Detail Information for IndEnz0005000749
IED ID IndEnz0005000749
Enzyme Type ID lipase000749
Protein Name Lysophospholipase-like protein 1
EC 3.1.2.22
Gene Name LYPLAL1
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 MAAASGSVLQRCIVSPAGRHSASLIFLHGSGDSGQGLRMWIKQVLNQDLTFQHIKIIYPTAPPRSYTPMKGGISNVWFDRFKITNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSNGVLPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILKLWILTKLPGEMEKQK
Enzyme Length 237
Uniprot Accession Number Q5VWZ2
Absorption
Active Site ACT_SITE 124; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 179; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 211; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMed:22399288};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000305|PubMed:22399288};
DNA Binding
EC Number 3.1.2.22
Enzyme Function FUNCTION: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site. {ECO:0000269|PubMed:22052940, ECO:0000269|PubMed:22399288}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Beta strand (11); Chain (1); Helix (8); Initiator methionine (1); Modified residue (1); Natural variant (2); Sequence conflict (1)
Keywords 3D-structure;Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Hydrolase;Reference proteome
Interact With Q8WUE5
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:22399288}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:22399288}.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 3U0V; 5KRE;
Mapped Pubmed ID 19557161; 20703240; 20724581; 20935629; 21674055; 21911578; 21953277; 22179955; 23221025; 26638075; 26848030; 27181159; 27391855; 27752939; 28645872; 29648650;
Motif
Gene Encoded By
Mass 26,316
Kinetics
Metal Binding
Rhea ID RHEA:19233; RHEA:19234
Cross Reference Brenda