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P04118

- COL_HUMAN

UniProt

P04118 - COL_HUMAN

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Protein
Colipase
Gene
CLPS
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. enzyme activator activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. lipid digestion Source: Reactome
  3. lipid metabolic process Source: ProtInc
  4. phototransduction, visible light Source: Reactome
  5. retinoid metabolic process Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Digestion, Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiREACT_24968. Retinoid metabolism and transport.
REACT_9518. Digestion of dietary lipid.

Names & Taxonomyi

Protein namesi
Recommended name:
Colipase
Gene namesi
Name:CLPS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2085. CLPS.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

PharmGKBiPA26611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717
Add
BLAST
Propeptidei18 – 225Enterostatin, activation peptide Reviewed prediction
PRO_0000005696
Chaini23 – 11290Colipase
PRO_0000005697Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP04118.
PeptideAtlasiP04118.
PRIDEiP04118.

PTM databases

PhosphoSiteiP04118.

Miscellaneous databases

PMAP-CutDBP04118.

Expressioni

Tissue specificityi

Expressed by the pancreas.

Gene expression databases

BgeeiP04118.
CleanExiHS_CLPS.
GenevestigatoriP04118.

Organism-specific databases

HPAiHPA010512.

Interactioni

Subunit structurei

Forms a 1:1 stoichiometric complex with pancreatic lipase.

Protein-protein interaction databases

STRINGi9606.ENSP00000259938.

Structurei

3D structure databases

ProteinModelPortaliP04118.
SMRiP04118. Positions 21-106.

Family & Domainsi

Sequence similaritiesi

Belongs to the colipase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42456.
HOGENOMiHOG000059253.
HOVERGENiHBG005373.
InParanoidiP04118.
KOiK14460.
OMAiCSAKTLY.
OrthoDBiEOG74N5K5.
PhylomeDBiP04118.
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.

P04118-1 [UniParc]FASTAAdd to Basket

« Hide

MEKILILLLV ALSVAYAAPG PRGIIINLEN GELCMNSAQC KSNCCQHSSA    50
LGLARCTSMA SENSECSVKT LYGIYYKCPC ERGLTCEGDK TIVGSITNTN 100
FGICHDAGRS KQ 112
Length:112
Mass (Da):11,954
Last modified:April 1, 1990 - v2
Checksum:i772872EBBE7C4DF8
GO

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81L → P.
Corresponds to variant rs2766597 [ dbSNP | Ensembl ].
VAR_053040
Natural varianti109 – 1091R → C.1 Publication
Corresponds to variant rs41270082 [ dbSNP | Ensembl ].
VAR_047105

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4811.1.
PIRiA42568. XLHU.
RefSeqiNP_001823.1. NM_001832.3.
UniGeneiHs.1340.

Genome annotation databases

EnsembliENST00000259938; ENSP00000259938; ENSG00000137392.
GeneIDi1208.
KEGGihsa:1208.
UCSCiuc003ole.2. human.

Polymorphism databases

DMDMi116900.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Colipase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4811.1.
PIRi A42568. XLHU.
RefSeqi NP_001823.1. NM_001832.3.
UniGenei Hs.1340.

3D structure databases

ProteinModelPortali P04118.
SMRi P04118. Positions 21-106.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000259938.

PTM databases

PhosphoSitei P04118.

Polymorphism databases

DMDMi 116900.

Proteomic databases

PaxDbi P04118.
PeptideAtlasi P04118.
PRIDEi P04118.

Protocols and materials databases

DNASUi 1208.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259938 ; ENSP00000259938 ; ENSG00000137392 .
GeneIDi 1208.
KEGGi hsa:1208.
UCSCi uc003ole.2. human.

Organism-specific databases

CTDi 1208.
GeneCardsi GC06M035765.
HGNCi HGNC:2085. CLPS.
HPAi HPA010512.
MIMi 120105. gene.
neXtProti NX_P04118.
PharmGKBi PA26611.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42456.
HOGENOMi HOG000059253.
HOVERGENi HBG005373.
InParanoidi P04118.
KOi K14460.
OMAi CSAKTLY.
OrthoDBi EOG74N5K5.
PhylomeDBi P04118.
TreeFami TF336178.

Enzyme and pathway databases

Reactomei REACT_24968. Retinoid metabolism and transport.
REACT_9518. Digestion of dietary lipid.

Miscellaneous databases

GeneWikii Colipase.
GenomeRNAii 1208.
NextBioi 4977.
PMAP-CutDB P04118.
PROi P04118.
SOURCEi Search...

Gene expression databases

Bgeei P04118.
CleanExi HS_CLPS.
Genevestigatori P04118.

Family and domain databases

InterProi IPR001981. Colipase.
IPR017914. Colipase_C.
IPR017915. Colipase_CS.
IPR017913. Colipase_N.
[Graphical view ]
PANTHERi PTHR10041. PTHR10041. 1 hit.
Pfami PF01114. Colipase. 1 hit.
PF02740. Colipase_C. 1 hit.
[Graphical view ]
PRINTSi PR00128. COLIPASE.
SMARTi SM00023. COLIPASE. 1 hit.
[Graphical view ]
PROSITEi PS00121. COLIPASE_1. 1 hit.
PS51342. COLIPASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiCOL_HUMAN
AccessioniPrimary (citable) accession number: P04118
Secondary accession number(s): Q5T9G7, Q5U809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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