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Insulin [Cleaved into: Insulin B chain; Insulin A chain]

 INS_BOVIN               Reviewed;         105 AA.
P01317;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
27-SEP-2017, entry version 166.
RecName: Full=Insulin;
Contains:
RecName: Full=Insulin B chain;
Contains:
RecName: Full=Insulin A chain;
Flags: Precursor;
Name=INS;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2456452; DOI=10.1210/mend-1-4-327;
D'Agostino J., Younes M.A., White J.W., Besch P.K., Field J.B.,
Frazier M.L.;
"Cloning and nucleotide sequence analysis of complementary
deoxyribonucleic acid for bovine preproinsulin.";
Mol. Endocrinol. 1:327-331(1987).
[2]
PROTEIN SEQUENCE OF 25-105.
PubMed=4928892;
Nolan C., Margoliash E., Peterson J.D., Steiner D.F.;
"The structure of bovine proinsulin.";
J. Biol. Chem. 246:2780-2795(1971).
[3]
PROTEIN SEQUENCE OF 25-54.
PubMed=14886311; DOI=10.1042/bj0490481;
Sanger F., Tuppy H.;
"The amino-acid sequence in the phenylalanyl chain of insulin. 2. The
investigation of peptides from enzymic hydrolysates.";
Biochem. J. 49:481-490(1951).
[4]
PROTEIN SEQUENCE OF 57-82.
PubMed=5545080;
Steiner D.F., Cho S., Oyer P.E., Terris S., Peterson J.D.,
Rubenstein A.H.;
"Isolation and characterization of proinsulin C-peptide from bovine
pancreas.";
J. Biol. Chem. 246:1365-1374(1971).
[5]
PROTEIN SEQUENCE OF 57-82.
PubMed=5105368; DOI=10.1111/j.1432-1033.1971.tb01377.x;
Salokangas A., Smyth D.G., Markussen J., Sundby F.;
"Bovine proinsulin: amino acid sequence of the C-peptide isolated from
pancreas.";
Eur. J. Biochem. 20:183-189(1971).
[6]
PROTEIN SEQUENCE OF 85-105.
PubMed=13032079; DOI=10.1042/bj0530366;
Sanger F., Thompson E.O.P.;
"The amino-acid sequence in the glycyl chain of insulin. 2. The
investigation of peptides from enzymic hydrolysates.";
Biochem. J. 53:366-374(1953).
[7]
PROTEIN SEQUENCE OF 25-54 AND 85-105, AND DISULFIDE BONDS.
PubMed=13249947; DOI=10.1042/bj0600541;
Ryle A.P., Sanger F., Smith L.F., Kitai R.;
"The disulphide bonds of insulin.";
Biochem. J. 60:541-556(1955).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-54.
Smith G.D., Duax W.L., Dodson E.J., Dodson G.G., de Graaf R.A.G.,
Reynolds C.D.;
"The structure of des-Phe b1 bovine insulin.";
Acta Crystallogr. B 38:3028-3032(1982).
[9]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 25-49.
PubMed=9141131;
DOI=10.1002/(SICI)1097-0134(199704)27:4<507::AID-PROT4>3.3.CO;2-H;
Brange J., Dodson G.G., Edwards D.J., Holden P.H., Whittingham J.L.;
"A model of insulin fibrils derived from the X-ray crystal structure
of a monomeric insulin (despentapeptide insulin).";
Proteins 27:507-516(1997).
-!- FUNCTION: Insulin decreases blood glucose concentration. It
increases cell permeability to monosaccharides, amino acids and
fatty acids. It accelerates glycolysis, the pentose phosphate
cycle, and glycogen synthesis in liver.
