Detail Information for IndEnz0010000477
IED ID IndEnz0010000477
Enzyme Type ID esterase000477
Protein Name Lysophospholipase NTE1
EC 3.1.1.5
Intracellular phospholipase B
Neuropathy target esterase homolog
Gene Name nte1 SPCC4B3.04c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Enzyme Sequence MDITDRILQNRIVSKVIFFVLRSVTLSLVSVTRFSLFLLSFATITVPKWAYKIVTYSLTIQFNFKSLLFLFFVSICVVILVVRYRYLNKYARLPHEAPIKEAKLGPDTNIRPSEPRIGFQNYLDEFLSAISIFGYLEKPVFVELARHIRTQRVAEGNTIYLGEQSSFILVVDGCFQVFTAPEKDSAEVVEEAGQPEYRLLTEVSNGAPLSSFFTVLELFTELIPEATSKENPFKSTTSSLRPGSSTTTEAGANNASKPHMPQPKKARIIAKAKIDTTIAVIPANAFHHLVHKFPNSSAQIVQVILTRFQRVTFSTGYEYLGLSDAIFSIEKNFNSLTAYELPNYIRSDIIDDFKKEAMSEHLSQASNESFIVLRSKGAQSRLSNQYFSKAFDKEHGNFVSDIDRSTANAGDLLSSTNPHSTLLSTSVGPLRKFPLNRSYSREVGDYDISASFRDGLLQCIFKSLGVFNYELKEDNDDLCTENDSSEGDSDSLKKVDFLGQIAMMSATDREEVKSSIVVSTKKSTILEFAKEIEIIFYKKGTTIVRQGDHADGLYYIIDGFLDATCPSKLTFSTSYDTDLGMHSFMIKPGGIVNYQACVSNYRSFINVTARSDVLVGFLPRSCLERIIDQEPLISLTIAKRLISLVPSLLLKLDFAVGWIHLNPDQVVYEKNDPSDCVYVVLNGRLRSIEDERGSARTQVDYFNEYGKGDSVGELEMLLNNRRSSTLFAIRDSELAKIPETLFNALSLSHPAVGLQLSKIIANRMNLLLNNKSMDGMQHQPHEKHSIRTLAIVPSSSTGLLILFSQKLTSVLSVMGKSVKVLRQSSVLEHLGKHAFSRMGRFKLSSYLSDLEDKYDILIYVADSGVGSAWLQTCIRQADCIYILAEADQNPNIGEYEQHLIAMKSTARKELVLLHPERFCPSGLTRLWLKERPWVYAHHHVQLRIGLDNEISQNNEAKVFLNIIRAKVQNLHYGFRKYIDWKHLHPVYQANRAQDSDFARLARRICGKAIALVLGGGGARGISQIGILYALEEAGIPFDIIGGTSIGAFNGGLYAWEADLVPMFGRAKKFCGRMANLWRFVLDVTYPQAAYTTGHEFNRGIWKTFGEIHIEDFWLPFYANTTNITHSRMDIHSSGYAWRYIRASMSLAGLVPPMLSDSGDMLLDGGYMDNLTVSHMQSLGASSIFAIDVGSEDSREPMHYGDTVSGVWALISRWIPFIPKTSFPSLAEIQSRLTYVTSVATGEKVKSMPGCFYMRPPVKDFPTLEFGSFEKIYNVGYNYGKEYVEKLKTSHKLDDILSPRDTSKRHPKFLSSRRNSL
Enzyme Length 1316
Uniprot Accession Number Q9USJ4
Absorption
Active Site ACT_SITE 1044; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 1163; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Activity Regulation ACTIVITY REGULATION: Inhibited by organophosphorus esters. {ECO:0000250}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
DNA Binding
EC Number 3.1.1.5
Enzyme Function FUNCTION: Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 516..644; /note=cNMP 1; NP_BIND 640..763; /note=cNMP 2
Features Active site (2); Chain (1); Compositional bias (1); Domain (1); Motif (3); Nucleotide binding (2); Region (2); Topological domain (3); Transmembrane (2)
Keywords Endoplasmic reticulum;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Reference proteome;Repeat;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20473289; 21712547; 23697806; 24763107; 25720772; 30726745; 33823663;
Motif MOTIF 1015..1020; /note=GXGXXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1042..1046; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; MOTIF 1163..1165; /note=DGA/G; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161
Gene Encoded By
Mass 147,846
Kinetics
Metal Binding
Rhea ID RHEA:15177
Cross Reference Brenda