AC MF_03141; DC Protein; auto TR HAMAP; MF_03141; -; 1; level=0 XX Names: lis1 XX ID LIS1 case DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha; DE AltName: Full=Lissencephaly-1 protein; DE Short=LIS-1; DE AltName: Full=PAF acetylhydrolase 45 kDa subunit; DE Short=PAF-AH 45 kDa subunit; DE AltName: Full=PAF-AH alpha; DE Short=PAFAH alpha; else case DE RecName: Full=Nuclear distribution protein nudF; DE AltName: Full=Lissencephaly-1 homolog; DE Short=LIS-1; else case and not DE RecName: Full=Nuclear distribution protein PAC1; DE AltName: Full=Lissencephaly-1 homolog; DE Short=LIS-1; DE AltName: Full=nudF homolog; else DE RecName: Full=Lissencephaly-1 homolog; end case case GN Name=PAFAH1B1; Synonyms=LIS1; else case GN Name=Lis-1; else case GN Name=lis-1; else case GN Name=nudF; Synonyms=lis1; else case and not GN Name=PAC1; Synonyms=LIS1; end case XX case CC -!- FUNCTION: Positively regulates the activity of the minus-end directed CC microtubule motor protein dynein. May enhance dynein-mediated CC microtubule sliding by targeting dynein to the microtubule plus end. CC Required for several dynein- and microtubule-dependent processes such CC as the maintenance of Golgi integrity, the peripheral transport of CC microtubule fragments and the coupling of the nucleus and centrosome. CC Required during brain development for the proliferation of neuronal CC precursors and the migration of newly formed neurons from the CC ventricular/subventricular zone toward the cortical plate. Neuronal CC migration involves a process called nucleokinesis, whereby migrating CC cells extend an anterior process into which the nucleus subsequently CC translocates. During nucleokinesis dynein at the nuclear surface may CC translocate the nucleus towards the centrosome by exerting force on CC centrosomal microtubules. Also required for proper activation of Rho CC GTPases and actin polymerization at the leading edge of locomoting CC cerebellar neurons and postmigratory hippocampal neurons in response to CC calcium influx triggered via NMDA receptors. May also play a role in CC other forms of cell locomotion including the migration of fibroblasts CC during wound healing. Non-catalytic subunit of an acetylhydrolase CC complex which inactivates platelet-activating factor (PAF) by removing CC the acetyl group at the SN-2 position. else case and not CC -!- FUNCTION: Positively regulates the activity of the minus-end directed CC microtubule motor protein dynein. May enhance dynein-mediated CC microtubule sliding by targeting dynein to the microtubule plus end. CC Required for several dynein- and microtubule-dependent processes such CC as the maintenance of Golgi integrity, the peripheral transport of CC microtubule fragments and the coupling of the nucleus and centrosome. CC May be required for proliferation of neuronal precursors and neuronal CC migration. else case or CC -!- FUNCTION: Positively regulates the activity of the minus-end directed CC microtubule motor protein dynein. Plays a central role in positioning CC the mitotic spindle at the bud neck during cell division. Targets CC cytoplasmic dynein to microtubule plus ends, thereby promoting dynein- CC mediated microtubule sliding along the bud cortex and consequently the CC movement of the mitotic spindle to the bud neck. else case and not ( or ) CC -!- FUNCTION: Positively regulates the activity of the minus-end directed CC microtubule motor protein dynein. May enhance dynein-mediated CC microtubule sliding by targeting dynein to the microtubule plus end. CC Required for nuclear migration during vegetative growth as well as CC development. Required for retrograde early endosome (EE) transport from CC the hyphal tip. Required for localization of dynein to the mitotic CC spindle poles. Recruits additional proteins to the dynein complex at CC SPBs. else CC -!- FUNCTION: Positively regulates the activity of the minus-end directed CC microtubule motor protein dynein. May enhance dynein-mediated CC microtubule sliding by targeting dynein to the microtubule plus end. CC Required for several dynein- and microtubule-dependent processes. end case case CC -!