LIPR2_RAT
ID LIPR2_RAT Reviewed; 468 AA.
AC P54318;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
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:0000250|UniProtKB:P17892};
DE AltName: Full=Galactolipase;
DE EC=3.1.1.26 {ECO:0000269|PubMed:9822688};
DE AltName: Full=Secretory glycoprotein GP-3 {ECO:0000303|PubMed:8486693};
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:8656075, ECO:0000269|PubMed:9822688};
DE Flags: Precursor;
GN Name=Pnliprp2 {ECO:0000312|RGD:620793};
GN Synonyms=Plrp2 {ECO:0000250|UniProtKB:P54317};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-46, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RX PubMed=8486693; DOI=10.1016/s0021-9258(18)82203-7;
RA Wishart M.J., Andrews P.C., Nichols R., Blevins G.T. Jr., Logsdon C.D.,
RA Williams J.A.;
RT "Identification and cloning of GP-3 from rat pancreatic acinar zymogen
RT granules as a glycosylated membrane-associated lipase.";
RL J. Biol. Chem. 268:10303-10311(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8203536; DOI=10.1152/ajpgi.1994.266.5.g914;
RA Payne R.M., Sims H.F., Jennens M.L., Lowe M.E.;
RT "Rat pancreatic lipase and two related proteins: enzymatic properties and
RT mRNA expression during development.";
RL Am. J. Physiol. 266:G914-G921(1994).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8656075;
RA Jennens M.L., Lowe M.E.;
RT "Rat GP-3 is a pancreatic lipase with kinetic properties that differ from
RT colipase-dependent pancreatic lipase.";
RL J. Lipid Res. 36:2374-2382(1995).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF SER-170 AND
RP HIS-281.
RX PubMed=32963038; DOI=10.1194/jlr.ra120001087;
RA Kuge H., Miyamoto I., Yagyu K.I., Honke K.;
RT "PLRP2 selectively localizes synaptic membrane proteins via acyl-chain
RT remodeling of phospholipids.";
RL J. Lipid Res. 61:1747-1763(2020).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 17-468, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-352, CATALYTIC ACTIVITY, ACTIVE SITE, AND FUNCTION.
RC TISSUE=Pancreas;
RX PubMed=9822688; DOI=10.1074/jbc.273.48.32121;
RA Roussel A., Yang Y., Ferrato F., Verger R., Cambillau C., Lowe M.;
RT "Structure and activity of rat pancreatic lipase-related protein 2.";
RL J. Biol. Chem. 273:32121-32128(1998).
CC -!- FUNCTION: Lipase that primarily hydrolyzes triglycerides and
CC galactosylglycerides (PubMed:8656075, PubMed:9822688). In neonates, may
CC play a major role in pancreatic digestion of dietary fats such as milk
CC fat globules enriched in long-chain triglycerides (By similarity).
CC Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides
CC without apparent positional specificity (PubMed:8656075). Can
CC completely deacylate triacylglycerols (By similarity). When the liver
CC matures and bile salt synthesis increases, likely functions mainly as a
CC galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes
CC monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG)
CC present in a plant-based diet, releasing long-chain polyunsaturated
CC fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty
CC acyls in galactolipids (PubMed:9822688). May act together with LIPF to
CC hydrolyze partially digested triglycerides (By similarity). Hydrolyzes
CC long-chain monoglycerides with high efficiency. In cytotoxic T cells,
CC contributes to perforin-dependent cell lysis, but is unlikely to
CC mediate direct cytotoxicity (By similarity). Also has low phospholipase
CC activity (PubMed:8656075, PubMed:9822688). In neurons, required for the
CC localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to
CC neurite tips through acyl chain remodeling of membrane phospholipids
CC (PubMed:32963038). The resulting OPPC-rich lipid membrane domain
CC recruits the t-SNARE protein STX4 by selectively interacting with the
CC STX4 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
CC (PubMed:32963038). {ECO:0000250|UniProtKB:P17892,
CC ECO:0000250|UniProtKB:P54317, ECO:0000269|PubMed:32963038,
CC ECO:0000269|PubMed:8656075, ECO:0000269|PubMed:9822688}.
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:8656075, ECO:0000269|PubMed:9822688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:8656075, ECO:0000305|PubMed:9822688};
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:0000269|PubMed:9822688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190;
CC Evidence={ECO:0000305|PubMed:9822688};
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:8656075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000305|PubMed:8656075};
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:8656075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000305|PubMed:8656075};
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:8656075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000305|PubMed:8656075};
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:0000269|PubMed:9822688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597;
CC Evidence={ECO:0000305|PubMed:9822688};
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:0000269|PubMed:9822688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541;
CC Evidence={ECO:0000305|PubMed:9822688};
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:0000269|PubMed:8656075};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665;
CC Evidence={ECO:0000305|PubMed:8656075};
CC -!- ACTIVITY REGULATION: CLPS stimulates triacylglycerol lipase activity.
