COL_MOUSE
ID COL_MOUSE Reviewed; 113 AA.
AC Q9CQC2; Q8VHR2; Q8VHR3;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Colipase {ECO:0000305};
DE Flags: Precursor;
GN Name=Clps {ECO:0000312|MGI:MGI:88421};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J, and CAST/EiJ; TISSUE=Pancreas;
RA Zuberi A.R., Poole A.C., York B., Smith Richards B.K.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=10769148; DOI=10.1021/bi9927235;
RA van Bennekum A.M., Fisher E.A., Blaner W.S., Harrison E.H.;
RT "Hydrolysis of retinyl esters by pancreatic triglyceride lipase.";
RL Biochemistry 39:4900-4906(2000).
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:10769148}.
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:0000255|PROSITE-ProRule:PRU00674}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the pancreas.
CC -!- SIMILARITY: Belongs to the colipase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00674}.
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DR EMBL; AF414676; AAL40730.1; -; mRNA.
DR EMBL; AF414677; AAL40731.1; -; mRNA.
DR EMBL; AF414678; AAL40732.1; -; Genomic_DNA.
DR EMBL; AF414679; AAL40733.1; -; Genomic_DNA.
DR EMBL; AK008635; BAB25796.1; -; mRNA.
DR EMBL; AK008815; BAB25909.1; -; mRNA.
DR EMBL; AK008834; BAB25918.1; -; mRNA.
DR EMBL; AK008839; BAB25921.1; -; mRNA.
DR EMBL; AK008874; BAB25944.1; -; mRNA.
DR EMBL; AK008879; BAB25947.1; -; mRNA.
DR EMBL; AK019047; BAB31524.1; -; mRNA.
DR EMBL; AK028141; BAC25769.1; -; mRNA.
DR EMBL; BC042935; AAH42935.1; -; mRNA.
DR CCDS; CCDS28581.1; -.
DR RefSeq; NP_001303994.1; NM_001317065.1.
DR RefSeq; NP_079745.1; NM_025469.3.
DR AlphaFoldDB; Q9CQC2; -.
DR SMR; Q9CQC2; -.
DR STRING; 10090.ENSMUSP00000025062; -.
DR PhosphoSitePlus; Q9CQC2; -.
DR CPTAC; non-CPTAC-3452; -.
DR MaxQB; Q9CQC2; -.
DR PaxDb; Q9CQC2; -.
DR PeptideAtlas; Q9CQC2; -.
DR PRIDE; Q9CQC2; -.
DR ProteomicsDB; 283345; -.
DR Antibodypedia; 15257; 263 antibodies from 24 providers.
DR DNASU; 109791; -.
DR Ensembl; ENSMUST00000025062; ENSMUSP00000025062; ENSMUSG00000024225.
DR GeneID; 109791; -.
DR KEGG; mmu:109791; -.
DR UCSC; uc008brf.1; mouse.
DR CTD; 1208; -.
DR MGI; MGI:88421; Clps.
DR VEuPathDB; HostDB:ENSMUSG00000024225; -.
DR eggNOG; ENOG502S4NY; Eukaryota.
DR GeneTree; ENSGT00390000012644; -.
DR HOGENOM; CLU_165591_0_0_1; -.
DR InParanoid; Q9CQC2; -.
DR OMA; NSIQCKS; -.
DR OrthoDB; 1504784at2759; -.
DR PhylomeDB; Q9CQC2; -.
DR TreeFam; TF336178; -.
DR Reactome; R-MMU-192456; Digestion of dietary lipid.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 109791; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Clps; mouse.
DR PRO; PR:Q9CQC2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CQC2; protein.
DR Bgee; ENSMUSG00000024225; Expressed in stomach and 40 other tissues.
DR ExpressionAtlas; Q9CQC2; baseline and differential.
DR Genevisible; Q9CQC2; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
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 Digestion; Disulfide bond; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..23
FT /note="Enterostatin, activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005698"
FT CHAIN 24..113
FT /note="Colipase"
FT /id="PRO_0000005699"
FT DISULFID 35..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 41..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 45..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 67..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
FT DISULFID 81..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00674"
SQ SEQUENCE 113 AA; 12445 MW; 9FC784631D1C413E CRC64;
MEKVLVLLLV SLLAVAYAAP GPRGLIINLE DGEICLNSMQ CKSRCCQHDT ILGIARCTHK
AMENSECSPK TLYGIYYRCP CERGLTCEGD RSIIGAITNT NYGICLDSRR SKQ
