LIS1_BRAFL
ID LIS1_BRAFL Reviewed; 406 AA.
AC C3XVT5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN ORFNames=BRAFLDRAFT_59218;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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}.
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DR EMBL; GG666469; EEN67878.1; -; Genomic_DNA.
DR RefSeq; XP_002611869.1; XM_002611823.1.
DR AlphaFoldDB; C3XVT5; -.
DR SMR; C3XVT5; -.
DR STRING; 7739.XP_002611869.1; -.
DR PRIDE; C3XVT5; -.
DR eggNOG; KOG0295; Eukaryota.
DR InParanoid; C3XVT5; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000001554; Partially assembled 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; 4.
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..406
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000405038"
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..185
FT /note="WD 2"
FT REPEAT 188..227
FT /note="WD 3"
FT REPEAT 230..269
FT /note="WD 4"
FT REPEAT 272..329
FT /note="WD 5"
FT REPEAT 332..371
FT /note="WD 6"
FT REPEAT 374..406
FT /note="WD 7"
FT REGION 74..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..81
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 74..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 46263 MW; F1A5A59F0373ABDF CRC64;
MVLSQRQREE LNKAIADYLR SNGYESALEA FQKEAEMPGE IEKKYTGLLE KKWTSVIRLQ
KKVMDLEAKL AEAEKEFQSG GPNKKERSPS EWIPRPPARY SLSGHRSPIT RVLFHPVYSV
MVSASEDATI KIWDYETGDF ERTLKGHTDA VQDVSFDQQG KLLASCSADM TIKLWDFQTF
ENIKTMHGHD HNVSSVHFMP NGDFLISASR DKTIKMWELA TGYCVKTFTG HREWVRTVRV
NQDGSLLASC SNDQTVRVWV VANKECKAEL REHEHVVECI AWAPESCNGH VSEVMGAEKK
GRSGPFLLSG SRDKTIKMWD ISTGVCIMTL VGHDNWVRGV VWHPGGKYII SASDDKTIRV
WDYKNKRCQK TLEAHQHFCT SIDFHRSAPY VITGSVDQTV KVWECR
