P04118 (COL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Colipase

Gene names

Name:

CLPS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	112 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Digestion Lipid degradation Lipid metabolism
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Diabetes mellitus
Domain	Signal
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW lipid digestion Traceable author statement. Source: Reactome phototransduction, visible light Traceable author statement. Source: Reactome positive regulation of catalytic activity Inferred from electronic annotation. Source: GOC retinoid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	extracellular region Traceable author statement. Source: Reactome
Molecular_function	enzyme activator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17
	Propeptide	18 – 22	5	Enterostatin, activation peptide Potential		PRO_0000005696
	Chain	23 – 112	90	Colipase		PRO_0000005697
Amino acid modifications
	Disulfide bond	34 ↔ 45		By similarity
	Disulfide bond	40 ↔ 56		By similarity
	Disulfide bond	44 ↔ 78		By similarity
	Disulfide bond	66 ↔ 86		By similarity
	Disulfide bond	80 ↔ 104		By similarity
Natural variations
	Natural variant	8	1	L → P. Corresponds to variant rs2766597 [ dbSNP | Ensembl ].		VAR_053040
	Natural variant	109	1	R → C. Ref.10 Corresponds to variant rs41270082 [ dbSNP | Ensembl ].		VAR_047105

Sequences

	Sequence		Length	Mass (Da)
	P04118 [UniParc]. Last modified April 1, 1990. Version 2. Checksum: 772872EBBE7C4DF8	FASTA	112	11,954
	10 20 30 40 50 60 MEKILILLLV ALSVAYAAPG PRGIIINLEN GELCMNSAQC KSNCCQHSSA LGLARCTSMA 70 80 90 100 110 SENSECSVKT LYGIYYKCPC ERGLTCEGDK TIVGSITNTN FGICHDAGRS KQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00022232.
PIR	XLHU. A42568.
RefSeq	NP_001823.1. NM_001832.3.
UniGene	Hs.1340.
3D structure databases
ProteinModelPortal	P04118.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000259938.
PTM databases
PhosphoSite	P04118.
Polymorphism databases
DMDM	116900.
Proteomic databases
PaxDb	P04118.
PeptideAtlas	P04118.
PRIDE	P04118.
Protocols and materials databases
DNASU	1208.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259938; ENSP00000259938; ENSG00000137392.
GeneID	1208.
KEGG	hsa:1208.
UCSC	uc003ole.2. human.
Organism-specific databases
CTD	1208.
GeneCards	GC06M035765.
HGNC	HGNC:2085. CLPS.
HPA	HPA010512.
MIM	120105. gene.
neXtProt	NX_P04118.
PharmGKB	PA26611.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42456.
HOGENOM	HOG000059253.
HOVERGEN	HBG005373.
InParanoid	P04118.
KO	K14460.
OMA	ENSECSP.
OrthoDB	EOG498V28.
PhylomeDB	P04118.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	P04118.
CleanEx	HS_CLPS.
Genevestigator	P04118.
GermOnline	ENSG00000137392. Homo sapiens.
Family and domain databases
InterPro	IPR001981. Colipase. IPR017914. Colipase_C. IPR017915. Colipase_CS. IPR017913. Colipase_N. [Graphical view]
PANTHER	PTHR10041. PTHR10041. 1 hit.
Pfam	PF01114. Colipase. 1 hit. PF02740. Colipase_C. 1 hit. [Graphical view]
PRINTS	PR00128. COLIPASE.
SMART	SM00023. COLIPASE. 1 hit. [Graphical view]
PROSITE	PS00121. COLIPASE_1. 1 hit. PS51342. COLIPASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1208.
NextBio	4977.
PMAP-CutDB	P04118.
SOURCE	Search...

Entry information

Entry name

COL_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.