LIS1A_DANRE
ID LIS1A_DANRE Reviewed; 410 AA.
AC Q7T394; Q07DR1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Lissencephaly-1 homolog A {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha a {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=pafah1b1a; Synonyms=lis1b {ECO:0000255|HAMAP-Rule:MF_03141};
GN ORFNames=si:dkey-95O3.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17785424; DOI=10.1073/pnas.0700178104;
RA Tsujikawa M., Omori Y., Biyanwila J., Malicki J.;
RT "Mechanism of positioning the cell nucleus in vertebrate photoreceptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14819-14824(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) 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; DQ141217; ABA29742.1; -; mRNA.
DR EMBL; BX324162; CAX13814.1; -; Genomic_DNA.
DR EMBL; BC053205; AAH53205.1; -; mRNA.
DR RefSeq; NP_958502.1; NM_201345.1.
DR RefSeq; XP_005157632.1; XM_005157575.3.
DR AlphaFoldDB; Q7T394; -.
DR SMR; Q7T394; -.
DR STRING; 7955.ENSDARP00000042217; -.
DR PaxDb; Q7T394; -.
DR Ensembl; ENSDART00000042218; ENSDARP00000042217; ENSDARG00000032013.
DR Ensembl; ENSDART00000190690; ENSDARP00000156578; ENSDARG00000032013.
DR GeneID; 394246; -.
DR KEGG; dre:394246; -.
DR CTD; 394246; -.
DR ZFIN; ZDB-GENE-040116-2; pafah1b1a.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q7T394; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR PhylomeDB; Q7T394; -.
DR TreeFam; TF105741; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DRE-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-DRE-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-DRE-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-DRE-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-DRE-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-DRE-8854518; AURKA Activation by TPX2.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q7T394; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000032013; Expressed in testis and 48 other tissues.
DR ExpressionAtlas; Q7T394; baseline and differential.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:ZFIN.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IMP:ZFIN.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
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 A"
FT /id="PRO_0000240416"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 106..145
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..375
FT /note="WD 6"
FT REPEAT 378..410
FT /note="WD 7"
FT COILED 56..83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 410 AA; 46513 MW; 36420812E74F8DF5 CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEIN IGGPIGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVIVSASEDA TIKVWDHETG DFERTLKGHT DSVQDISFDH TGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VATGYCVKTF TGHREWVRMV
RPNQDGTLIA SSSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESAH PTILEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDVSIGMC LMTLVGHDNW VRGVLVHPGG KYIVSCADDK
TLRIWDYKNK RCTKTLSAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
