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 22-JUL-2008, entry version 98. 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; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88288209; PubMed=2456452; 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 RT deoxyribonucleic acid for bovine preproinsulin."; RL Mol. Endocrinol. 1:327-331(1987). RN [2] RP PROTEIN SEQUENCE OF 25-105. RX MEDLINE=71166442; PubMed=4928892; 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; 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 MEDLINE=71116409; PubMed=5545080; RA Steiner D.F., Cho S., Oyer P.E., Terris S., Peterson J.D., RA 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 MEDLINE=71257721; PubMed=5105368; 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; 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; 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 MEDLINE=97285914; PubMed=9141131; RX DOI=10.1002/(SICI)1097-0134(199704)27:4<507::AID-PROT4>3.3.CO;2-H; 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 RT of a monomeric insulin (despentapeptide insulin)."; RL Proteins 27:507-516(1997). 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. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th CC century - Issue 9 of April 2001; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt009.shtml"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M54979; AAA30722.1; -; mRNA. DR PIR; A40909; IPBO. DR RefSeq; NP_776351.1; -. DR UniGene; Bt.453; -. 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 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 SMR; P01317; 25-105. DR Ensembl; ENSBTAG00000013003; Bos taurus. DR GeneID; 280829; -. DR KEGG; bta:280829; -. DR HOVERGEN; P01317; -. DR LinkHub; P01317; -. DR InterPro; IPR004825; Ins/IGF/relaxin. 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 3D-structure; Carbohydrate metabolism; KW Cleavage on pair of basic residues; Direct protein sequencing; KW Glucose metabolism; Hormone; Secreted; Signal. FT SIGNAL 1 24 FT PEPTIDE 25 54 Insulin B chain. FT /FTId=PRO_0000015764. FT PROPEP 57 82 C peptide. FT /FTId=PRO_0000015765. FT PEPTIDE 85 105 Insulin A chain. FT /FTId=PRO_0000015766. FT DISULFID 31 91 Interchain (between B and A chains). FT DISULFID 43 104 Interchain (between B and A chains). FT DISULFID 90 95 FT HELIX 32 43 FT HELIX 44 46 FT HELIX 86 90 FT HELIX 97 101 SQ SEQUENCE 105 AA; 11393 MW; 75307CF78E61C06A CRC64; MALWTRLRPL LALLALWPPP PARAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREVEG PQVGALELAG GPGAGGLEGP PQKRGIVEQC CASVCSLYQL ENYCN //