CC Triacylglycerol lipase activity is not inhibited by increasing bile
CC salt concentration. {ECO:0000269|PubMed:8656075}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8 (lipase activity in the presence of bile salts) and
CC 7.0-7.25 (lipase activity in the absence of bile salts).
CC {ECO:0000269|PubMed:8656075};
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:0000269|PubMed:8486693}; Peripheral membrane
CC protein {ECO:0000305|PubMed:8486693}. Cell projection, neuron
CC projection {ECO:0000269|PubMed:32963038}. Note=Localizes to neurite
CC tips in neuronal cells. {ECO:0000269|PubMed:32963038}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic acinar cells (at protein
CC level). {ECO:0000269|PubMed:8486693}.
CC -!- INDUCTION: By NGF (at protein level). {ECO:0000269|PubMed:32963038}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L09216; AAA41250.1; ALT_INIT; mRNA.
DR PIR; A46696; A46696.
DR RefSeq; NP_476554.1; NM_057206.1.
DR PDB; 1BU8; X-ray; 1.80 A; A=17-468.
DR PDBsum; 1BU8; -.
DR AlphaFoldDB; P54318; -.
DR SMR; P54318; -.
DR STRING; 10116.ENSRNOP00000063609; -.
DR ESTHER; ratno-4plip; Pancreatic_lipase.
DR GlyGen; P54318; 2 sites.
DR iPTMnet; P54318; -.
DR PRIDE; P54318; -.
DR GeneID; 117554; -.
DR KEGG; rno:117554; -.
DR CTD; 5408; -.
DR RGD; 620793; Pnliprp2.
DR eggNOG; ENOG502QUK7; Eukaryota.
DR InParanoid; P54318; -.
DR OrthoDB; 534956at2759; -.
DR BRENDA; 3.1.1.26; 5301.
DR Reactome; R-RNO-192456; Digestion of dietary lipid.
DR UniPathway; UPA00256; -.
DR EvolutionaryTrace; P54318; -.
DR PRO; PR:P54318; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0016298; F:lipase activity; IDA:RGD.
DR GO; GO:0004620; F:phospholipase activity; IDA:RGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:RGD.
DR GO; GO:0006968; P:cellular defense response; ISO:RGD.
DR GO; GO:0019376; P:galactolipid catabolic process; IDA:RGD.
DR GO; GO:0044258; P:intestinal lipid catabolic process; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
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; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEP:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0019433; P:triglyceride catabolic process; ISS:UniProtKB.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 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; PTHR11610; 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; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8486693"
FT CHAIN 17..468
FT /note="Pancreatic lipase-related protein 2"
FT /id="PRO_0000017796"
FT DOMAIN 356..468
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 92..104
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT REGION 256..278
FT /note="Required for galactolipase activity"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT ACT_SITE 170
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9822688"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:9822688"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037,
FT ECO:0000269|PubMed:9822688"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P54317"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9822688"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 20..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9822688"
FT DISULFID 108..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9822688"
FT DISULFID 255..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9822688"
FT DISULFID 303..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9822688"
FT DISULFID 317..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9822688"
FT DISULFID 452..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152,
FT ECO:0000269|PubMed:9822688"
FT MUTAGEN 170
FT /note="S->G: Abolishes rescue of lipase-deficient activity
FT in Pnliprp2 knockout neurons."
FT /evidence="ECO:0000269|PubMed:32963038"
FT MUTAGEN 281
FT /note="H->L: Abolishes rescue of lipase-deficient activity
FT in Pnliprp2 knockout neurons."
FT /evidence="ECO:0000269|PubMed:32963038"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 132..157
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1BU8"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1BU8"
FT TURN 198..202
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1BU8"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:1BU8"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 356..365
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 370..380
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 433..442
FT /evidence="ECO:0007829|PDB:1BU8"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:1BU8"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:1BU8"
SQ SEQUENCE 468 AA; 52535 MW; B41FB0B339BA9A6F CRC64;
MLLCWIVSLL LATVGGKEVC YGHLGCFSND KPWAGMLQRP LKIFPWSPED IDTRFLLYTN
ENPNNYQKIS ATEPDTIKFS NFQLDRKTRF IVHGFIDKGE DGWLLDMCKK MFQVEKVNCI
CVDWRRGSRT EYTQASYNTR VVGAEIAFLV QVLSTEMGYS PENVHLIGHS LGAHVVGEAG
RRLEGHVGRI TGLDPAEPCF QGLPEEVRLD PSDAMFVDVI HTDSAPIIPY LGFGMSQKVG
HLDFFPNGGK EMPGCQKNIL STIVDINGIW EGTQNFVACN HLRSYKYYAS SILNPDGFLG
YPCSSYEKFQ QNDCFPCPEE GCPKMGHYAD QFEGKTATVE QTVYLNTGDS GNFTRWRYKV
SVTLSGAKKL SGYILVALYG NNGNSKQYEI FKGSLKPEAR HVRDIDVDIN VGEIQKVKFL
WNNKVINLFR PTLGASQITV QSGVDGKEYN FCSSDTVRED VLQSLYPC
