LIS1_BOVIN
ID LIS1_BOVIN Reviewed; 410 AA.
AC P43033;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit beta {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000305};
DE AltName: Full=Lissencephaly-1 protein {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=PAF acetylhydrolase 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=PAF-AH 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=PAF-AH alpha {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=PAFAH alpha {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAFAH1B1 {ECO:0000250|UniProtKB:P43034,
GN ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1 {ECO:0000255|HAMAP-Rule:MF_03141}, PAFAHA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8028668; DOI=10.1038/370216a0;
RA Hattori M., Adachi H., Tsujimoto M., Arai H., Inoue K.;
RT "Miller-Dieker lissencephaly gene encodes a subunit of brain platelet-
RT activating factor acetylhydrolase.";
RL Nature 370:216-218(1994).
RN [2]
RP SUBUNIT, FUNCTION, MUTAGENESIS OF HIS-149, AND INTERACTION WITH PAFAH1B3
RP AND PAFAH1B2.
RX PubMed=10542206; DOI=10.1074/jbc.274.45.31827;
RA Manya H., Aoki J., Kato H., Ishii J., Hino S., Arai H., Inoue K.;
RT "Biochemical characterization of various catalytic complexes of the brain
RT platelet-activating factor acetylhydrolase.";
RL J. Biol. Chem. 274:31827-31832(1999).
RN [3]
RP INTERACTION WITH PAFAH1B2; PAFAH1B3 AND NDE1.
RX PubMed=10940388; DOI=10.1016/s0014-5793(00)01856-1;
RA Kitagawa M., Umezu M., Aoki J., Koizumi H., Arai H., Inoue K.;
RT "Direct association of LIS1, the lissencephaly gene product, with a
RT mammalian homologue of a fungal nuclear distribution protein, rNUDE.";
RL FEBS Lett. 479:57-62(2000).
RN [4]
RP INTERACTION WITH DYNEIN AND DYNACTIN.
RX PubMed=11056532; DOI=10.1038/35041020;
RA Faulkner N.E., Dujardin D.L., Tai C.-Y., Vaughan K.T., O'Connell C.B.,
RA Wang Y.-L., Vallee R.B.;
RT "A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein
RT function.";
RL Nat. Cell Biol. 2:784-791(2000).
RN [5]
RP FUNCTION, INTERACTION WITH DYNACTIN, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=14584027; DOI=10.1002/cm.10151;
RA Payne C., St John J.C., Ramalho-Santos J., Schatten G.;
RT "LIS1 association with dynactin is required for nuclear motility and
RT genomic union in the fertilized mammalian oocyte.";
RL Cell Motil. Cytoskeleton 56:245-251(2003).
CC -!- FUNCTION: Regulatory subunit (beta subunit) of the cytosolic type I
CC platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an
CC enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2
CC position of PAF and its analogs and participates in the PAF
CC inactivation (PubMed:10542206). Regulates the PAF-AH (I) activity in a
CC catalytic dimer composition-dependent manner (PubMed:10542206).
CC Positively regulates the activity of the minus-end directed microtubule
CC motor protein dynein. May enhance dynein-mediated microtubule sliding
CC by targeting dynein to the microtubule plus end. Required for several
CC dynein- and microtubule-dependent processes such as the maintenance of
CC Golgi integrity, the peripheral transport of microtubule fragments and
CC the coupling of the nucleus and centrosome. Required during brain
CC development for the proliferation of neuronal precursors and the
CC migration of newly formed neurons from the ventricular/subventricular
CC zone toward the cortical plate. Neuronal migration involves a process
CC called nucleokinesis, whereby migrating cells extend an anterior
CC process into which the nucleus subsequently translocates. During
CC nucleokinesis dynein at the nuclear surface may translocate the nucleus
CC towards the centrosome by exerting force on centrosomal microtubules.
CC Also required for proper activation of Rho GTPases and actin
CC polymerization at the leading edge of locomoting cerebellar neurons and
CC postmigratory hippocampal neurons in response to calcium influx
CC triggered via NMDA receptors. May also play a role in other forms of
CC cell locomotion including the migration of fibroblasts during wound
CC healing (By similarity). Required for pronuclear migration during
CC fertilization. Required for dynein recruitment to microtubule plus ends
CC and BICD2-bound cargos (By similarity). May modulate the Reelin pathway
CC through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By
CC similarity). {ECO:0000250|UniProtKB:P43034,
CC ECO:0000250|UniProtKB:P63005, ECO:0000255|HAMAP-Rule:MF_03141,
CC ECO:0000269|PubMed:10542206, ECO:0000269|PubMed:14584027}.