- SUBUNIT: Can self-associate. Interacts with DCX, dynein, dynactin, CC IQGAP1, KATNB1, NDE1, NDEL1, NUDC and RSN. Interacts with DISC1, and CC this interaction is enhanced by NDEL1. Interacts with DAB1 when DAB1 is CC phosphorylated in response to RELN/reelin signaling. Component of CC cytosolic PAF-AH IB, which is composed of PAFAH1B1 (alpha), PAFAH1B2 CC (beta) and PAFAH1B3 (gamma) subunits. Trimer formation is not essential CC for the catalytic activity of the enzyme which is contributed solely by CC the PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. else case CC -!- SUBUNIT: Can self-associate. Interacts with dynein, dynactin, @gn(NDE1) CC and @gn(NDEL1). else case CC -!- SUBUNIT: Self-associates. Interacts with nudE and dynein. else case and not CC -!- SUBUNIT: Self-associates. Interacts with @gn(NDL1) and dynein. else case CC -!- SUBUNIT: May be a component of a dynein regulatory complex composed of CC at least lis-1 and nud-2. Interacts with nud-2. end case case CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, CC spindle. Nucleus membrane. Note=Localizes to the plus end of CC microtubules and to the centrosome. May localize to the nuclear CC membrane. Redistributes to axons during neuronal development. Also CC localizes to the microtubules of the manchette in elongating spermatids CC and to the meiotic spindle in spermatocytes. else case or CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC spindle pole. Note=Localizes to the plus ends of microtubules and the CC mitotic spindle poles. else case and not ( or ) CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC spindle pole. Note=Localizes to the plus ends of microtubules at the CC hyphal tip and the mitotic spindle poles. else case not CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome. Note=Localizes to the plus CC end of microtubules and to the centrosome. end case case CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to CC activate dynein. end case CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family. XX DR PROSITE; PS50896; LISH; 0-1; trigger=yes DR PROSITE; PS00678; WD_REPEATS_1; 1-6; trigger=no DR PROSITE; PS50082; WD_REPEATS_2; 1-8; trigger=no DR PROSITE; PS50294; WD_REPEATS_REGION; 1; trigger=no DR Pfam; PF08513; LisH; 1; trigger=no DR Pfam; PF00400; WD40; 7; trigger=no DR PRINTS; PR00320; GPROTEINBRPT; 1; trigger=no DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1; trigger=no DR General; Coiled_coil; -; 1-unlimited; trigger=yes DR REP; Repeat_WD40; WD40; 7-8; trigger=yes XX KW Cell cycle KW Cell division KW Coiled coil KW Cytoplasm KW Cytoskeleton KW Microtubule KW Mitosis KW Transport case KW Developmental protein KW Differentiation KW Neurogenesis end case case KW Lipid degradation KW Lipid metabolism KW Membrane KW Nucleus end case XX GO GO:0005737; C:cytoplasm GO GO:0005875; C:microtubule associated complex GO GO:0070840; F:dynein complex binding GO GO:0051012; P:microtubule sliding GO GO:0000132; P:establishment of mitotic spindle orientation GO GO:0007017; P:microtubule-based process case GO GO:0007399; P:nervous system development end case XX FT From: LIS1_HUMAN (P43034) case FT INIT_MET 1 FT /note="Removed" FT Condition: M end case case FT REGION Nter..102 FT /note="Interaction with NDEL1" FT REGION Nter..66 FT /note="Interaction with NDE1" FT REGION Nter..38 FT /note="Required for self-association and interaction with FT PAFAH1B2 and PAFAH1B3" FT REGION 83..Cter FT /note="Interaction with dynein and dynactin" FT REGION 367..409 FT /note="Interaction with DCX" FT REGION 388..Cter FT /note="Interaction with NDEL1" end case XX Size: 390-529; Related: None; Template: P43034; Q00664; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in ASPCL, CHAGB, DANRE, NEUCR, PARTE, PENCW, PENMQ, PODAN, POSPM, SALSA, SORMK, UNCRE Plasmid: None Comments: None XX # Revision 1.12 2019/11/20 //