COL_HUMAN
ID COL_HUMAN Reviewed; 112 AA.
AC P04118; Q5T9G7; Q5U809;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Colipase {ECO:0000305};
DE Flags: Precursor;
GN Name=CLPS {ECO:0000312|HGNC:HGNC:2085};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2337598; DOI=10.1021/bi00455a032;
RA Lowe M.E., Rosenblum J.L., McEwen P., Strauss A.W.;
RT "Cloning and characterization of the human colipase cDNA.";
RL Biochemistry 29:823-828(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1643046; DOI=10.1021/bi00146a013;
RA Sims H.F., Lowe M.E.;
RT "The human colipase gene: isolation, chromosomal location, and tissue-
RT specific expression.";
RL Biochemistry 31:7120-7125(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-112.
RC TISSUE=Pancreas;
RA Reichwald K., Petz U., Platzer M.;
RT "Structure of human pancreatic colipase gene (CLPS).";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 23-108.
RC TISSUE=Pancreas;
RX PubMed=6691986; DOI=10.1016/0167-4838(84)90175-4;
RA Sternby B., Engstroem A., Hellman U., Vihert A.M., Sternby N.-H.,
RA Borgstroem B.;
RT "The primary sequence of human pancreatic colipase.";
RL Biochim. Biophys. Acta 784:75-80(1984).
RN [9]
RP FUNCTION.
RX PubMed=17401110; DOI=10.1194/jlr.m600486-jlr200;
RA Eydoux C., De Caro J., Ferrato F., Boullanger P., Lafont D., Laugier R.,
RA Carriere F., De Caro A.;
RT "Further biochemical characterization of human pancreatic lipase-related
RT protein 2 expressed in yeast cells.";
RL J. Lipid Res. 48:1539-1549(2007).
RN [10]
RP FUNCTION.
RX PubMed=26494624; DOI=10.1074/jbc.m115.683375;
RA Xiao X., Lowe M.E.;
RT "The beta5-Loop and Lid Domain Contribute to the Substrate Specificity of
RT Pancreatic Lipase-related Protein 2 (PNLIPRP2).";
RL J. Biol. Chem. 290:28847-28856(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH PNLIP, AND
RP INTERACTION WITH PNLIP.
RX PubMed=8479519; DOI=10.1038/362814a0;
RA van Tilbeurgh H., Egloff M.-P., Martinez C., Rugani N., Verger R.,
RA Cambillau C.;
RT "Interfacial activation of the lipase-procolipase complex by mixed micelles
RT revealed by X-ray crystallography.";
RL Nature 362:814-820(1993).
RN [12]
RP VARIANT CYS-109, AND ASSOCIATION WITH TYPE 2 DIABETES.
RX PubMed=16189801; DOI=10.1002/mnfr.200500087;
RA Lindner I., Helwig U., Rubin D., Li Y., Fisher E., Boeing H., Mohlig M.,
RA Spranger J., Pfeiffer A., Hampe J., Schreiber S., Doring F.,
RA Schrezenmeir J.;
RT "Putative association between a new polymorphism in exon 3 (Arg109Cys) of
RT the pancreatic colipase gene and type 2 diabetes mellitus in two
RT independent Caucasian study populations.";
RL Mol. Nutr. Food Res. 49:972-976(2005).
CC -!- FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the
CC lipase to anchor itself to the lipid-water interface. Without colipase
CC the enzyme is washed off by bile salts, which have an inhibitory effect
CC on the lipase. {ECO:0000269|PubMed:17401110,
CC ECO:0000269|PubMed:26494624}.
CC -!- FUNCTION: Enterostatin has a biological activity as a satiety signal.
CC {ECO:0000305}.
CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase.
CC {ECO:0000269|PubMed:16189801}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the pancreas.
CC {ECO:0000269|PubMed:2337598}.
CC -!- POLYMORPHISM: Variant Cys-109 is statistically significantly associated
CC with an increased risk of type 2 diabetes.
CC {ECO:0000269|PubMed:16189801}.
CC -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00674}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Colipase entry;
CC URL="https://en.wikipedia.org/wiki/Colipase";
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DR EMBL; J02883; AAA52054.1; -; mRNA.
DR EMBL; M95529; AAB05818.1; -; Genomic_DNA.
DR EMBL; BT006812; AAP35458.1; -; mRNA.
DR EMBL; AL157823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03850.1; -; Genomic_DNA.
DR EMBL; BC007061; AAH07061.1; -; mRNA.
DR EMBL; BC017897; AAH17897.1; -; mRNA.
DR EMBL; AY780648; AAV35728.1; -; mRNA.
