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Protein

Colipase

Gene

CLPS

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
Enterostatin has a biological activity as a satiety signal.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Digestion, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-SSC-192456. Digestion of dietary lipid.
R-SSC-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Colipase
Alternative name(s):
Procolipase II
Gene namesi
Name:CLPS
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Propeptidei18 – 225Enterostatin, activation peptide1 PublicationPRO_0000005702
Chaini23 – 11290ColipasePRO_0000005703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 45
Disulfide bondi40 ↔ 56
Disulfide bondi44 ↔ 78
Disulfide bondi66 ↔ 86
Disulfide bondi80 ↔ 104

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP02703.

Expressioni

Tissue specificityi

Expressed by the pancreas.

Gene expression databases

GenevisibleiP02703. SS.

Interactioni

Subunit structurei

Forms a 1:1 stoichiometric complex with pancreatic lipase.PROSITE-ProRule annotation4 Publications

Protein-protein interaction databases

MINTiMINT-1179431.
STRINGi9823.ENSSSCP00000001686.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 284Combined sources
Beta strandi30 – 334Combined sources
Helixi37 – 393Combined sources
Beta strandi40 – 434Combined sources
Beta strandi48 – 525Combined sources
Beta strandi64 – 674Combined sources
Beta strandi71 – 777Combined sources
Beta strandi84 – 885Combined sources
Helixi92 – 976Combined sources
Beta strandi101 – 1066Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ETHX-ray2.80B/D18-110[»]
1LPAX-ray3.04A18-110[»]
1LPBX-ray2.46A18-110[»]
1N8SX-ray3.04C18-110[»]
1PCNNMR-A18-110[»]
1PCONMR-A18-110[»]
ProteinModelPortaliP02703.
SMRiP02703. Positions 18-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02703.

Family & Domainsi

Sequence similaritiesi

Belongs to the colipase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IYZJ. Eukaryota.
ENOG410YQC6. LUCA.
GeneTreeiENSGT00390000012644.
HOGENOMiHOG000059253.
HOVERGENiHBG005373.
InParanoidiP02703.
KOiK14460.
OMAiCSAKTLY.
OrthoDBiEOG74N5K5.
TreeFamiTF336178.

Family and domain databases

InterProiIPR001981. Colipase.
IPR017914. Colipase_C.
IPR017915. Colipase_CS.
IPR017913. Colipase_N.
[Graphical view]
PANTHERiPTHR10041. PTHR10041. 1 hit.
PfamiPF01114. Colipase. 1 hit.
PF02740. Colipase_C. 1 hit.
[Graphical view]
PRINTSiPR00128. COLIPASE.
SMARTiSM00023. COLIPASE. 1 hit.
[Graphical view]
PROSITEiPS00121. COLIPASE_1. 1 hit.
PS51342. COLIPASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02703-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKVLALLLV TLTVAYAVPD PRGIIINLDE GELCLNSAQC KSNCCQHDTI
60 70 80 90 100
LSLSRCALKA RENSECSAFT LYGVYYKCPC ERGLTCEGDK SLVGSITNTN
110
FGICHDVGRS SD
Length:112
Mass (Da):12,140
Last modified:October 25, 2002 - v3
Checksum:iAE0AE89956E5A846
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541Missing AA sequence (PubMed:4858821).Curated
Sequence conflicti67 – 671Missing AA sequence (PubMed:4858821).Curated
Sequence conflicti106 – 1061D → N AA sequence (PubMed:6691986).Curated
Sequence conflicti106 – 1061D → N AA sequence (PubMed:4858821).Curated
Sequence conflicti111 – 1122SD → DS AA sequence (PubMed:6691986).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148567 mRNA. Translation: AAF67823.1.
DQ073448 Genomic DNA. Translation: AAZ22441.1.
PIRiA03162. XLPG2.
RefSeqiNP_999368.1. NM_214203.1.
XP_013833274.1. XM_013977820.1.
XP_013833275.1. XM_013977821.1.
XP_013833276.1. XM_013977822.1.
UniGeneiSsc.514.

