LIS1_IXOSC
ID LIS1_IXOSC Reviewed; 411 AA.
AC B7PS00;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN ORFNames=IscW_ISCW007420;
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel;
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC microtubule motor protein dynein. May enhance dynein-mediated
CC microtubule sliding by targeting dynein to the microtubule plus end.
CC Required for several dynein- and microtubule-dependent processes.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC09372.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS775781; EEC09372.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002401479.1; XM_002401435.1.
DR AlphaFoldDB; B7PS00; -.
DR SMR; B7PS00; -.
DR STRING; 6945.B7PS00; -.
DR PRIDE; B7PS00; -.
DR EnsemblMetazoa; ISCI007420-RA; ISCI007420-PA; ISCI007420.
DR GeneID; 8030493; -.
DR KEGG; isc:IscW_ISCW007420; -.
DR VEuPathDB; VectorBase:ISCI007420; -.
DR VEuPathDB; VectorBase:ISCW007420; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; B7PS00; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
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:0048854; P:brain morphogenesis; IBA:GO_Central.
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: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; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..411
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000405052"
FT DOMAIN 7..39
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 104..145
FT /note="WD 1"
FT REPEAT 146..187
FT /note="WD 2"
FT REPEAT 188..227
FT /note="WD 3"
FT REPEAT 230..269
FT /note="WD 4"
FT REPEAT 272..334
FT /note="WD 5"
FT REPEAT 337..376
FT /note="WD 6"
FT REPEAT 379..411
FT /note="WD 7"
FT REGION 77..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 77..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 46091 MW; 66F5205DCC6E48C7 CRC64;
MVLSQRQREE LNKAIADYLA SNGFMEALES FKKETDMPGD IDKKYAGLLE KKWTSVIRLQ
KKVMDLEGRL AEAEKEYISG TPSREKRSPT EWIPRPPERS ALLGHRAPIT RVLFHPVYSV
VVSASEDASI KVWDYETGDF ERTIKGHTDS VQDIAFDHTG QFLASCSADM TIKLWDFKSY
ECLRTMHGHD HNVSSVCFLP SGDHVVSCSR DKSIKMWEVA TGYCVRTFTG HRDWVRMVRV
NSDGSLLASC SNDQTVRVWV VGTKECKLEL REHDHVVECV AWAPAHAQLC GAAGDSNRRP
GAGGAQGTGP FLVSGSRDKT IKVWDVSTGL ALFTLVGHDN WVRGVKFHPG GKYLLSASDD
KTLRVWELAH QRCCKTLDAH SHFCTSLDFH RTAPYVVTGS VDQTVKVWEC R
