ID LIPR2_MOUSE Reviewed; 482 AA.
AC P17892; Q4VBW7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 24-JAN-2024, entry version 173.
DE RecName: Full=Pancreatic lipase-related protein 2 {ECO:0000250|UniProtKB:P54317};
DE Short=PL-RP2 {ECO:0000250|UniProtKB:P54317};
DE AltName: Full=Cytotoxic T lymphocyte lipase {ECO:0000305|PubMed:2302735};
DE AltName: Full=Galactolipase;
DE EC=3.1.1.26 {ECO:0000250|UniProtKB:P54317};
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:21382969};
DE Flags: Precursor;
GN Name=Pnliprp2 {ECO:0000312|MGI:MGI:1336202};
GN Synonyms=Plrp2 {ECO:0000250|UniProtKB:P54317};
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 [MRNA], FUNCTION, ACTIVITY REGULATION, AND INDUCTION BY
RP IL4.
RC TISSUE=T-cell;
RX PubMed=2302735; DOI=10.1016/0092-8674(90)90596-7;
RA Grusby M.J., Nabavi N., Wong H., Dick R.F., Bluestone J.A., Schotz M.C.,
RA Glimcher L.H.;
RT "Cloning of an interleukin-4 inducible gene from cytotoxic T lymphocytes
RT and its identification as a lipase.";
RL Cell 60:451-459(1990).
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=9813028; DOI=10.1074/jbc.273.47.31215;
RA Lowe M.E., Kaplan M.H., Jackson-Grusby L., D'Agostino D., Grusby M.J.;
RT "Decreased neonatal dietary fat absorption and T cell cytotoxicity in
RT pancreatic lipase-related protein 2-deficient mice.";
RL J. Biol. Chem. 273:31215-31221(1998).
RN [6]
RP FUNCTION, AND INDUCTION BY IL4.
RX PubMed=19451396; DOI=10.1189/jlb.1208766;
RA Alves B.N., Leong J., Tamang D.L., Elliott V., Edelnant J., Redelman D.,
RA Singer C.A., Kuhn A.R., Miller R., Lowe M.E., Hudig D.;
RT "Pancreatic lipase-related protein 2 (PLRP2) induction by IL-4 in cytotoxic
RT T lymphocytes (CTLs) and reevaluation of the negative effects of its gene
RT ablation on cytotoxicity.";
RL J. Leukoc. Biol. 86:701-712(2009).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=21382969; DOI=10.1194/jlr.m014290;
RA Xiao X., Ross L.E., Miller R.A., Lowe M.E.;
RT "Kinetic properties of mouse pancreatic lipase-related protein-2 suggest
RT the mouse may not model human fat digestion.";
RL J. Lipid Res. 52:982-990(2011).
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides (PubMed:21382969, PubMed:9813028). In neonates,
CC may play a major role in pancreatic digestion of dietary fats such as
CC milk fat globules enriched in long-chain triglycerides
CC (PubMed:9813028). Hydrolyzes short-, medium- and long-chain fatty acyls
CC in triglycerides without apparent positional specificity
CC (PubMed:21382969). Can completely deacylate triacylglycerols (By
CC similarity). When the liver matures and bile salt synthesis increases,
CC likely functions mainly as a galactolipase and monoacylglycerol lipase.
CC Hydrolyzes monogalactosyldiglycerols (MGDG) and
CC digalactosyldiacylglycerols (DGDG) present in a plant-based diet,
CC releasing long-chain polyunsaturated fatty acids (By similarity).
