| IED ID | IndEnz0005000410 |
| Enzyme Type ID | lipase000410 |
| Protein Name |
Phospholipase DDHD2 EC 3.1.1.- DDHD domain-containing protein 2 SAM, WWE and DDHD domain-containing protein 1 |
| Gene Name | Ddhd2 Kiaa0725 Samwd1 |
| 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 | MSSGESHQEQLSQSDPSPSPNSCSSFELIDMDASSSYEPVSPHWFYCKVLDSKELWIPFNSEDSQQLEDAYGSGKDCNERIVPTDGGRYDVHLGERMRYAVYWDELPSEVRRCTWFYKGDKDNKYVPYSESFSQVLEDTYMLAVTLDEWKKKIESPNREIIVLHNPKLMVHYQPIAGSDEWGSTSTEQGRPRSVKRGVENIPVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENEQIGRVEFLPVNWHSPLHSTGVDIDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIVDTVASEMNRIYTLFLQRNPDFKGGVSIAGHSLGSLILFDILTNQKNSIGDIDSEKGSLSSAEDRGDASTLEEDLKKLQLSEFVTVFEKEKVDREALALCTDRDLQEMGIPLGPRKKILNHFSARKNSVSINRPAMSASEVNISKENGDYLDVGIGQVSVKYPRLNYKPEIFFAFGSPIGMFLTVRGLRRIDPNYKFPTCKGFFNIYHPFDPVAYRIEPMVAPGIEFEPMLIPHHKGRKRMHLELREGLTRMSMDLKNNLLGSLRMAWKSFTRGPYPALQASETAEETEAEPESSSEKSNEANTEEPPVEVKEEAPISVGMLNGGQRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTVLLVLKEIYQTQGVFLDQPLQ |
| Enzyme Length | 699 |
| Uniprot Accession Number | Q80Y98 |
| Absorption | |
| Active Site | ACT_SITE 351; /evidence=ECO:0000305 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:45128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74546, ChEBI:CHEBI:77593; Evidence={ECO:0000250|UniProtKB:O94830};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45129; Evidence={ECO:0000250|UniProtKB:O94830}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839, ChEBI:CHEBI:77593; Evidence={ECO:0000250|UniProtKB:O94830};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000250|UniProtKB:O94830}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:45132, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73007, ChEBI:CHEBI:76088; Evidence={ECO:0000250|UniProtKB:O94830};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45133; Evidence={ECO:0000250|UniProtKB:O94830}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+) + hexadecanoate; Xref=Rhea:RHEA:43968, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75029, ChEBI:CHEBI:77342; Evidence={ECO:0000250|UniProtKB:O94830};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43969; Evidence={ECO:0000250|UniProtKB:O94830}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:O94830};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784; Evidence={ECO:0000250|UniProtKB:O94830}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (4); Chain (1); Compositional bias (1); Domain (3); Erroneous initiation (2); Frameshift (1); Modified residue (1); Region (2); Sequence conflict (2) |
| Keywords | Alternative splicing;Cytoplasm;Golgi apparatus;Hydrolase;Lipid degradation;Lipid metabolism;Phosphoprotein;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Note=Cycles between the Golgi apparatus and the cytosol. DDHD2 recruitment to the Golgi/endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is regulated by the levels of phosphoinositides, including PI(4)P (By similarity). {ECO:0000250}. |
| Modified Residue | MOD_RES 447; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12520002; 14610273; 21267068; 21677750; 24599962; 25267624; 29278326; 30038238; 9119401; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,577 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:45128; RHEA:45129; RHEA:40943; RHEA:40944; RHEA:45132; RHEA:45133; RHEA:43968; RHEA:43969; RHEA:38783; RHEA:38784 |
| Cross Reference Brenda |