LIS1_CAEBR
ID LIS1_CAEBR Reviewed; 390 AA.
AC A8XZJ9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=lis-1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=CBG21225;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600921; CAP37998.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XZJ9; -.
DR SMR; A8XZJ9; -.
DR STRING; 6238.CBG21225; -.
DR WormBase; CBG21225; CBP40912; WBGene00040066; Cbr-lis-1.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; A8XZJ9; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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; 6.
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..390
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000405054"
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 189..228
FT /note="WD 3"
FT REPEAT 231..270
FT /note="WD 4"
FT REPEAT 272..313
FT /note="WD 5"
FT REPEAT 316..355
FT /note="WD 6"
FT REPEAT 358..390
FT /note="WD 7"
FT COILED 54..80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 390 AA; 44549 MW; 5B0B43CFCE7E81AB CRC64;
MSLSERQREE INRAVAEYLQ NNGYSEAFNM LLKEASLSEN DIKPLGGILE KKWTTVLRLQ
RKVNDLEAKL LESQQEINHG APTRDKRQAA DWIPRPPETQ KLIGHRLPVT RVIFHPLWTI
MASCSEDATI KVWDYETGQL EKTLKGHTDA VNDIAIDAAG KQLVSCSTDL TIKLWDFGQS
YDCLKSLKGH EHTVSSVTFL PTGDFVLSAS RDHTIKQWDI STGYCVFTFR GHNDWVRMIR
ISHDGTLFAS GSLDQTVSVW SLPRKQRNWY FEIMSMRWSV SKPEGNSTHI LFSGSRDRSI
KAWNISTGEV IFTLSAHENW VRGLAFHPKG KYLVSVADDK MMRIWELSAQ RCMKAIEAHE
HFVSTVAFHQ TNPYVITGSV DMSCKVWECR
