| IED ID | IndEnz0010001746 |
| Enzyme Type ID | esterase001746 |
| Protein Name |
Patatin-like phospholipase domain-containing protein 7 EC 3.1.1.- EC 3.1.1.5 Liver NTE-related protein 1 NTE-related esterase |
| Gene Name | Pnpla7 Nre Ntel1 |
| 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 | MQKEEDVCPEAGYCLGTALSSWGLHFMEEHSQSTMLMGIGIGVLLTLAFVGLAAFFVYRKVSRFRRAEPIPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTAAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVASTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPESQAIPLLSVASVAGRAKRQMSYGPEEQLERSPRLSEFNSSDQRSVAVSGPLLKRSCSVPLPPIHGEIDELRQAQGSGSNTSAFQESQEGATSDLGMAYNRARILPHSEEQLGSSLASKSKKSVVAETSAVFHYSEKPRDEPGPSGRTDAIFRAATKDLLTLMKLDDPSLLDGRVAFLHVPAGTIVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAHFYEIMRKRPDVVLGVAHTVVRRMSSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVEMLTHQARATTVHAVRDSELAKLPAGALTSIKRRYPQVVTRLIHLLGEKILGSLQQGSGTGHQLGFNTASSKWDLGNPPGNLSTVAAMPVSEDVPLTAFALELQHALSAIGPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADSTLTPWTQRCIRQADCILIVGLGDQEPALGELEQMLESTAVRAQKQLILLHKEEGPAPSRTVEWLNMRSWCSGHLHLCCPRRVFSKRSLPKLVEMYTRIFQRPPDRHSDFSRLARILTGNAIALVLGGGGARGCAQVGILRALAECGIPVDIIGGTSIGAFMGALFAEERSYSQIRIRAKQWAEDMTSMVKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGALWRYVRASMSLSGYMPPLCDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGPAGFDIWVRSGVLEKMLQDQQGTSKRMDCGVFTCPNSSFTDLAEIVSRIEPAKVAAVDDESDYQTEYEEELPAIPKETYADFQSTGIELDSDSECEPSMSQGPHSLTSPKQSQDSFPWLPNQDDQGPRLYRPS |
| Enzyme Length | 1349 |
| Uniprot Accession Number | Q5BK26 |
| Absorption | |
| Active Site | ACT_SITE 980; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1100; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:A2AJ88};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:A2AJ88}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823; Evidence={ECO:0000250|UniProtKB:A2AJ88};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808; Evidence={ECO:0000250|UniProtKB:A2AJ88}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:A2AJ88};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896; Evidence={ECO:0000250|UniProtKB:A2AJ88}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:A2AJ88};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000250|UniProtKB:A2AJ88}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:A2AJ88};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:A2AJ88}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57597; Evidence={ECO:0000250|UniProtKB:A2AJ88};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093; Evidence={ECO:0000250|UniProtKB:A2AJ88}; |
| DNA Binding | |
| EC Number | 3.1.1.-; 3.1.1.5 |
| Enzyme Function | FUNCTION: Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Also can deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0). {ECO:0000250|UniProtKB:A2AJ88}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 170..297; /note=cNMP 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00060; NP_BIND 496..599; /note=cNMP 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00060; NP_BIND 610..715; /note=cNMP 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00060 |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Modified residue (4); Motif (3); Mutagenesis (1); Nucleotide binding (3); Region (3); Sequence conflict (3); Topological domain (2); Transmembrane (1) |
| Keywords | Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A2AJ88}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:A2AJ88}. Lipid droplet {ECO:0000250|UniProtKB:A2AJ88}. |
| Modified Residue | MOD_RES 341; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 377; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6ZV29; MOD_RES 1277; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 1281; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 951..956; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 978..982; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1100..1102; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 150,024 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15177; RHEA:15178; RHEA:40807; RHEA:40808; RHEA:40895; RHEA:40896; RHEA:40499; RHEA:40500; RHEA:40435; RHEA:40436; RHEA:49092; RHEA:49093 |
| Cross Reference Brenda |