CC Hydrolyzes medium- and long-chain fatty acyls in galactolipids (By
CC similarity). May act together with LIPF to hydrolyze partially digested
CC triglycerides (By similarity). Hydrolyzes long-chain monoglycerides
CC with high efficiency (By similarity). In cytotoxic T cells, contributes
CC to perforin-dependent cell lysis, but is unlikely to mediate direct
CC cytotoxicity (PubMed:2302735, PubMed:9813028, PubMed:19451396). Also
CC has low phospholipase activity (By similarity). In neurons, required
CC for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC)
CC to neurite tips through acyl chain remodeling of membrane phospholipids
CC (By similarity). The resulting OPPC-rich lipid membrane domain recruits
CC the t-SNARE protein STX4 by selectively interacting with the STX4
CC transmembrane domain and this promotes surface expression of the
CC dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion
CC of SLC6A3-containing transport vesicles with the plasma membrane (By
CC similarity). {ECO:0000250|UniProtKB:P54317,
CC ECO:0000250|UniProtKB:P54318, ECO:0000269|PubMed:19451396,
CC ECO:0000269|PubMed:21382969, ECO:0000269|PubMed:2302735,
CC ECO:0000269|PubMed:9813028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000269|PubMed:21382969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:21382969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-
CC beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+);
CC Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000269|PubMed:21382969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:21382969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-
CC octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+)
CC + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153,
CC ChEBI:CHEBI:88155; Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:21382969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:21382969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:21382969};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000305|PubMed:21382969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol +
CC H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol
CC = a fatty acid + H(+) + long chain acyl-3-O-beta-D-galactosyl-sn-
CC glycerol; Xref=Rhea:RHEA:48700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90477, ChEBI:CHEBI:90770;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-3-O-beta-D-galactosyl-sn-glycerol + H2O = H(+)
CC + octanoate + octanoyl-3-(beta-D-galactosyl)-sn-glycerol;
CC Xref=Rhea:RHEA:48696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:90453, ChEBI:CHEBI:90769;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-3-beta-D-galactosyl-sn-glycerol + H2O =
CC dodecanoate + dodecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:48540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90340, ChEBI:CHEBI:90515;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-beta-D-galactosyl-2,3-didodecanoyl-sn-glycerol + H2O = 1-
CC beta-D-galactosyl-dodecanoyl-sn-glycerol + dodecanoate + H(+);
CC Xref=Rhea:RHEA:48536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90342, ChEBI:CHEBI:90514;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-
CC sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-
CC (1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90310;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + long chain 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-
CC beta-D-galactosyl]-sn-glycerol = a fatty acid + H(+) + long chain
CC acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol;
CC Xref=Rhea:RHEA:48708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:90463, ChEBI:CHEBI:90774;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-O-
CC [alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol;
CC Xref=Rhea:RHEA:48692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:90457, ChEBI:CHEBI:90768;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC galactosyl]-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-O-[alpha-
CC D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:48516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:90337, ChEBI:CHEBI:90359;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a fatty acid
CC + a monoacyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:44664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:84465;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000250|UniProtKB:P54317};
CC -!- ACTIVITY REGULATION: CLPS stimulates triacylglycerol lipase activity
CC (PubMed:21382969, PubMed:2302735). Triacylglycerol lipase activity is
CC not inhibited by increasing bile salt concentration (PubMed:21382969).
CC {ECO:0000269|PubMed:21382969, ECO:0000269|PubMed:2302735}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000250|UniProtKB:P54317}.
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000250|UniProtKB:P54317}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen
CC granule membrane {ECO:0000250|UniProtKB:P54318}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P54318}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:P54318}. Note=Localizes to neurite
CC tips in neuronal cells. {ECO:0000250|UniProtKB:P54318}.
CC -!- TISSUE SPECIFICITY: Expressed in acinar cells of pancreas (at protein
CC level). {ECO:0000269|PubMed:9813028}.
CC -!- INDUCTION: Up-regulated in CD8-positive T cells by IL4/interleukin-4.
CC {ECO:0000269|PubMed:19451396, ECO:0000269|PubMed:2302735}.
CC -!- DISRUPTION PHENOTYPE: Suckling mutant mice show inefficient fat
CC digestion associated with fat malabsorption and decreased rates of
CC weight gain. {ECO:0000269|PubMed:9813028}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M30687; AAA37491.1; -; mRNA.
DR EMBL; AK131882; BAE20849.1; -; mRNA.
DR EMBL; AC102548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094923; AAH94923.1; -; mRNA.
DR CCDS; CCDS38030.1; -.
DR PIR; A34671; A34671.
DR RefSeq; NP_035258.2; NM_011128.2.
DR AlphaFoldDB; P17892; -.
DR SMR; P17892; -.
DR STRING; 10090.ENSMUSP00000026081; -.
DR SwissLipids; SLP:000001480; -.