CC -!- SUBUNIT: Can self-associate. Component of the cytosolic PAF-AH (I)
CC heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2
CC (alpha2) and PAFAH1B3 (alpha1) subunits. The catalytic activity of the
CC enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits,
CC whereas the beta subunit (PAFAH1B1) has regulatory activity. Trimer
CC formation is not essential for the catalytic activity
CC (PubMed:10542206). Interacts with the catalytic dimer of PAF-AH (I)
CC heterotetrameric enzyme: interacts with PAFAH1B2 homodimer
CC (alpha2/alpha2 homodimer), PAFAH1B3 homodimer (alpha1/alpha1 homodimer)
CC and PAFAH1B2-PAFAH1B3 heterodimer (alpha2/alpha1 heterodimer)
CC (PubMed:10940388). Interacts with DCX, IQGAP1, KATNB1, NDEL1, NUDC and
CC RSN. Interacts with DISC1, and this interaction is enhanced by NDEL1.
CC Interacts with DAB1 when DAB1 is phosphorylated in response to
CC RELN/reelin signaling (By similarity). Interacts with dynein and NDE1
CC (PubMed:10940388, PubMed:11056532). Interacts with dynactin
CC (PubMed:11056532, PubMed:14584027). {ECO:0000250|UniProtKB:P43034,
CC ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:10542206,
CC ECO:0000269|PubMed:10940388, ECO:0000269|PubMed:11056532,
CC ECO:0000269|PubMed:14584027}.
CC -!- INTERACTION:
CC P43033; Q9ES39: Nde1; Xeno; NbExp=2; IntAct=EBI-1007886, EBI-1007897;
CC P43033; O35264: Pafah1b2; Xeno; NbExp=2; IntAct=EBI-1007886, EBI-915500;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03141, ECO:0000269|PubMed:14584027}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000255|HAMAP-
CC Rule:MF_03141, ECO:0000269|PubMed:14584027}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000255|HAMAP-Rule:MF_03141}. Nucleus membrane
CC {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of
CC microtubules and to the centrosome. Redistributes to axons during
CC neuronal development. Also localizes to the microtubules of the
CC manchette in elongating spermatids and to the meiotic spindle in
CC spermatocytes (By similarity). May localize to the nuclear membrane.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- DEVELOPMENTAL STAGE: Expression increases during fertilization of the
CC oocyte. {ECO:0000269|PubMed:14584027}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- MISCELLANEOUS: Originally the subunits of the type I platelet-
CC activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1),
CC beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity). Now these
CC subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and
CC alpha1 (PAFAH1B3) respectively (By similarity).
CC {ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P68402,
CC ECO:0000250|UniProtKB:Q15102, ECO:0000250|UniProtKB:Q29460}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000255|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 EMBL; D30615; BAA06305.1; -; mRNA.
DR RefSeq; NP_777088.1; NM_174663.2.
DR AlphaFoldDB; P43033; -.
DR SMR; P43033; -.
DR BioGRID; 159754; 2.
DR CORUM; P43033; -.
DR IntAct; P43033; 3.
DR STRING; 9913.ENSBTAP00000052656; -.
DR PaxDb; P43033; -.
DR PRIDE; P43033; -.
DR GeneID; 282513; -.
DR KEGG; bta:282513; -.
DR CTD; 5048; -.
DR eggNOG; KOG0295; Eukaryota.
DR InParanoid; P43033; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0034452; F:dynactin binding; IDA:BHF-UCL.
DR GO; GO:0070840; F:dynein complex binding; IDA:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0043274; F:phospholipase binding; IDA:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
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 GO; GO:0046469; P:platelet activating factor metabolic process; IDA:BHF-UCL.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; SSF109925; 1.
DR SUPFAM; SSF50978; SSF50978; 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; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation;
KW Direct protein sequencing; Lipid degradation; Lipid metabolism; Membrane;
KW Microtubule; Mitosis; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..410
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit beta"
FT /id="PRO_0000051060"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 106..147
FT /note="WD 1"
FT REPEAT 148..187
FT /note="WD 2"
FT REPEAT 190..229
FT /note="WD 3"
FT REPEAT 232..271
FT /note="WD 4"
FT REPEAT 274..333
FT /note="WD 5"
FT REPEAT 336..377
FT /note="WD 6"
FT REPEAT 378..410
FT /note="WD 7"
FT REGION 1..102
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 1..66
FT /note="Interaction with NDE1"
FT /evidence="ECO:0000269|PubMed:10940388"
FT REGION 1..38
FT /note="Required for self-association and interaction with
FT PAFAH1B2 and PAFAH1B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 83..410
FT /note="Interaction with dynein and dynactin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 367..409
FT /note="Interaction with DCX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REGION 388..410
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COILED 56..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43034"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43034"
FT MUTAGEN 149
FT /note="H->R: Loss of binding to the catalytic dimers. Loss
FT of the ability to regulate PAF-AH (I) activity."
FT /evidence="ECO:0000269|PubMed:10542206"
SQ SEQUENCE 410 AA; 46613 MW; FE5C2DF0AB98F3B4 CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEAAYSV FKKEAELDMN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVEDISFDH 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