-!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
disulfide bonds. {ECO:0000269|PubMed:13249947}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-3989070, EBI-3989070;
P08069:IGF1R (xeno); NbExp=4; IntAct=EBI-3989070, EBI-475981;
P06213:INSR (xeno); NbExp=5; IntAct=EBI-3989070, EBI-475899;
A1S3N8:Sama_0787 (xeno); NbExp=2; IntAct=EBI-3989070, EBI-7016414;
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
century - Issue 9 of April 2001;
URL="http://web.expasy.org/spotlight/back_issues/009";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M54979; AAA30722.1; -; mRNA.
PIR; A40909; IPBO.
UniGene; Bt.453; -.
PDB; 1APH; X-ray; 2.00 A; A=85-105, B=25-54.
PDB; 1BPH; X-ray; 2.00 A; A=85-105, B=25-54.
PDB; 1CPH; X-ray; 1.90 A; A=85-105, B=25-54.
PDB; 1DPH; X-ray; 1.90 A; A=85-105, B=25-54.
PDB; 1HO0; NMR; -; A=25-54.
PDB; 1PID; X-ray; 1.30 A; A/C=85-105, B/D=25-49.
PDB; 2A3G; X-ray; 2.25 A; A/C=85-105, B/D=25-54.
PDB; 2BN1; X-ray; 1.40 A; A=85-105, B=25-54.
PDB; 2BN3; X-ray; 1.40 A; A=85-105, B=25-54.
PDB; 2INS; X-ray; 2.50 A; A/C=85-105, B/D=26-54.
PDB; 2ZP6; X-ray; 2.56 A; A/C=85-105, B/D=25-54.
PDB; 4BS3; X-ray; 2.30 A; A=85-105, B=25-54.
PDB; 4E7T; X-ray; 1.40 A; A/C=85-105, B/D=25-54.
PDB; 4E7U; X-ray; 1.30 A; A/C=85-105, B/D=25-54.
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.
PDB; 4I5Y; X-ray; 1.80 A; A=85-105, B=25-54.
PDB; 4I5Z; X-ray; 1.80 A; A=85-105, B=25-54.
PDB; 4IDW; X-ray; 2.70 A; A/C=85-105, B/D=25-54.
PDB; 4IHN; X-ray; 1.16 A; A=85-105, B=25-54.
PDB; 4M4F; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
PDB; 4M4H; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
PDB; 4M4I; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
PDB; 4M4J; X-ray; 1.90 A; A/C=85-105, B/D=25-54.
PDB; 4M4L; X-ray; 1.45 A; A/C=85-105, B/D=25-54.
PDB; 4M4M; X-ray; 1.50 A; A/C=85-105, B/D=25-54.
PDB; 5AZZ; X-ray; 1.45 A; A=85-105, B=25-54.
PDB; 5KQV; X-ray; 4.40 A; A/I=85-105, B/J=25-54.
PDB; 5MIZ; NMR; -; A=85-105, B=25-54.
PDBsum; 1APH; -.
PDBsum; 1BPH; -.
PDBsum; 1CPH; -.
PDBsum; 1DPH; -.
PDBsum; 1HO0; -.
PDBsum; 1PID; -.
PDBsum; 2A3G; -.
PDBsum; 2BN1; -.
PDBsum; 2BN3; -.
PDBsum; 2INS; -.
PDBsum; 2ZP6; -.
PDBsum; 4BS3; -.
PDBsum; 4E7T; -.
PDBsum; 4E7U; -.
PDBsum; 4E7V; -.
PDBsum; 4I5Y; -.
PDBsum; 4I5Z; -.
PDBsum; 4IDW; -.
PDBsum; 4IHN; -.
PDBsum; 4M4F; -.
PDBsum; 4M4H; -.
PDBsum; 4M4I; -.
PDBsum; 4M4J; -.
PDBsum; 4M4L; -.
PDBsum; 4M4M; -.
PDBsum; 5AZZ; -.
PDBsum; 5KQV; -.
PDBsum; 5MIZ; -.
ProteinModelPortal; P01317; -.
SMR; P01317; -.
DIP; DIP-52901N; -.
IntAct; P01317; 5.
