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 |