LIS1_XENLA
ID LIS1_XENLA Reviewed; 410 AA.
AC Q90ZL4; Q6DE72;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=pafah1b1; Synonyms=lis1 {ECO:0000255|HAMAP-Rule:MF_03141};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Hayashi M.A.F., Hongo I., Okamoto H.;
RT "Xenopus laevis LIS1.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 PAF inactivation.
CC Regulates the PAF-AH (I) activity in a catalytic dimer composition-
CC dependent manner (By similarity). Positively regulates the activity of
CC the minus-end directed microtubule motor protein dynein. May enhance
CC dynein-mediated microtubule sliding by targeting dynein to the
CC microtubule plus end. Required for several dynein- and microtubule-
CC dependent processes such as the maintenance of Golgi integrity, the
CC peripheral transport of microtubule fragments and the coupling of the
CC nucleus and centrosome. May be required for proliferation of neuronal
CC precursors and neuronal migration. {ECO:0000250|UniProtKB:P43033,
CC ECO:0000255|HAMAP-Rule:MF_03141}.
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 (By similarity).
CC Interacts with dynein, dynactin, nde1 and ndel1.
CC {ECO:0000250|UniProtKB:P43033, ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the
CC plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-
CC Rule:MF_03141}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
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DR EMBL; AY032881; AAK52334.1; -; mRNA.
DR EMBL; BC077270; AAH77270.1; -; mRNA.
DR RefSeq; NP_001083934.1; NM_001090465.1.
DR AlphaFoldDB; Q90ZL4; -.
DR SMR; Q90ZL4; -.
DR IntAct; Q90ZL4; 2.
DR GeneID; 399199; -.
DR KEGG; xla:399199; -.
DR CTD; 399199; -.
DR Xenbase; XB-GENE-17330834; pafah1b1.L.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 399199; Expressed in testis and 19 other tissues.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS: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:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-UniRule.
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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Microtubule; Mitosis; Neurogenesis;
KW Reference proteome; Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT CHAIN 2..410
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000240419"
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..189
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 379..410
FT /note="WD 7"
FT COILED 56..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT CONFLICT 45
FT /note="I -> K (in Ref. 2; AAH77270)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="L -> I (in Ref. 2; AAH77270)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="R -> K (in Ref. 2; AAH77270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46762 MW; 228D3F6173B4C66C CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDIKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPIGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVTASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ
GFECLRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY STISDATGSE
TKRSGKPGPF LLSGSRDKTI KMWDISIGMC LMTLVGHDNW VRGVQFHPGG KFILSCADDK
TIRIWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
