| IED ID | IndEnz0005000531 |
| Enzyme Type ID | lipase000531 |
| Protein Name |
Omega-hydroxyceramide transacylase EC 2.3.1.296 Patatin-like phospholipase domain-containing protein 1 |
| Gene Name | Pnpla1 |
| 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 | MDEQVFKGDPDTPHSISFSGSGFLSYYQAGAVDALRDLAPRMLDTAHRFAGTSAGAVIAALVVCGIEMEKYLRVLNMGLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGFIPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVILQEYYYRGYNDAVSYLRRLNAAYLDSPSKRVIFPRVEVYCQIEVALGHEPPPPSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESGCKESVESPVSLRVSISKQPSVSPLSPAQPVPVMRPTGPRDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAADSRGSKTGSSVPIGSPESPRLLLRSSQGATASRATLGLPPLSPSTPPAGPPVEDLGPERPTATGSPALSQLTGSAAPGTGKKAPHKPLLVEGPGEDSNTAKTMFKRKQKTNATRECFHRNAQSKKPASKLKSAPCPLNFPVLPKRVWVTYKPHPSRIQDYSYPEGVSGQNS |
| Enzyme Length | 599 |
| Uniprot Accession Number | Q3V1D5 |
| Absorption | |
| Active Site | ACT_SITE 53; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 172; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(omega-hydroxy-ultra-long chain fatty acyl)-sphingoid base = a diacylglycerol + an N-[omega-(9Z,12Z-octadecadienoyloxy)-O-ultra-long chain fatty acyl]-sphingoid base; Xref=Rhea:RHEA:61528, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:144784, ChEBI:CHEBI:144785; EC=2.3.1.296; Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61529; Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(omega-hydroxy-ultra-long chain fatty acyl)-sphing-4-enine = a diacylglycerol + an N-(omega-(9Z,12Z-octadecadienoyloxy)-ultra-long chain fatty acyl)-sphing-4-enine; Xref=Rhea:RHEA:65692, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157662, ChEBI:CHEBI:157663; Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65693; Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + N-(28-hydroxyoctacosanoyl)-sphing-4-enine = a diacylglycerol + N-(28-(9Z,12Z-octadecadienoyloxy)-octacosanoyl)-sphing-4-enine; Xref=Rhea:RHEA:65648, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157643, ChEBI:CHEBI:157652; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65649; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z,12Z)-octadecadienoylglycerol + N-(30-hydroxytriacontanoyl)-sphing-4-enine = di-(9Z,12Z)-octadecadienoylglycerol + N-[30-(9Z,12Z-octadecadienoyloxy)-triacontanoyl]-sphing-4-enine; Xref=Rhea:RHEA:55264, ChEBI:CHEBI:34862, ChEBI:CHEBI:75844, ChEBI:CHEBI:138658, ChEBI:CHEBI:138664; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55265; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + N-(32-hydroxydotriacontanoyl)-sphing-4-enine = a diacylglycerol + N-(32-(9Z,12Z-octadecadienoyloxy)-dotricontanoyl)-sphing-4-enine; Xref=Rhea:RHEA:65652, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157644, ChEBI:CHEBI:157653; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65653; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + N-(32-hydroxydotriacontenoyl)-sphing-4-enine = a diacylglycerol + an N-(32-(9Z,12Z-octadecadienoyloxy)-dotriacontenoyl)-sphing-4-enine; Xref=Rhea:RHEA:65668, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157645, ChEBI:CHEBI:157657; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65669; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(34-hydroxytetratriacontenoyl)-sphing-4-enine = a diacylglycerol + an N-(34-(9Z,12Z-octadecadienoyloxy)-tetratriacontenoyl)-sphing-4-enine; Xref=Rhea:RHEA:65672, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157646, ChEBI:CHEBI:157656; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65673; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(34-hydroxytetratriacontadienoyl)-sphing-4-enine = a diacylglycerol + an N-(34-(9Z,12Z-octadecadienoyloxy)-tetratriacontadienoyl)-sphing-4-enine; Xref=Rhea:RHEA:65676, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157647, ChEBI:CHEBI:157658; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65677; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(36-hydroxyhexatriacontenoyl)-sphing-4-enine = a diacylglycerol + an N-(36-(9Z,12Z-octadecadienoyloxy)-hexatriacontenoyl)-sphing-4-enine; Xref=Rhea:RHEA:65680, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157648, ChEBI:CHEBI:157659; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65681; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(36-hydroxyhexatriacontadienoyl)-sphing-4-enine = a diacylglycerol + an N-(36-(9Z,12Z-octadecadienoyloxy)-hexatriacontadienoyl)-sphing-4-enine; Xref=Rhea:RHEA:65684, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157649, ChEBI:CHEBI:157660; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65685; Evidence={ECO:0000305|PubMed:28248300}; CATALYTIC ACTIVITY: Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an N-(38-hydroxyoctatriacontenoyl)-sphing-4-enine = a diacylglycerol + an N-(38-(9Z,12Z-octadecadienoyloxy)-octatriacontenoyl)-sphing-4-enine; Xref=Rhea:RHEA:65688, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157650, ChEBI:CHEBI:157661; Evidence={ECO:0000305|PubMed:28248300};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65689; Evidence={ECO:0000305|PubMed:28248300}; |
| DNA Binding | |
| EC Number | 2.3.1.296 |
| Enzyme Function | FUNCTION: Omega-hydroxyceramide transacylase involved in the synthesis of omega-O-acylceramides (esterified omega-hydroxyacyl-sphingosine; EOS), which are extremely hydrophobic lipids involved in skin barrier formation (PubMed:27751867, PubMed:28248300). Catalyzes the last step of the synthesis of omega-O-acylceramides by transferring linoleic acid from triglycerides to an omega-hydroxyceramide (PubMed:27751867, PubMed:28248300). Omega-O-acylceramides, are required for the biogenesis of lipid lamellae in the stratum corneum and the formation of the cornified lipid envelope which are essential for the epidermis barrier function (PubMed:27751867, PubMed:28248300). These lipids also play a role in keratinocyte differentiation (PubMed:28248300). May also act on omega-hydroxylated ultra-long chain fatty acids (omega-OH ULCFA) and acylglucosylceramides (GlcEOS) (PubMed:28248300). {ECO:0000269|PubMed:27751867, ECO:0000269|PubMed:28248300}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (4); Domain (1); Motif (2); Region (1) |
| Keywords | Cytoplasm;Lipid biosynthesis;Lipid metabolism;Reference proteome;Transferase |
| Interact With | |
| Induction | INDUCTION: Up-regulated upon induced differentiation of keratinocytes. {ECO:0000269|PubMed:28248300}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N8W4}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21267068; 21677750; 27267404; 27626380; 28369476; 31356814; 31578523; |
| Motif | MOTIF 51..55; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 172..174; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 65,170 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:61528; RHEA:61529; RHEA:65692; RHEA:65693; RHEA:65648; RHEA:65649; RHEA:55264; RHEA:55265; RHEA:65652; RHEA:65653; RHEA:65668; RHEA:65669; RHEA:65672; RHEA:65673; RHEA:65676; RHEA:65677; RHEA:65680; RHEA:65681; RHEA:65684; RHEA:65685; RHEA:65688; RHEA:65689 |
| Cross Reference Brenda |