STRING; 9913.ENSBTAP00000017289; -.
Allergome; 2118; Bos d Insulin.
PaxDb; P01317; -.
eggNOG; ENOG410J0XC; Eukaryota.
eggNOG; ENOG4111VJB; LUCA.
HOGENOM; HOG000261669; -.
HOVERGEN; HBG006137; -.
InParanoid; P01317; -.
EvolutionaryTrace; P01317; -.
PMAP-CutDB; P01317; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005158; F:insulin receptor binding; IDA:AgBase.
GO; GO:0035938; P:estradiol secretion; IDA:AgBase.
GO; GO:0007631; P:feeding behavior; IDA:AgBase.
GO; GO:0044381; P:glucose import in response to insulin stimulus; IDA:AgBase.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:AgBase.
GO; GO:0032099; P:negative regulation of appetite; IDA:AgBase.
GO; GO:1903488; P:negative regulation of lactation; IDA:AgBase.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:AgBase.
GO; GO:1903524; P:positive regulation of blood circulation; IDA:AgBase.
GO; GO:1903431; P:positive regulation of cell maturation; IDA:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0032024; P:positive regulation of insulin secretion; IDA:AgBase.
GO; GO:1903489; P:positive regulation of lactation; IDA:AgBase.
GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IDA:AgBase.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:AgBase.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:AgBase.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:AgBase.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:AgBase.
GO; GO:0009306; P:protein secretion; IMP:AgBase.
GO; GO:1903544; P:response to butyrate; IDA:AgBase.
GO; GO:0032094; P:response to food; IDA:AgBase.
GO; GO:0009749; P:response to glucose; IMP:AgBase.
GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
GO; GO:0009408; P:response to heat; IDA:AgBase.
GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
GO; GO:0031667; P:response to nutrient levels; IDA:AgBase.
Gene3D; 1.10.100.10; -; 1.
InterPro; IPR004825; Insulin.
InterPro; IPR016179; Insulin-like.
InterPro; IPR022353; Insulin_CS.
InterPro; IPR022352; Insulin_family.
Pfam; PF00049; Insulin; 1.
PRINTS; PR00277; INSULIN.
PRINTS; PR00276; INSULINFAMLY.
SMART; SM00078; IlGF; 1.
SUPFAM; SSF56994; SSF56994; 1.
PROSITE; PS00262; INSULIN; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glucose metabolism;
Hormone; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:13249947,
ECO:0000269|PubMed:14886311,
ECO:0000269|PubMed:4928892}.
PEPTIDE 25 54 Insulin B chain.
{ECO:0000269|PubMed:2456452}.
/FTId=PRO_0000015764.
PROPEP 57 82 C peptide.
/FTId=PRO_0000015765.
PEPTIDE 85 105 Insulin A chain.
{ECO:0000269|PubMed:2456452}.
/FTId=PRO_0000015766.
DISULFID 31 91 Interchain (between B and A chains).
{ECO:0000269|PubMed:13249947}.
DISULFID 43 104 Interchain (between B and A chains).
{ECO:0000269|PubMed:13249947}.
DISULFID 90 95 {ECO:0000269|PubMed:13249947,
ECO:0000269|PubMed:4928892}.
HELIX 33 43 {ECO:0000244|PDB:4IHN}.
HELIX 44 46 {ECO:0000244|PDB:4IHN}.
STRAND 48 50 {ECO:0000244|PDB:4E7U}.
HELIX 86 90 {ECO:0000244|PDB:4IHN}.
TURN 91 94 {ECO:0000244|PDB:4IHN}.
HELIX 97 101 {ECO:0000244|PDB:4IHN}.
SEQUENCE 105 AA; 11393 MW; 75307CF78E61C06A CRC64;
MALWTRLRPL LALLALWPPP PARAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG
PQVGALELAG GPGAGGLEGP PQKRGIVEQC CASVCSLYQL ENYCN


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