ID LIS1_CHICK Reviewed; 410 AA.
AC Q9PTR5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 161.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAFAH1B1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1 {ECO:0000255|HAMAP-Rule:MF_03141};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=10603088; DOI=10.1007/s004270050010;
RA Shmueli O., Reiner O.;
RT "Expression of chLIS1, a chicken homolog of LIS1.";
RL Dev. Genes Evol. 210:51-54(2000).
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 -!- DEVELOPMENTAL STAGE: Expressed in the intermediate and lateral
CC mesoderm, posterior neural tube, notochord and somites of stage 9
CC embryos. Expressed in the neural tube, roof plate, notochord, somites,
CC dermomymotomes and eye of stage 20 embryos. This expression pattern
CC persists in stage 27 embryos, where expression is also seen in the
CC heart, intestine and dorsal aorta. Weakly and uniformly expressed in
CC the stage 35 embryo. {ECO:0000269|PubMed:10603088}.
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; AF113946; AAF18938.1; -; mRNA.
DR RefSeq; NP_989655.1; NM_204324.1.
DR RefSeq; XP_015151145.1; XM_015295659.1.
DR RefSeq; XP_015151146.1; XM_015295660.1.
DR RefSeq; XP_015151147.1; XM_015295661.1.
DR AlphaFoldDB; Q9PTR5; -.
DR SMR; Q9PTR5; -.
DR STRING; 9031.ENSGALP00000009354; -.
DR PaxDb; 9031-ENSGALP00000009354; -.
DR Ensembl; ENSGALT00000086604; ENSGALP00000064620; ENSGALG00000005834.
DR Ensembl; ENSGALT00010071537.1; ENSGALP00010044227.1; ENSGALG00010029593.1.
DR Ensembl; ENSGALT00015054657; ENSGALP00015032787; ENSGALG00015022365.
DR GeneID; 374224; -.
DR KEGG; gga:374224; -.
DR CTD; 5048; -.
DR VEuPathDB; HostDB:geneid_374224; -.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q9PTR5; -.
DR OMA; GAHEGPF; -.
DR OrthoDB; 1798470at2759; -.
DR PhylomeDB; Q9PTR5; -.
DR TreeFam; TF105741; -.
DR Reactome; R-GGA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR Reactome; R-GGA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-GGA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-GGA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-GGA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-GGA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-GGA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-GGA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-GGA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-GGA-68877; Mitotic Prometaphase.
DR Reactome; R-GGA-8854518; AURKA Activation by TPX2.
DR Reactome; R-GGA-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q9PTR5; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000005834; Expressed in brain and 14 other cell types or tissues.
DR ExpressionAtlas; Q9PTR5; baseline and differential.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; ISS:UniProtKB.
DR GO; GO:0000235; C:astral microtubule; IEA:Ensembl.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IEA:Ensembl.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0032420; C:stereocilium; IEA:Ensembl.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0001675; P:acrosome assembly; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
DR GO; GO:0060117; P:auditory receptor cell development; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0021540; P:corpus callosum morphogenesis; IEA:Ensembl.
DR GO; GO:0043622; P:cortical microtubule organization; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:1904936; P:interneuron migration; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0051661; P:maintenance of centrosome location; IEA:Ensembl.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IEA:Ensembl.
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:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0097529; P:myeloid leukocyte migration; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0051081; P:nuclear membrane disassembly; IEA:Ensembl.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0040019; P:positive regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IEA:Ensembl.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
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; PTHR19848:SF8; E3 UBIQUITIN-PROTEIN LIGASE TRAF7; 1.
DR PANTHER; PTHR19848; WD40 REPEAT PROTEIN; 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; 5.
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_0000240415"
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 COILED 56..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 410 AA; 46664 MW; FC5848D06E0DCA20 CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH TGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY STISEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDISTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK
TLRVWDFKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR
//
