IED Industry Enzyme Database

Detail Information for IndEnz0005000006
IED ID IndEnz0005000006
Enzyme Type ID lipase000006
Protein Name Pancreatic lipase-related protein 2
PL-RP2
Cytotoxic T lymphocyte lipase
Galactolipase
EC 3.1.1.26
Secretory glycoprotein GP-3
Triacylglycerol lipase
EC 3.1.1.3
Gene Name Pnliprp2 Plrp2
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MLLCWIVSLLLATVGGKEVCYGHLGCFSNDKPWAGMLQRPLKIFPWSPEDIDTRFLLYTNENPNNYQKISATEPDTIKFSNFQLDRKTRFIVHGFIDKGEDGWLLDMCKKMFQVEKVNCICVDWRRGSRTEYTQASYNTRVVGAEIAFLVQVLSTEMGYSPENVHLIGHSLGAHVVGEAGRRLEGHVGRITGLDPAEPCFQGLPEEVRLDPSDAMFVDVIHTDSAPIIPYLGFGMSQKVGHLDFFPNGGKEMPGCQKNILSTIVDINGIWEGTQNFVACNHLRSYKYYASSILNPDGFLGYPCSSYEKFQQNDCFPCPEEGCPKMGHYADQFEGKTATVEQTVYLNTGDSGNFTRWRYKVSVTLSGAKKLSGYILVALYGNNGNSKQYEIFKGSLKPEARHVRDIDVDINVGEIQKVKFLWNNKVINLFRPTLGASQITVQSGVDGKEYNFCSSDTVREDVLQSLYPC
Enzyme Length 468
Uniprot Accession Number P54318
Absorption
Active Site ACT_SITE 170; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:9822688"; ACT_SITE 194; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:9822688"; ACT_SITE 281; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:9822688"
Activity Regulation ACTIVITY REGULATION: CLPS stimulates triacylglycerol lipase activity. Triacylglycerol lipase activity is not inhibited by increasing bile salt concentration. {ECO:0000269|PubMed:8656075}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:8656075, ECO:0000269|PubMed:9822688};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000305|PubMed:8656075, ECO:0000305|PubMed:9822688}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+); Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26; Evidence={ECO:0000269|PubMed:9822688};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190; Evidence={ECO:0000305|PubMed:9822688}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:8656075};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000305|PubMed:8656075}; CATALYTIC ACTIVITY: Reaction=di-(9Z)-octadecenoylglycerol + H2O = (9Z)-octadecenoate + (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:47868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937, ChEBI:CHEBI:75945; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47869; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:39955, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75937; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39956; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+) + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153, ChEBI:CHEBI:88155; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2,3-tributanoylglycerol + H2O = butanoate + dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020, ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:8656075};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476; Evidence={ECO:0000305|PubMed:8656075}; CATALYTIC ACTIVITY: Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) + octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978, ChEBI:CHEBI:88066; Evidence={ECO:0000269|PubMed:8656075};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865; Evidence={ECO:0000305|PubMed:8656075}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoylglycerol + H2O = decanoate + decanoylglycerol + H(+); Xref=Rhea:RHEA:48596, ChEBI:CHEBI:11152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:90605; Evidence={ECO:0000269|PubMed:9822688};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48597; Evidence={ECO:0000305|PubMed:9822688}; CATALYTIC ACTIVITY: Reaction=H2O + long chain 1,2-diacyl-3-O-beta-D-galactosyl-sn-glycerol = a fatty acid + H(+) + long chain acyl-3-O-beta-D-galactosyl-sn-glycerol; Xref=Rhea:RHEA:48700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:90477, ChEBI:CHEBI:90770; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48701; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-3-O-beta-D-galactosyl-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-(beta-D-galactosyl)-sn-glycerol; Xref=Rhea:RHEA:48696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:90453, ChEBI:CHEBI:90769; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48697; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-3-beta-D-galactosyl-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-beta-D-galactosyl-sn-glycerol + H(+); Xref=Rhea:RHEA:48540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90340, ChEBI:CHEBI:90515; Evidence={ECO:0000269|PubMed:9822688};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48541; Evidence={ECO:0000305|PubMed:9822688}; CATALYTIC ACTIVITY: