LIS1_RAT
ID LIS1_RAT Reviewed; 410 AA.
AC P63004; O35592; P43035; P81692; Q9R2A6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha {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:0000312|RGD:620331}; Synonyms=Lis-1, Lis1, Pafaha;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9459487; DOI=10.1016/s0167-4889(97)00128-6;
RA Watanabe M., Aoki J., Manya H., Arai H., Inoue K.;
RT "Molecular cloning of cDNAs encoding alpha1, alpha2, and beta subunits of
RT rat brain platelet-activating factor acetylhydrolase.";
RL Biochim. Biophys. Acta 1401:73-79(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9660828; DOI=10.1074/jbc.273.29.18567;
RA Manya H., Aoki J., Watanabe M., Adachi T., Asou H., Inoue Y., Arai H.,
RA Inoue K.;
RT "Switching of platelet-activating factor acetylhydrolase catalytic subunits
RT in developing rat brain.";
RL J. Biol. Chem. 273:18567-18572(1998).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11001923; DOI=10.1093/oxfordjournals.hmg.a018911;
RA Caspi M., Atlas R., Kantor A., Sapir T., Reiner O.;
RT "Interaction between LIS1 and doublecortin, two lissencephaly gene
RT products.";
RL Hum. Mol. Genet. 9:2205-2213(2000).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11056530; DOI=10.1038/35041000;
RA Smith D.S., Niethammer M., Ayala R., Zhou Y., Gambello M.J.,
RA Wynshaw-Boris A., Tsai L.-H.;
RT "Regulation of cytoplasmic dynein behaviour and microtubule organization by
RT mammalian Lis1.";
RL Nat. Cell Biol. 2:767-775(2000).
RN [6]
RP FUNCTION.
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 [7]
RP INTERACTION WITH NDEL1 AND DYNEIN.
RC TISSUE=Brain;
RX PubMed=11163260; DOI=10.1016/s0896-6273(00)00147-1;
RA Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
RA Morabito M., Tsai L.-H.;
RT "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic
RT dynein.";
RL Neuron 28:697-711(2000).
RN [8]
RP FUNCTION.
RX PubMed=16144905; DOI=10.1083/jcb.200505166;
RA Tsai J.-W., Chen Y., Kriegstein A.R., Vallee R.B.;
RT "LIS1 RNA interference blocks neural stem cell division, morphogenesis, and
RT motility at multiple stages.";
RL J. Cell Biol. 170:935-945(2005).
RN [9]
RP INTERACTION WITH DYNEIN, AND SUBCELLULAR LOCATION.
RX PubMed=16481446; DOI=10.1523/jneurosci.5095-05.2006;
RA Mesngon M.T., Tarricone C., Hebbar S., Guillotte A.M., Schmitt E.W.,
RA Lanier L., Musacchio A., King S.J., Smith D.S.;
RT "Regulation of cytoplasmic dynein ATPase by Lis1.";
RL J. Neurosci. 26:2132-2139(2006).
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). 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. Positively regulates the
CC activity of the minus-end directed microtubule motor protein dynein.
CC May enhance dynein-mediated microtubule sliding by targeting dynein to
CC the 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. Required during brain development for the
CC proliferation of neuronal precursors and the migration of newly formed
CC neurons from the ventricular/subventricular zone toward the cortical
CC plate. Neuronal migration involves a process called nucleokinesis,
CC whereby migrating cells extend an anterior process into which the
CC nucleus subsequently translocates. During nucleokinesis dynein at the
CC nuclear surface may translocate the nucleus towards the centrosome by
CC exerting force on centrosomal microtubules. May also play a role in
CC other forms of cell locomotion including the migration of fibroblasts
CC during wound healing. Required for dynein recruitment to microtubule
CC plus ends and BICD2-bound cargos (By similarity). May modulate the
CC Reelin pathway through interaction of the PAF-AH (I) catalytic dimer
CC with VLDLR (By similarity). {ECO:0000250|UniProtKB:P43033,
CC ECO:0000250|UniProtKB:P43034, ECO:0000250|UniProtKB:P63005,
CC ECO:0000269|PubMed:11056532, ECO:0000269|PubMed:16144905}.
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. Interacts with
CC the catalytic dimer of PAF-AH (I) heterotetrameric enzyme: interacts
CC with PAFAH1B2 homodimer (alpha2/alpha2 homodimer), PAFAH1B3 homodimer
CC (alpha1/alpha1 homodimer) and PAFAH1B2-PAFAH1B3 heterodimer
CC (alpha2/alpha1 heterodimer) (By similarity). Interacts with DCX,
CC dynactin, IQGAP1, KATNB1, NDE1, 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. Interacts with
CC dynein and NDEL1 (PubMed:11163260, PubMed:16481446). Interacts with
CC INTS13. Interacts with DCDC1 (By similarity).