Genome annotation databases

EnsembliENSSSCT00000001730; ENSSSCP00000001686; ENSSSCG00000001552.
GeneIDi397407.
KEGGissc:397407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148567 mRNA. Translation: AAF67823.1.
DQ073448 Genomic DNA. Translation: AAZ22441.1.
PIRiA03162. XLPG2.
RefSeqiNP_999368.1. NM_214203.1.
XP_013833274.1. XM_013977820.1.
XP_013833275.1. XM_013977821.1.
XP_013833276.1. XM_013977822.1.
UniGeneiSsc.514.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ETHX-ray2.80B/D18-110[»]
1LPAX-ray3.04A18-110[»]
1LPBX-ray2.46A18-110[»]
1N8SX-ray3.04C18-110[»]
1PCNNMR-A18-110[»]
1PCONMR-A18-110[»]
ProteinModelPortaliP02703.
SMRiP02703. Positions 18-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1179431.
STRINGi9823.ENSSSCP00000001686.

Proteomic databases

PaxDbiP02703.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000001730; ENSSSCP00000001686; ENSSSCG00000001552.
GeneIDi397407.
KEGGissc:397407.

Organism-specific databases

CTDi1208.

Phylogenomic databases

eggNOGiENOG410IYZJ. Eukaryota.
ENOG410YQC6. LUCA.
GeneTreeiENSGT00390000012644.
HOGENOMiHOG000059253.
HOVERGENiHBG005373.
InParanoidiP02703.
KOiK14460.
OMAiCSAKTLY.
OrthoDBiEOG74N5K5.
TreeFamiTF336178.

Enzyme and pathway databases

ReactomeiR-SSC-192456. Digestion of dietary lipid.
R-SSC-975634. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTraceiP02703.

Gene expression databases

GenevisibleiP02703. SS.

Family and domain databases

InterProiIPR001981. Colipase.
IPR017914. Colipase_C.
IPR017915. Colipase_CS.
IPR017913. Colipase_N.
[Graphical view]
PANTHERiPTHR10041. PTHR10041. 1 hit.
PfamiPF01114. Colipase. 1 hit.
PF02740. Colipase_C. 1 hit.
[Graphical view]
PRINTSiPR00128. COLIPASE.
SMARTiSM00023. COLIPASE. 1 hit.
[Graphical view]
PROSITEiPS00121. COLIPASE_1. 1 hit.
PS51342. COLIPASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1."
    Darnis S., Juge N., Marino C., Aviles F.X., Puigserver A., Chaix J.-C., Guo X.-J.
    Eur. J. Biochem. 259:719-725(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  2. "Polymorphism of Sus scrofa gene encoding pancreatic colipase."
    Pan G., Liu Y.G., Xiong Y.Z.
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: PROTEIN SEQUENCE OF 18-112.
  4. "The primary structure of porcine colipase II. I. The amino acid sequence."
    Charles M., Erlanson C., Bianchetta J.D., Joffre J., Guidoni A.A., Rovery M.
    Biochim. Biophys. Acta 359:186-197(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-108.
  5. "The primary structure of porcine colipase II. II. The disulfide bridges."
    Erlanson C., Charles M., Astier M., Desnuelle P.
    Biochim. Biophys. Acta 359:198-203(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  6. "Structure of the pancreatic lipase-procolipase complex."
    van Tilbeurgh H., Sarda L., Verger R., Cambillau C.
    Nature 359:159-162(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-112 IN COMPLEX WITH PNLIP.
  7. "Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography."
    van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R., Cambillau C.
    Nature 362:814-820(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
  8. "Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase."
    Egloff M.-P., Sarda L., Verger R., Cambillau C., van Tilbeurgh H.
    Protein Sci. 4:44-57(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP, DISULFIDE BONDS.
  9. "Lipase activation by nonionic detergents. The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex."
    Hermoso J., Pignol D., Kerfelec B., Crenon I., Chapus C., Fontecilla-Camps J.-C.
    J. Biol. Chem. 271:18007-18016(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-95 IN COMPLEX WITH PNLIP.
  10. "Solution structure of porcine pancreatic procolipase as determined from 1H homonuclear two-dimensional and three-dimensional NMR."
    Breg J.N., Sarda L., Cozzone P.J., Rugani N., Boelens R., Kaptein R.
    Eur. J. Biochem. 227:663-672(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 18-110, SEQUENCE REVISION TO 54.

Entry informationi

Entry nameiCOL_PIG
AccessioniPrimary (citable) accession number: P02703
Secondary accession number(s): Q3I5G6, Q9N1T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2002
Last modified: July 6, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.