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P04118 (COL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Colipase
Gene names
Name:CLPS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length112 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Enterostatin has a biological activity as a satiety signal.

Subunit structure

Forms a 1:1 stoichiometric complex with pancreatic lipase.

Subcellular location

Secreted.

Tissue specificity

Expressed by the pancreas.

Polymorphism

Variant Cys-109 is statistically significantly associated with an increased risk of type 2 diabetes.

Sequence similarities

Belongs to the colipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Propeptide18 – 225Enterostatin, activation peptide Potential
PRO_0000005696
Chain23 – 11290Colipase
PRO_0000005697

Amino acid modifications

Disulfide bond34 ↔ 45 By similarity
Disulfide bond40 ↔ 56 By similarity
Disulfide bond44 ↔ 78 By similarity
Disulfide bond66 ↔ 86 By similarity
Disulfide bond80 ↔ 104 By similarity

Natural variations

Natural variant81L → P.
Corresponds to variant rs2766597 [ dbSNP | Ensembl ].
VAR_053040
Natural variant1091R → C. Ref.10
Corresponds to variant rs41270082 [ dbSNP | Ensembl ].
VAR_047105

Sequences

Sequence LengthMass (Da)Tools
P04118 [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 772872EBBE7C4DF8

FASTA11211,954
        10         20         30         40         50         60 
MEKILILLLV ALSVAYAAPG PRGIIINLEN GELCMNSAQC KSNCCQHSSA LGLARCTSMA 

        70         80         90        100        110 
SENSECSVKT LYGIYYKCPC ERGLTCEGDK TIVGSITNTN FGICHDAGRS KQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the human colipase cDNA."
Lowe M.E., Rosenblum J.L., McEwen P., Strauss A.W.
Biochemistry 29:823-828(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The human colipase gene: isolation, chromosomal location, and tissue-specific expression."
Sims H.F., Lowe M.E.
Biochemistry 31:7120-7125(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[7]"Structure of human pancreatic colipase gene (CLPS)."
Reichwald K., Petz U., Platzer M.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-112.
Tissue: Pancreas.
[8]"The primary sequence of human pancreatic colipase."
Sternby B., Engstroem A., Hellman U., Vihert A.M., Sternby N.-H., Borgstroem B.
Biochim. Biophys. Acta 784:75-80(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-108.
Tissue: Pancreas.
[9]"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 (3.0 ANGSTROMS).
[10]"Putative association between a new polymorphism in exon 3 (Arg109Cys) of the pancreatic colipase gene and type 2 diabetes mellitus in two independent Caucasian study populations."
Lindner I., Helwig U., Rubin D., Li Y., Fisher E., Boeing H., Mohlig M., Spranger J., Pfeiffer A., Hampe J., Schreiber S., Doring F., Schrezenmeir J.
Mol. Nutr. Food Res. 49:972-976(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-109, ASSOCIATION WITH TYPE 2 DIABETES.
+Additional computationally mapped references.

Web resources

Wikipedia

Colipase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02883 mRNA. Translation: AAA52054.1.
M95529 Genomic DNA. Translation: AAB05818.1.
BT006812 mRNA. Translation: AAP35458.1.
AL157823 Genomic DNA. Translation: CAI21642.1.
CH471081 Genomic DNA. Translation: EAX03850.1.
BC007061 mRNA. Translation: AAH07061.1.
BC017897 mRNA. Translation: AAH17897.1.
AY780648 mRNA. Translation: AAV35728.1.
PIRXLHU. A42568.
RefSeqNP_001823.1. NM_001832.3.
UniGeneHs.1340.

3D structure databases

ProteinModelPortalP04118.
SMRP04118. Positions 21-106.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000259938.

PTM databases

PhosphoSiteP04118.

Polymorphism databases

DMDM116900.

Proteomic databases

PaxDbP04118.
PeptideAtlasP04118.
PRIDEP04118.

Protocols and materials databases

DNASU1208.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259938; ENSP00000259938; ENSG00000137392.
GeneID1208.
KEGGhsa:1208.
UCSCuc003ole.2. human.

Organism-specific databases

CTD1208.
GeneCardsGC06M035765.
HGNCHGNC:2085. CLPS.
HPAHPA010512.
MIM120105. gene.
neXtProtNX_P04118.
PharmGKBPA26611.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42456.
HOGENOMHOG000059253.
HOVERGENHBG005373.
InParanoidP04118.
KOK14460.
OMACSAKTLY.
OrthoDBEOG74N5K5.
PhylomeDBP04118.
TreeFamTF336178.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeP04118.
CleanExHS_CLPS.
GenevestigatorP04118.

Family and domain databases

InterProIPR001981. Colipase.
IPR017914. Colipase_C.
IPR017915. Colipase_CS.
IPR017913. Colipase_N.
[Graphical view]
PANTHERPTHR10041. PTHR10041. 1 hit.
PfamPF01114. Colipase. 1 hit.
PF02740. Colipase_C. 1 hit.
[Graphical view]
PRINTSPR00128. COLIPASE.
SMARTSM00023. COLIPASE. 1 hit.
[Graphical view]
PROSITEPS00121. COLIPASE_1. 1 hit.
PS51342. COLIPASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiColipase.
GenomeRNAi1208.
NextBio4977.
PMAP-CutDBP04118.
PROP04118.
SOURCESearch...

Entry information

Entry nameCOL_HUMAN
AccessionPrimary (citable) accession number: P04118
Secondary accession number(s): Q5T9G7, Q5U809
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM