ID COL_PIG Reviewed; 112 AA. AC P02703; Q3I5G6; Q9N1T6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 3. DT 22-JUL-2008, entry version 70. DE RecName: Full=Colipase; DE AltName: Full=Procolipase II; DE Flags: Precursor; GN Name=CLPS; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pancreas; RX MEDLINE=99192816; PubMed=10092856; RA Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., RA Chaix J.-C., Guo X.-J.; RT "Cloning, sequencing and functional expression of a cDNA encoding RT porcine pancreatic preprocarboxypeptidase A1."; RL Eur. J. Biochem. 259:719-725(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Pan G., Liu Y.G., Xiong Y.Z.; RT "Polymorphism of Sus scrofa gene encoding pancreatic colipase."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 18-112. RX MEDLINE=84104937; PubMed=6691986; DOI=10.1016/0167-4838(84)90175-4; RA Sternby B., Engstroem A., Hellman U., Vihert A.M., Sternby N.-H., RA Borgstroem B.; RT "The primary sequence of human pancreatic colipase."; RL Biochim. Biophys. Acta 784:75-80(1984). RN [4] RP PROTEIN SEQUENCE OF 23-108. RX MEDLINE=74290109; PubMed=4858821; RA Charles M., Erlanson C., Bianchetta J.D., Joffre J., Guidoni A.A., RA Rovery M.; RT "The primary structure of porcine colipase II. I. The amino acid RT sequence."; RL Biochim. Biophys. Acta 359:186-197(1974). RN [5] RP DISULFIDE BONDS. RX MEDLINE=74290110; PubMed=4603223; RA Erlanson C., Charles M., Astier M., Desnuelle P.; RT "The primary structure of porcine colipase II. II. The disulfide RT bridges."; RL Biochim. Biophys. Acta 359:198-203(1974). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-112 IN COMPLEX WITH PNLIP. RX MEDLINE=92396238; PubMed=1522902; DOI=10.1038/359159a0; RA van Tilbeurgh H., Sarda L., Verger R., Cambillau C.; RT "Structure of the pancreatic lipase-procolipase complex."; RL Nature 359:159-162(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP. RX MEDLINE=93241293; PubMed=8479519; DOI=10.1038/362814a0; RA van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., RA Cambillau C.; RT "Interfacial activation of the lipase-procolipase complex by mixed RT micelles revealed by X-ray crystallography."; RL Nature 362:814-820(1993). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP, RP AND DISULFIDE BONDS. RX MEDLINE=95291181; PubMed=7773176; RA Egloff M.-P., Sarda L., Verger R., Cambillau C., van Tilbeurgh H.; RT "Crystallographic study of the structure of colipase and of the RT interaction with pancreatic lipase."; RL Protein Sci. 4:44-57(1995). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP. RX MEDLINE=96279347; PubMed=8663362; DOI=10.1074/jbc.271.30.18007; RA Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C., RA Fontecilla-Camps J.-C.; RT "Lipase activation by nonionic detergents. The crystal structure of RT the porcine lipase-colipase-tetraethylene glycol monooctyl ether RT complex."; RL J. Biol. Chem. 271:18007-18016(1996). RN [10] RP STRUCTURE BY NMR OF 18-110, AND SEQUENCE REVISION TO 54. RX MEDLINE=95172049; PubMed=7867624; RA Breg J.N., Sarda L., Cozzone P.J., Rugani N., Boelens R., Kaptein R.; RT "Solution structure of porcine pancreatic procolipase as determined RT from 1H homonuclear two-dimensional and three-dimensional NMR."; RL Eur. J. Biochem. 227:663-672(1995). CC -!- FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows CC the lipase to anchor itself to the lipid-water interface. Without CC colipase the enzyme is washed off by bile salts, which have an CC inhibitory effect on the lipase. CC -!- FUNCTION: Enterostatin has a biological activity as a satiety CC signal. CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic CC lipase. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the pancreas. CC -!- SIMILARITY: Belongs to the colipase family. 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; AF148567; AAF67823.1; -; mRNA. DR EMBL; DQ073448; AAZ22441.1; -; Genomic_DNA. DR PIR; A03162; XLPG2. DR RefSeq; NP_999368.1; -. DR UniGene; Ssc.514; -. DR PDB; 1ETH; X-ray; 2.80 A; B/D=18-110. DR PDB; 1LPA; X-ray; 3.04 A; A=18-110. DR PDB; 1LPB; X-ray; 2.46 A; A=18-110. DR PDB; 1N8S; X-ray; 3.04 A; C=18-110. DR PDB; 1PCN; NMR; -; A=18-110. DR PDB; 1PCO; NMR; -; A=18-110. DR PDBsum; 1ETH; -. DR PDBsum; 1LPA; -. DR PDBsum; 1LPB; -. DR PDBsum; 1N8S; -. DR PDBsum; 1PCN; -. DR PDBsum; 1PCO; -. DR GeneID; 397407; -. DR KEGG; ssc:397407; -. DR HOVERGEN; P02703; -. DR LinkHub; P02703; -. DR InterPro; IPR001981; Colipase. DR Pfam; PF01114; Colipase; 1. DR Pfam; PF02740; Colipase_C; 1. DR PRINTS; PR00128; COLIPASE. DR SMART; SM00023; COLIPASE; 1. DR PROSITE; PS00121; COLIPASE_1; 1. DR PROSITE; PS51342; COLIPASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Digestion; Direct protein sequencing; Lipid degradation; KW Secreted; Signal. FT SIGNAL 1 17 FT PROPEP 18 22 Enterostatin, activation peptide. FT /FTId=PRO_0000005702. FT CHAIN 23 112 Colipase. FT /FTId=PRO_0000005703. FT DISULFID 34 45 FT DISULFID 40 56 FT DISULFID 44 78 FT DISULFID 66 86 FT DISULFID 80 104 FT CONFLICT 54 54 Missing (in Ref. 4; AA sequence). FT CONFLICT 67 67 Missing (in Ref. 4; AA sequence). FT CONFLICT 106 106 D -> N (in Ref. 3 and 4). FT CONFLICT 111 112 SD -> DS (in Ref. 3; AA sequence). FT HELIX 37 39 FT STRAND 40 43 FT STRAND 48 52 FT STRAND 64 67 FT STRAND 71 77 FT STRAND 84 88 FT HELIX 92 97 FT STRAND 101 106 SQ SEQUENCE 112 AA; 12140 MW; AE0AE89956E5A846 CRC64; MEKVLALLLV TLTVAYAVPD PRGIIINLDE GELCLNSAQC KSNCCQHDTI LSLSRCALKA RENSECSAFT LYGVYYKCPC ERGLTCEGDK SLVGSITNTN FGICHDVGRS SD //