ID A0A1S2ZKN5_ERIEU Unreviewed; 410 AA.
AC A0A1S2ZKN5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000256|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 protein {ECO:0000256|HAMAP-Rule:MF_03141};
DE Short=LIS-1 {ECO:0000256|HAMAP-Rule:MF_03141};
DE AltName: Full=PAF acetylhydrolase 45 kDa subunit {ECO:0000256|HAMAP-Rule:MF_03141};
DE Short=PAF-AH 45 kDa subunit {ECO:0000256|HAMAP-Rule:MF_03141};
DE AltName: Full=PAF-AH alpha {ECO:0000256|HAMAP-Rule:MF_03141};
DE Short=PAFAH alpha {ECO:0000256|HAMAP-Rule:MF_03141};
GN Name=PAFAH1B1 {ECO:0000256|HAMAP-Rule:MF_03141,
GN ECO:0000313|RefSeq:XP_007520845.1};
GN Synonyms=LIS1 {ECO:0000256|HAMAP-Rule:MF_03141};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007520845.1};
RN [1] {ECO:0000313|RefSeq:XP_007520845.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|HAMAP-
CC Rule:MF_03141}.
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. {ECO:0000256|HAMAP-
CC Rule:MF_03141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000256|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000256|HAMAP-Rule:MF_03141}. Nucleus membrane
CC {ECO:0000256|HAMAP-Rule:MF_03141}. 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. {ECO:0000256|HAMAP-
CC Rule:MF_03141}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000256|HAMAP-Rule:MF_03141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007520845.1; XM_007520783.2.
DR AlphaFoldDB; A0A1S2ZKN5; -.
DR SMR; A0A1S2ZKN5; -.
DR STRING; 9365.ENSEEUP00000008133; -.
DR CTD; 5048; -.
DR eggNOG; KOG0295; Eukaryota.
DR InParanoid; A0A1S2ZKN5; -.
DR OrthoDB; 1798470at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-UniRule.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03141; lis1; 1.
DR InterPro; IPR017252; Dynein_regulator_LIS1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA; 1.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 6.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03141};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP-
KW Rule:MF_03141}; Developmental protein {ECO:0000256|HAMAP-Rule:MF_03141};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP-
KW Rule:MF_03141}; Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03141};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03141};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|HAMAP-Rule:MF_03141};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902, ECO:0000256|HAMAP-
KW Rule:MF_03141}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03141};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03141};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
FT REPEAT 104..145
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 146..187
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 188..229
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 230..271
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 308..333
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 334..375
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 376..410
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..102
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
FT REGION 1..66
FT /note="Interaction with NDE1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
FT REGION 1..38
FT /note="Required for self-association and interaction with
FT PAFAH1B2 and PAFAH1B3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
FT REGION 83..410
FT /note="Interaction with dynein and dynactin"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
FT REGION 388..410
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03141"
SQ SEQUENCE 410 AA; 46670 MW; 4DBF6A24A6B131CD CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK
TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
//
