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Pancreatic lipase-related protein 2 (PL-RP2) (EC 3.1.1.26) (EC 3.1.1.3) (Cytotoxic T-lymphocyte lipase) (Galactolipase)

 LIPR2_MOUSE             Reviewed;         482 AA.
P17892; Q4VBW7;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
17-FEB-2016, sequence version 2.
23-MAY-2018, entry version 141.
RecName: Full=Pancreatic lipase-related protein 2 {ECO:0000250|UniProtKB:P54317};
Short=PL-RP2 {ECO:0000250|UniProtKB:P54317};
EC=3.1.1.26;
EC=3.1.1.3;
AltName: Full=Cytotoxic T-lymphocyte lipase {ECO:0000305|PubMed:2302735};
AltName: Full=Galactolipase;
Flags: Precursor;
Name=Pnliprp2 {ECO:0000312|MGI:MGI:1336202};
Synonyms=Plrp2 {ECO:0000250|UniProtKB:P54317};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, AND FUNCTION.
TISSUE=T-cell;
PubMed=2302735; DOI=10.1016/0092-8674(90)90596-7;
Grusby M.J., Nabavi N., Wong H., Dick R.F., Bluestone J.A.,
Schotz M.C., Glimcher L.H.;
"Cloning of an interleukin-4 inducible gene from cytotoxic T
lymphocytes and its identification as a lipase.";
Cell 60:451-459(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND ENZYME REGULATION.
PubMed=21382969; DOI=10.1194/jlr.M014290;
Xiao X., Ross L.E., Miller R.A., Lowe M.E.;
"Kinetic properties of mouse pancreatic lipase-related protein-2
suggest the mouse may not model human fat digestion.";
J. Lipid Res. 52:982-990(2011).
-!- FUNCTION: Lipase with broad substrate specificity. Can hydrolyze
both phospholipids and galactolipids. Acts preferentially on
monoglycerides, phospholipids and galactolipids. Contributes to
milk fat hydrolysis (By similarity).
{ECO:0000250|UniProtKB:P54317, ECO:0000269|PubMed:21382969,
ECO:0000269|PubMed:2302735}.
-!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a
carboxylate.
-!- CATALYTIC ACTIVITY: 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2
H(2)O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates.
-!- ENZYME REGULATION: CLPS stimulates triacylglycerol lipase activity
(PubMed:21382969, PubMed:2302735). Triacylglycerol lipase activity
is not inhibited by increasing bile salt concentration
(PubMed:21382969). {ECO:0000269|PubMed:21382969,
ECO:0000269|PubMed:2302735}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- INDUCTION: By interleukin-4.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
{ECO:0000305}.
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EMBL; M30687; AAA37491.1; -; mRNA.
EMBL; AK131882; BAE20849.1; -; mRNA.
EMBL; AC102548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC094923; AAH94923.1; -; mRNA.
CCDS; CCDS38030.1; -.
PIR; A34671; A34671.
RefSeq; NP_035258.2; NM_011128.2.
UniGene; Mm.212333; -.
ProteinModelPortal; P17892; -.
SMR; P17892; -.
STRING; 10090.ENSMUSP00000026081; -.
SwissLipids; SLP:000001480; -.
ESTHER; mouse-LIPR2; Pancreatic_lipase.
PhosphoSitePlus; P17892; -.
PaxDb; P17892; -.
PeptideAtlas; P17892; -.
PRIDE; P17892; -.
Ensembl; ENSMUST00000026081; ENSMUSP00000026081; ENSMUSG00000025091.
GeneID; 18947; -.
KEGG; mmu:18947; -.
UCSC; uc008iau.2; mouse.
CTD; 5408; -.
MGI; MGI:1336202; Pnliprp2.
eggNOG; ENOG410IHRX; Eukaryota.
eggNOG; ENOG410Y92X; LUCA.
GeneTree; ENSGT00760000119069; -.
HOGENOM; HOG000038552; -.
HOVERGEN; HBG003243; -.
InParanoid; P17892; -.
KO; K14075; -.
OMA; PWDPKDI; -.
OrthoDB; EOG091G0DJ5; -.
TreeFam; TF324997; -.
PRO; PR:P17892; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025091; -.
CleanEx; MM_PNLIPRP2; -.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0102549; F:1-18:1-2-16:0-monogalactosyldiacylglycerol lipase activity; IEA:UniProtKB-EC.
GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0047714; F:galactolipase activity; ISS:UniProtKB.
GO; GO:0004620; F:phospholipase activity; ISS:UniProtKB.
GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
GO; GO:0006968; P:cellular defense response; IMP:MGI.
GO; GO:0019376; P:galactolipid catabolic process; ISS:UniProtKB.
GO; GO:0044258; P:intestinal lipid catabolic process; IMP:MGI.
GO; GO:0009395; P:phospholipid catabolic process; ISS:UniProtKB.
CDD; cd00707; Pancreat_lipase_like; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013818; Lipase/vitellogenin.
InterPro; IPR016272; Lipase_LIPH.
InterPro; IPR033906; Lipase_N.
InterPro; IPR002331; Lipase_panc.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR000734; TAG_lipase.
PANTHER; PTHR11610; PTHR11610; 1.
Pfam; PF00151; Lipase; 1.
Pfam; PF01477; PLAT; 1.
PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
PRINTS; PR00823; PANCLIPASE.
PRINTS; PR00821; TAGLIPASE.
SMART; SM00308; LH2; 1.
SUPFAM; SSF49723; SSF49723; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS50095; PLAT; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding;
Reference proteome; Secreted; Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 482 Pancreatic lipase-related protein 2.
/FTId=PRO_0000017794.
DOMAIN 370 482 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
ACT_SITE 184 184 Nucleophile. {ECO:0000250}.
ACT_SITE 208 208 Charge relay system. {ECO:0000250}.
ACT_SITE 295 295 Charge relay system. {ECO:0000250}.
METAL 219 219 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 222 222 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 224 224 Calcium. {ECO:0000250}.
METAL 227 227 Calcium. {ECO:0000250}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 40 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 122 133 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 269 293 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 317 328 {ECO:0000255|PROSITE-ProRule:PRU00152}.
DISULFID 466 482 {ECO:0000255|PROSITE-ProRule:PRU00152}.
CONFLICT 156 156 V -> L (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 182 182 G -> P (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 266 266 M -> I (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 331 331 C -> S (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 362 364 GDS -> ADT (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 381 381 A -> P (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 397 397 G -> A (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 454 457 VQRG -> LQRA (in Ref. 1; AAA37491).
{ECO:0000305}.
CONFLICT 467 467 S -> T (in Ref. 1; AAA37491).
{ECO:0000305}.
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


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