DR CCDS; CCDS4811.1; -.
DR PIR; A42568; XLHU.
DR RefSeq; NP_001823.1; NM_001832.3.
DR AlphaFoldDB; P04118; -.
DR SMR; P04118; -.
DR BioGRID; 107618; 3.
DR STRING; 9606.ENSP00000259938; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR DrugBank; DB02451; B-nonylglucoside.
DR DrugBank; DB08222; METHOXYUNDECYLPHOSPHINIC ACID.
DR iPTMnet; P04118; -.
DR PhosphoSitePlus; P04118; -.
DR BioMuta; CLPS; -.
DR DMDM; 116900; -.
DR MassIVE; P04118; -.
DR PaxDb; P04118; -.
DR PeptideAtlas; P04118; -.
DR PRIDE; P04118; -.
DR ProteomicsDB; 51655; -.
DR Antibodypedia; 15257; 263 antibodies from 24 providers.
DR DNASU; 1208; -.
DR Ensembl; ENST00000259938.7; ENSP00000259938.2; ENSG00000137392.10.
DR GeneID; 1208; -.
DR KEGG; hsa:1208; -.
DR MANE-Select; ENST00000259938.7; ENSP00000259938.2; NM_001832.4; NP_001823.1.
DR UCSC; uc003ole.3; human.
DR CTD; 1208; -.
DR DisGeNET; 1208; -.
DR GeneCards; CLPS; -.
DR HGNC; HGNC:2085; CLPS.
DR HPA; ENSG00000137392; Tissue enriched (pancreas).
DR MIM; 120105; gene.
DR neXtProt; NX_P04118; -.
DR OpenTargets; ENSG00000137392; -.
DR PharmGKB; PA26611; -.
DR VEuPathDB; HostDB:ENSG00000137392; -.
DR eggNOG; ENOG502S4NY; Eukaryota.
DR GeneTree; ENSGT00390000012644; -.
DR HOGENOM; CLU_165591_0_0_1; -.
DR InParanoid; P04118; -.
DR OMA; NSIQCKS; -.
DR OrthoDB; 1504784at2759; -.
DR PhylomeDB; P04118; -.
DR TreeFam; TF336178; -.
DR PathwayCommons; P04118; -.
DR Reactome; R-HSA-192456; Digestion of dietary lipid.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P04118; -.
DR BioGRID-ORCS; 1208; 51 hits in 1066 CRISPR screens.
DR GeneWiki; Colipase; -.
DR GenomeRNAi; 1208; -.
DR Pharos; P04118; Tbio.
DR PRO; PR:P04118; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P04118; protein.
DR Bgee; ENSG00000137392; Expressed in body of pancreas and 100 other tissues.
DR ExpressionAtlas; P04118; baseline and differential.
DR Genevisible; P04118; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0032094; P:response to food; IBA:GO_Central.
DR CDD; cd00039; COLIPASE; 1.
DR InterPro; IPR001981; Colipase.
DR InterPro; IPR017914; Colipase_C.
DR InterPro; IPR017915; Colipase_CS.
DR InterPro; IPR017913; Colipase_N.
DR PANTHER; PTHR10041; PTHR10041; 1.
DR Pfam; PF01114; Colipase; 1.
DR Pfam; PF02740; Colipase_C; 1.
DR PRINTS; PR00128; COLIPASE.
DR SMART; SM00023; COLIPASE; 1.
DR PROSITE; PS00121; COLIPASE_1; 1.
DR PROSITE; PS51342; COLIPASE_2; 1.
PE 1: Evidence at protein level;
KW Diabetes mellitus; Digestion; Direct protein sequencing; Disulfide bond;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT PROPEP 18..22
FT /note="Enterostatin, activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005696"
FT CHAIN 23..112
FT /note="Colipase"
FT /id="PRO_0000005697"
FT DISULFID 34..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 40..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 44..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 66..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 80..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT VARIANT 8
FT /note="L -> P (in dbSNP:rs2766597)"
FT /id="VAR_053040"
FT VARIANT 109
FT /note="R -> C (in dbSNP:rs41270082)"
FT /evidence="ECO:0000269|PubMed:16189801"
FT /id="VAR_047105"
SQ SEQUENCE 112 AA; 11954 MW; 772872EBBE7C4DF8 CRC64;
MEKILILLLV ALSVAYAAPG PRGIIINLEN GELCMNSAQC KSNCCQHSSA LGLARCTSMA
SENSECSVKT LYGIYYKCPC ERGLTCEGDK TIVGSITNTN FGICHDAGRS KQ
