDA:AgBase.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IDA:AgBase.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
DR GO; GO:0032099; P:negative regulation of appetite; IDA:AgBase.
DR GO; GO:1903488; P:negative regulation of lactation; IDA:AgBase.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:AgBase.
DR GO; GO:1903524; P:positive regulation of blood circulation; IDA:AgBase.
DR GO; GO:1903431; P:positive regulation of cell maturation; IDA:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IDA:AgBase.
DR GO; GO:1903489; P:positive regulation of lactation; IDA:AgBase.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IDA:AgBase.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:AgBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:AgBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:AgBase.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:AgBase.
DR GO; GO:0009306; P:protein secretion; IMP:AgBase.
DR GO; GO:1903544; P:response to butyrate; IDA:AgBase.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
DR GO; GO:0009749; P:response to glucose; IMP:AgBase.
DR GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
DR GO; GO:0031667; P:response to nutrient levels; IDA:AgBase.
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 3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:13249947,
FT ECO:0000269|PubMed:14886311, ECO:0000269|PubMed:4928892"
FT PEPTIDE 25..54
FT /note="Insulin B chain"
FT /evidence="ECO:0000269|PubMed:2456452"
FT /id="PRO_0000015764"
FT PROPEP 57..82
FT /note="C peptide"
FT /id="PRO_0000015765"
FT PEPTIDE 85..105
FT /note="Insulin A chain"
FT /evidence="ECO:0000269|PubMed:2456452"
FT /id="PRO_0000015766"
FT DISULFID 31..91
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000269|PubMed:13249947"
FT DISULFID 43..104
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000269|PubMed:13249947"
FT DISULFID 90..95
FT /evidence="ECO:0000269|PubMed:13249947,
FT ECO:0000269|PubMed:4928892"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:4IHN"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4IHN"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4E7U"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:4IHN"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:4IHN"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:4IHN"
SQ SEQUENCE 105 AA; 11393 MW; 75307CF78E61C06A CRC64;
MALWTRLRPL LALLALWPPP PARAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG
PQVGALELAG GPGAGGLEGP PQKRGIVEQC CASVCSLYQL ENYCN
