Detail Information for IndEnz0005000668
IED ID IndEnz0005000668
Enzyme Type ID lipase000668
Protein Name Lipase member H
LIPH
EC 3.1.1.-
LPD lipase-related protein
Membrane-associated phosphatidic acid-selective phospholipase A1-alpha
mPA-PLA1 alpha
Phospholipase A1 member B
Gene Name LIPH LPDLR MPAPLA1 PLA1B
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MLRFYLFISLLCLSRSDAEETCPSFTRLSFHSAVVGTGLNVRLMLYTRKNLTCAQTINSSAFGNLNVTKKTTFIVHGFRPTGSPPVWMDDLVKGLLSVEDMNVVVVDWNRGATTLIYTHASSKTRKVAMVLKEFIDQMLAEGASLDDIYMIGVSLGAHISGFVGEMYDGWLGRITGLDPAGPLFNGKPHQDRLDPSDAQFVDVIHSDTDALGYKEPLGNIDFYPNGGLDQPGCPKTILGGFQYFKCDHQRSVYLYLSSLRESCTITAYPCDSYQDYRNGKCVSCGTSQKESCPLLGYYADNWKDHLRGKDPPMTKAFFDTAEESPFCMYHYFVDIITWNKNVRRGDITIKLRDKAGNTTESKINHEPTTFQKYHQVSLLARFNQDLDKVAAISLMFSTGSLIGPRYKLRILRMKLRSLAHPERPQLCRYDLVLMENVETVFQPILCPELQL
Enzyme Length 451
Uniprot Accession Number Q8WWY8
Absorption
Active Site ACT_SITE 154; /note=Nucleophile; ACT_SITE 178; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 248; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by sodium vanadate. {ECO:0000269|PubMed:12963729}.
Binding Site
Calcium Binding
catalytic Activity 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:0000269|PubMed:12963729};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000305|PubMed:12963729};
DNA Binding
EC Number 3.1.1.-
Enzyme Function FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2-acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid. Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG). {ECO:0000269|PubMed:12063250, ECO:0000269|PubMed:12963729}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (4); Erroneous initiation (1); Glycosylation (3); Mutagenesis (1); Natural variant (2); Signal peptide (1)
Keywords Cell membrane;Disease variant;Disulfide bond;Glycoprotein;Heparin-binding;Hydrolase;Hypotrichosis;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12963729}. Cell membrane {ECO:0000269|PubMed:12063250, ECO:0000269|PubMed:12963729}; Peripheral membrane protein.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17333281; 18445047; 18795930; 18820939; 19262606; 19536142; 19766349; 19892526; 20107739; 20213768; 21352330; 21426374; 21857648; 22125978; 22475755; 23066499; 23550552; 24380866; 24586639; 24628704; 25123262; 25201209; 25899282; 26341494; 26645693; 27375176; 27641630; 27763569; 28425126; 29346610; 29974973; 30651409; 32618099;
Motif
Gene Encoded By
Mass 50,859
Kinetics
Metal Binding
Rhea ID RHEA:40943; RHEA:40944
Cross Reference Brenda 3.1.1.32;