DR ESTHER; mouse-LIPR2; Pancreatic_lipase.
DR GlyCosmos; P17892; 3 sites, No reported glycans.
DR GlyGen; P17892; 3 sites.
DR PhosphoSitePlus; P17892; -.
DR PaxDb; 10090-ENSMUSP00000026081; -.
DR PeptideAtlas; P17892; -.
DR ProteomicsDB; 292263; -.
DR Antibodypedia; 73327; 118 antibodies from 16 providers.
DR DNASU; 18947; -.
DR Ensembl; ENSMUST00000026081.5; ENSMUSP00000026081.4; ENSMUSG00000025091.5.
DR GeneID; 18947; -.
DR KEGG; mmu:18947; -.
DR UCSC; uc008iau.2; mouse.
DR AGR; MGI:1336202; -.
DR CTD; 5408; -.
DR MGI; MGI:1336202; Pnliprp2.
DR VEuPathDB; HostDB:ENSMUSG00000025091; -.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR GeneTree; ENSGT00940000155139; -.
DR InParanoid; P17892; -.
DR OMA; CFSNEKP; -.
DR OrthoDB; 3428256at2759; -.
DR PhylomeDB; P17892; -.
DR TreeFam; TF324997; -.
DR Reactome; R-MMU-192456; Digestion of dietary lipid.
DR UniPathway; UPA00256; -.
DR BioGRID-ORCS; 18947; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Pnliprp2; mouse.
DR PRO; PR:P17892; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P17892; Protein.
DR Bgee; ENSMUSG00000025091; Expressed in crypt of Lieberkuhn of small intestine and 57 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0042589; C:zymogen granule membrane; ISO:MGI.
DR GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0047714; F:galactolipase activity; ISS:UniProtKB.
DR GO; GO:0016298; F:lipase activity; ISO:MGI.
DR GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0006968; P:cellular defense response; IMP:MGI.
DR GO; GO:0019376; P:galactolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0044258; P:intestinal lipid catabolic process; IMP:MGI.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0019433; P:triglyceride catabolic process; ISS:UniProtKB.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR CDD; cd01759; PLAT_PL; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR002331; Lipase_panc.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF165; PANCREATIC LIPASE-RELATED PROTEIN 2; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00823; PANCLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell projection; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..482
FT /note="Pancreatic lipase-related protein 2"
FT /id="PRO_0000017794"
FT DOMAIN 370..482
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 106..118
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT REGION 270..292
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 184
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 295
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 122..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 269..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 317..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 331..336
FT /evidence="ECO:0000250|UniProtKB:P54317,
FT ECO:0000255|PROSITE-ProRule:PRU00152"
FT DISULFID 466..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT CONFLICT 156
FT /note="V -> L (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="G -> P (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="M -> I (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="C -> S (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..364
FT /note="GDS -> ADT (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="A -> P (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="G -> A (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..457
FT /note="VQRG -> LQRA (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="S -> T (in Ref. 1; AAA37491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54017 MW; 616E5F972362BE3C CRC64;
MPMDVRGCLF PSVQMLLCWL VSLLLATVGG KEVCYGHLGC FSNDKPWAGM IQRPSKIFPW
SPEDIDTRFL LYTNENPNNY QIISATDPAT INASNFQLDR KTRFIIHGFI DKGEEGWLLD
MCKKMFQVEK VNCICVDWKR GSRTEYTQAS YNTRVVGAEI AFLVQVLSTE MGYSPENVHL
IGHSLGSHVA GEAGRRLEGH VGRITGLDPA EPCFQGLPEE VRLDPSDAMF VDVIHTDSAP
IIPYLGFGMS QKVGHLDFFP NGGKEMPGCQ KNILSTIVDI NGIWEGTRNF AACNHLRSYK
YYASSILNPD GFLGYPCSSY EKFQHNDCFP CPEQGCPKMG HYADQFEGKT ATVEQTFFLN
TGDSGNFTRW RYKVSVTLSG AKKLSGYILV ALYGCNGNSK QYEVFKGSLQ PEARYIRDID
VDVNVGEIQK VKFLWNNKVI NLFRPTMGAS QITVQRGKDG KEFNFCSSNT VHEDVLQSLY
PC
//
