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UniProtKB/Swiss-Prot entry P02703


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COL_PIG
Primary accession number P02703
Secondary accession numbers Q3I5G6 Q9N1T6
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on October 25, 2002 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 70)
Name and origin of the protein
Protein name Colipase [Precursor]
Synonym Procolipase II
Gene name
Name: CLPS
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pancreas;
PubMed=10092856 [NCBI, ExPASy, EBI, Israel, Japan]
Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., Chaix J.-C., Guo X.-J.;
"Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1.";
Eur. J. Biochem. 259:719-725(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Pan G., Liu Y.G., Xiong Y.Z.;
"Polymorphism of Sus scrofa gene encoding pancreatic colipase.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 18-112.
DOI=10.1016/0167-4838(84)90175-4; PubMed=6691986 [NCBI, ExPASy, EBI, Israel, Japan]
Sternby B., Engstroem A., Hellman U., Vihert A.M., Sternby N.-H., Borgstroem B.;
"The primary sequence of human pancreatic colipase.";
Biochim. Biophys. Acta 784:75-80(1984).
[4]
PROTEIN SEQUENCE OF 23-108.
PubMed=4858821 [NCBI, ExPASy, EBI, Israel, Japan]
Charles M., Erlanson C., Bianchetta J.D., Joffre J., Guidoni A.A., Rovery M.;
"The primary structure of porcine colipase II. I. The amino acid sequence.";
Biochim. Biophys. Acta 359:186-197(1974).
[5]
DISULFIDE BONDS.
PubMed=4603223 [NCBI, ExPASy, EBI, Israel, Japan]
Erlanson C., Charles M., Astier M., Desnuelle P.;
"The primary structure of porcine colipase II. II. The disulfide bridges.";
Biochim. Biophys. Acta 359:198-203(1974).
[6]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-112 IN COMPLEX WITH PNLIP.
DOI=10.1038/359159a0; PubMed=1522902 [NCBI, ExPASy, EBI, Israel, Japan]
van Tilbeurgh H., Sarda L., Verger R., Cambillau C.;
"Structure of the pancreatic lipase-procolipase complex.";
Nature 359:159-162(1992).
[7]
X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
DOI=10.1038/362814a0; PubMed=8479519 [NCBI, ExPASy, EBI, Israel, Japan]
van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C.;
"Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography.";
Nature 362:814-820(1993).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP, AND DISULFIDE BONDS.
PubMed=7773176 [NCBI, ExPASy, EBI, Israel, Japan]
Egloff M.-P., Sarda L., Verger R., Cambillau C., van Tilbeurgh H.;
"Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase.";
Protein Sci. 4:44-57(1995).
[9]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
DOI=10.1074/jbc.271.30.18007; PubMed=8663362 [NCBI, ExPASy, EBI, Israel, Japan]
Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C., Fontecilla-Camps J.-C.;
"Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex.";
J. Biol. Chem. 271:18007-18016(1996).
[10]
STRUCTURE BY NMR OF 18-110, AND SEQUENCE REVISION TO 54.
PubMed=7867624 [NCBI, ExPASy, EBI, Israel, Japan]
Breg J.N., Sarda L., Cozzone P.J., Rugani N., Boelens R., Kaptein R.;
"Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR.";
Eur. J. Biochem. 227:663-672(1995).
Comments
  • FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase.
  • FUNCTION: Enterostatin has a biological activity as a satiety signal.
  • SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the pancreas.
  • SIMILARITY: Belongs to the colipase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF148567; AAF67823.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ073448; AAZ22441.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A03162; XLPG2.
RefSeq NP_999368.1; -.
UniGene Ssc.514
3D structure databases
PDB
1ETH; X-ray; 2.80 A; B/D=18-110.[ExPASy / RCSB / EBI]
1LPA; X-ray; 3.04 A; A=18-110.[ExPASy / RCSB / EBI]
1LPB; X-ray; 2.46 A; A=18-110.[ExPASy / RCSB / EBI]
1N8S; X-ray; 3.04 A; C=18-110.[ExPASy / RCSB / EBI]
1PCN; NMR; -; A=18-110.[ExPASy / RCSB / EBI]
1PCO; NMR; -; A=18-110.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ETH; -.
1LPA; -.
1LPB; -.
1N8S; -.
1PCN; -.
1PCO; -.
ModBase P02703.
Family and domain databases
InterPro IPR001981; Colipase.
Graphical view of domain structure.
Pfam PF01114; Colipase; 1.
PF02740; Colipase_C; 1.
Pfam graphical view of domain structure.
PRINTS PR00128; COLIPASE.
SMART SM00023; COLIPASE; 1.
SMART graphical view of domain structure.
PROSITE PS00121; COLIPASE_1; 1.
PS51342; COLIPASE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P02703.
Genome annotation databases
GeneID 397407; -.
KEGG ssc:397407; -.
Phylogenomic databases
HOVERGEN P02703; -.
Other
LinkHub P02703; -.
ProtoNet P02703.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Digestion; Direct protein sequencing; Lipid degradation; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17      
PROPEP   18    22  5     Enterostatin, activation peptide. PRO_0000005702
CHAIN   23   112  90     Colipase. PRO_0000005703
DISULFID   34    45         
DISULFID   40    56         
DISULFID   44    78         
DISULFID   66    86         
DISULFID   80   104         
CONFLICT   54    54        Missing (in Ref. 4; AA sequence). 
CONFLICT   67    67        Missing (in Ref. 4; AA sequence). 
CONFLICT   106   106        D -> N (in Ref. 3 and 4). 
CONFLICT   111   112        SD -> DS (in Ref. 3; AA sequence). 
HELIX   37    39  3      
STRAND   40    43  4      
STRAND   48    52  5      
STRAND   64    67  4      
STRAND   71    77  7      
STRAND   84    88  5      
HELIX   92    97  6      
STRAND   101   106  6      
Sequence information
Length: 112 AA [This is the length of the unprocessed precursor] Molecular weight: 12140 Da [This is the MW of the unprocessed precursor] CRC64: AE0AE89956E5A846 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEKVLALLLV TLTVAYAVPD PRGIIINLDE GELCLNSAQC KSNCCQHDTI LSLSRCALKA 

        70         80         90        100        110 
RENSECSAFT LYGVYYKCPC ERGLTCEGDK SLVGSITNTN FGICHDVGRS SD 

P02703 in FASTA format

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View entry in raw text format (no links)
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