CC {ECO:0000250|UniProtKB:P43033, ECO:0000250|UniProtKB:P43034,
CC ECO:0000250|UniProtKB:P63005, ECO:0000269|PubMed:11163260,
CC ECO:0000269|PubMed:16481446}.
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}. 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. May localize to the nuclear
CC membrane. Also localizes to the microtubules of the manchette in
CC elongating spermatids and to the meiotic spindle in spermatocytes (By
CC similarity). Redistributes to axons during neuronal development.
CC {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11001923,
CC ECO:0000269|PubMed:11056530, ECO:0000269|PubMed:16481446}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, with highest expression
CC in brain. Expressed in fetal and adult brain. In neural cells,
CC expressed in granule cells, astroglial cells, and oligodendrocytes
CC (PubMed:9660828). {ECO:0000269|PubMed:9459487,
CC ECO:0000269|PubMed:9660828}.
CC -!- DEVELOPMENTAL STAGE: During the embryonic stages, high expressed in the
CC brain, spinal cord, sensory ganglia (dorsal root and trigeminal
CC ganglia), and thymus. In brain found throughout the ventricular and
CC marginal zones. {ECO:0000269|PubMed:9660828}.
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}.
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DR EMBL; AF016049; AAC27975.1; -; mRNA.
DR EMBL; BC072510; AAH72510.1; -; mRNA.
DR RefSeq; NP_113951.1; NM_031763.3.
DR RefSeq; XP_017453039.1; XM_017597550.1.
DR AlphaFoldDB; P63004; -.
DR SMR; P63004; -.
DR BioGRID; 249758; 2.
DR IntAct; P63004; 2.
DR MINT; P63004; -.
DR STRING; 10116.ENSRNOP00000003696; -.
DR iPTMnet; P63004; -.
DR PhosphoSitePlus; P63004; -.
DR SwissPalm; P63004; -.
DR World-2DPAGE; 0004:P63004; -.
DR jPOST; P63004; -.
DR PaxDb; P63004; -.
DR PRIDE; P63004; -.
DR Ensembl; ENSRNOT00000003696; ENSRNOP00000003696; ENSRNOG00000002755.
DR GeneID; 83572; -.
DR KEGG; rno:83572; -.
DR CTD; 5048; -.
DR RGD; 620331; Pafah1b1.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; P63004; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR PhylomeDB; P63004; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:P63004; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002755; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P63004; RN.
DR GO; GO:0008247; C:1-alkyl-2-acetylglycerophosphocholine esterase complex; IDA:UniProtKB.
DR GO; GO:0000235; C:astral microtubule; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0090724; C:central region of growth cone; IDA:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0005871; C:kinesin complex; IDA:RGD.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0031514; C:motile cilium; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032420; C:stereocilium; ISO:RGD.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0045505; F:dynein intermediate chain binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; TAS:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0001675; P:acrosome assembly; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0001667; P:ameboidal-type cell migration; ISO:RGD.
DR GO; GO:0060117; P:auditory receptor cell development; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0021540; P:corpus callosum morphogenesis; ISO:RGD.
DR GO; GO:0043622; P:cortical microtubule organization; ISO:RGD.
DR GO; GO:0051660; P:establishment of centrosome localization; IMP:RGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:RGD.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; ISO:RGD.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051661; P:maintenance of centrosome location; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; ISO:RGD.
DR GO; GO:0031023; P:microtubule organizing center organization; ISO:RGD.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007017; P:microtubule-based process; ISO:RGD.
DR GO; GO:0097529; P:myeloid leukocyte migration; IEA:Ensembl.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; IMP:RGD.
DR GO; GO:0051081; P:nuclear membrane disassembly; ISO:RGD.
DR GO; GO:0007097; P:nuclear migration; IMP:RGD.
DR GO; GO:0036035; P:osteoclast development; ISO:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0051130; P:positive regulation of cellular component organization; ISO:RGD.
DR GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:RGD.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISO:RGD.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:RGD.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
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:0043087; P:regulation of GTPase activity; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0008090; P:retrograde axonal transport; ISO:RGD.
DR GO; GO:0017145; P:stem cell division; IMP:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISO:RGD.
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; Lipid degradation;
KW Lipid metabolism; Membrane; Microtubule; Mitosis; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..410
FT /note="Platelet-activating factor acetylhydrolase IB
FT subunit alpha"
FT /id="PRO_0000051065"
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:0000255|HAMAP-Rule:MF_03141"
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"
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