Reaction=1-beta-D-galactosyl-2,3-didodecanoyl-sn-glycerol + H2O = 1-beta-D-galactosyl-dodecanoyl-sn-glycerol + dodecanoate + H(+); Xref=Rhea:RHEA:48536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90342, ChEBI:CHEBI:90514; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48537; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396, ChEBI:CHEBI:28868, ChEBI:CHEBI:90310; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=H2O + long chain 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol = a fatty acid + H(+) + long chain acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol; Xref=Rhea:RHEA:48708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:90463, ChEBI:CHEBI:90774; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48709; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = H(+) + octanoate + octanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol; Xref=Rhea:RHEA:48692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:90457, ChEBI:CHEBI:90768; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48693; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=1,2-didodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = dodecanoate + dodecanoyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:90337, ChEBI:CHEBI:90359; Evidence={ECO:0000250|UniProtKB:P54317};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48517; Evidence={ECO:0000250|UniProtKB:P54317}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + a monoacyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:44664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:84465; Evidence={ECO:0000269|PubMed:8656075};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44665; Evidence={ECO:0000305|PubMed:8656075};
DNA Binding
EC Number 3.1.1.26; 3.1.1.3
Enzyme Function FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8656075, PubMed:9822688). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8656075). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:9822688). May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:8656075, PubMed:9822688). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (PubMed:32963038). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (PubMed:32963038). {ECO:0000250|UniProtKB:P17892, ECO:0000250|UniProtKB:P54317, ECO:0000269|PubMed:32963038, ECO:0000269|PubMed:8656075, ECO:0000269|PubMed:9822688}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8 (lipase activity in the presence of bile salts) and 7.0-7.25 (lipase activity in the absence of bile salts). {ECO:0000269|PubMed:8656075};
Pathway PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. {ECO:0000250|UniProtKB:P54317}.; PATHWAY: Glycolipid metabolism. {ECO:0000250|UniProtKB:P54317}.
nucleotide Binding
Features Active site (3); Beta strand (22); Chain (1); Disulfide bond (6); Domain (1); Erroneous initiation (1); Glycosylation (2); Helix (16); Metal binding (4); Mutagenesis (2); Region (2); Signal peptide (1); Turn (4)
Keywords 3D-structure;Calcium;Cell projection;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Metal-binding;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: By NGF (at protein level). {ECO:0000269|PubMed:32963038}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P54317}. Zymogen granule membrane {ECO:0000269|PubMed:8486693}; Peripheral membrane protein {ECO:0000305|PubMed:8486693}. Cell projection, neuron projection {ECO:0000269|PubMed:32963038}. Note=Localizes to neurite tips in neuronal cells. {ECO:0000269|PubMed:32963038}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000269|PubMed:8486693
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1BU8;
Mapped Pubmed ID 15181189; 17010228; 17936733; 8765145; 8967484; 9748646;
Motif
Gene Encoded By
Mass 52,535
Kinetics
Metal Binding METAL 205; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P54317; METAL 208; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P54317; METAL 210; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P54317; METAL 213; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P54317
Rhea ID RHEA:12044; RHEA:12045; RHEA:13189; RHEA:13190; RHEA:38575; RHEA:38576; RHEA:47868; RHEA:47869; RHEA:39955; RHEA:39956; RHEA:38487; RHEA:38488; RHEA:48024; RHEA:48025; RHEA:40475; RHEA:40476; RHEA:47864; RHEA:47865; RHEA:48596; RHEA:48597; RHEA:48700; RHEA:48701; RHEA:48696; RHEA:48697; RHEA:48540; RHEA:48541; RHEA:48536; RHEA:48537; RHEA:48372; RHEA:48373; RHEA:48708; RHEA:48709; RHEA:48692; RHEA:48693; RHEA:48516; RHEA:48517; RHEA:44664; RHEA:44665
Cross Reference Brenda 3.1.1.26;