| IED ID | IndEnz0010000008 |
| Enzyme Type ID | esterase000008 |
| Protein Name |
Patatin-like phospholipase domain-containing protein 7 EC 3.1.1.- EC 3.1.1.5 Neuropathy target esterase-related esterase NRE NTE-related esterase |
| Gene Name | Pnpla7 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MQNEEDACLEAGYCLGTTLSSWRLHFMEEQSQSTMLMGIGIGALLTLAFVGITFFFVYRRVRRLRRAEPTPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTSAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPESQAIPLLSVASVAGRAKRQMSYGPEEQLERSLRPSEFSSSDHGSSCVTVSGPLLKRSCSVPLPSNHGEVDELRQSQGSGSNTSAFQESHEGATSDLGMAYNRARILPHSDEQLGNSLASKSKKSVVAETPSAIFHYSENFRDETGACGKTDAIFRAATKDLLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAHFYEIMRKRPDVVLGVAHTVVKRMSSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGALTSIKRRYPQVVTRLIHLLGEKILGSLQQGSATGHQLGFNTASSKWDLGNPPGNLSTVAALPASEDVPLTAFALELQHALSAIGPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADGTLTPWTQRCIRQADCILIVGLGEQEPAVGELEQMLESTAVRAQKQLILLHKEDGPVPSRTVEWLNMRSWCSGHLHLCCPRRVFSKRSLPKLVEMYTRVFQRPPDRHSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGMTSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQDQQGTSKRKDCGVFTCPNSSFTDLAEIVSRIEPAKVAAVDDESDYQTEYEEELPAIPKETYADFQSTGIELDSDSEYEPSMLQGPPSLTSPEQSQDSFPWLPNQDDQGPRLEHPS |
| Enzyme Length | 1352 |
| Uniprot Accession Number | A2AJ88 |
| Absorption | |
| Active Site | ACT_SITE 983; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1103; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: cAMP does not regulate lysophospholipase activity in vitro (PubMed:18086666, PubMed:28887301). Slightly inhibited by organophosphorus (OP) compounds such as mipafox, which is likely why mice are less sensitive to distal axonophathy induced by OPs compared to humans (PubMed:18086666). {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}. |
| 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:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; 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:0000269|PubMed:28887301};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808; Evidence={ECO:0000269|PubMed:28887301}; 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:0000269|PubMed:28887301};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896; Evidence={ECO:0000269|PubMed:28887301}; 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:0000269|PubMed:28887301};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500; Evidence={ECO:0000269|PubMed:28887301}; 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:0000269|PubMed:18086666};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000269|PubMed:18086666}; 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:0000269|PubMed:18086666};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093; Evidence={ECO:0000269|PubMed:18086666}; |
| DNA Binding | |
| EC Number | 3.1.1.-; 3.1.1.5 |
| Enzyme Function | FUNCTION: Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine (PubMed:18086666, PubMed:28887301). Also can deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0) (PubMed:22326266, PubMed:18086666, PubMed:28887301). {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:22326266, ECO:0000269|PubMed:28887301}.; FUNCTION: [Isoform 2]: Lysophospholipase. {ECO:0000269|PubMed:22326266}.; FUNCTION: [Isoform 3]: Lacks lysophospholipase activity. {ECO:0000269|PubMed:22326266}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18086666}; |
| Pathway | |
| nucleotide Binding | NP_BIND 170..297; /note=cNMP 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00060; NP_BIND 499..585; /note=cNMP 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00060; NP_BIND 613..718; /note=cNMP 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00060 |
| Features | Active site (2); Alternative sequence (4); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (6); Modified residue (4); Motif (3); Nucleotide binding (3); Region (4); Sequence caution (1); Sequence conflict (6); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Repeat;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | INDUCTION: By nutritional conditions (PubMed:22326266, PubMed:18086666). Expression of isoform 3 is switched to the expression of isoform 2 during fasting (PubMed:22326266). {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:22326266}.; INDUCTION: [Isoform 1]: Expression levels are not affected by fasting. {ECO:0000269|PubMed:22326266}.; INDUCTION: [Isoform 2]: In white adipose tissue, cardiac muscle, skeletal muscle, and testis, expression levels are down-regulated under well-fed conditions and are up-regulated during fasting. {ECO:0000269|PubMed:22326266}.; INDUCTION: [Isoform 3]: In white adipose tissue, cardiac muscle, skeletal muscle, and testis, expression levels are up-regulated under well-fed conditions and are down-regulated during fasting. {ECO:0000269|PubMed:22326266}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; Single-pass type III membrane protein {ECO:0000269|PubMed:28887301}. Lipid droplet {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}. |
| Modified Residue | MOD_RES 341; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17242355; MOD_RES 379; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6ZV29; MOD_RES 1280; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 1284; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q5BK26 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 12520002; 12640454; 15226823; 18486363; 18799693; 22307796; 32103509; |
| Motif | MOTIF 954..959; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 981..985; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1103..1105; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 150,494 |
| 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 |