| IED ID | IndEnz0010000696 |
| Enzyme Type ID | esterase000696 |
| Protein Name |
Platelet-activating factor acetylhydrolase IB subunit beta Lissencephaly-1 protein LIS-1 PAF acetylhydrolase 45 kDa subunit PAF-AH 45 kDa subunit PAF-AH alpha PAFAH alpha |
| Gene Name | Pafah1b1 Lis-1 Lis1 Pafaha |
| 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 | MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR |
| Enzyme Length | 410 |
| Uniprot Accession Number | P63005 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos (By similarity). May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (PubMed:17330141). {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034, ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:11344260, ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:12911752, ECO:0000269|PubMed:14507966, ECO:0000269|PubMed:14578885, ECO:0000269|PubMed:14691133, ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:15473966, ECO:0000269|PubMed:16107726, ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:16369480, ECO:0000269|PubMed:16481446, ECO:0000269|PubMed:17330141}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (30); Chain (1); Coiled coil (1); Domain (1); Helix (6); Modified residue (2); Mutagenesis (9); Region (6); Repeat (7); Turn (5) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Cell cycle;Cell division;Coiled coil;Cytoplasm;Cytoskeleton;Developmental protein;Differentiation;Direct protein sequencing;Lipid degradation;Lipid metabolism;Membrane;Microtubule;Mitosis;Neurogenesis;Nucleus;Phosphoprotein;Reference proteome;Repeat;Transport;WD repeat |
| Interact With | Q9ERR1; Q61205; Q9GZM8 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Nucleus membrane {ECO:0000255|HAMAP-Rule:MF_03141}. Note=May localize to the nuclear membrane (By similarity). Localizes to the plus end of microtubules and to the centrosome. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes. {ECO:0000250}. |
| Modified Residue | MOD_RES 53; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P43034; MOD_RES 109; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P43034 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1UUJ; 1VYH; |
| Mapped Pubmed ID | 10026115; 10371146; 10393212; 10403203; 10491172; 10541472; 10729324; 11159375; 11172053; 11210178; 11803439; 11911856; 12130536; 12200366; 12520002; 12629176; 12775763; 12904583; 12905154; 13129914; 14610273; 14681479; 15208636; 15331402; 15762842; 15998744; 16141072; 16172262; 16445939; 16602821; 16615898; 17130546; 17148952; 17314247; 17433713; 17555748; 17881479; 17903175; 17967808; 17997972; 18075262; 18075263; 18267077; 18331715; 18434304; 18446829; 18469343; 18514414; 18524253; 18799693; 18809722; 18983980; 19515951; 19734909; 19861636; 19874786; 19938147; 20007476; 20181597; 20360068; 20364144; 20531249; 20620871; 20624590; 21092859; 21183738; 21267068; 21350014; 21423666; 21515572; 21734362; 21844209; 21911489; 21935943; 22028625; 22073305; 22114287; 22522921; 22973010; 23483698; 23483716; 23533177; 23673330; 23783758; 23830831; 23926272; 24030547; 24487275; 24812355; 24853954; 24952961; 25245017; 25698733; 26079645; 26098214; 26496610; 26834590; 27029586; 2740347; 27994513; 28039900; 28446568; 28630356; 28836069; 29150182; 29404402; 29470990; 29475944; 29562183; 30923192; 31027966; 31073041; 31474834; 33150866; 7767001; 8619131; 8954729; 9199935; 9601647; 9623676; 9697693; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,670 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |