LIS1_GLOMM
ID LIS1_GLOMM Reviewed; 411 AA.
AC D3TLL6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=20353571; DOI=10.1186/1471-2164-11-213;
RA Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z.,
RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RT "An insight into the sialome of Glossina morsitans morsitans.";
RL BMC Genomics 11:213-213(2010).
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; EZ422318; ADD18594.1; -; mRNA.
DR AlphaFoldDB; D3TLL6; -.
DR SMR; D3TLL6; -.
DR STRING; 37546.D3TLL6; -.
DR PRIDE; D3TLL6; -.
DR VEuPathDB; VectorBase:GMOY000875; -.
DR PhylomeDB; D3TLL6; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
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; 6.
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 Microtubule; Mitosis; Repeat; Transport; WD repeat.
FT CHAIN 1..411
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000405051"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 106..147
FT /note="WD 1"
FT REPEAT 149..187
FT /note="WD 2"
FT REPEAT 191..230
FT /note="WD 3"
FT REPEAT 233..272
FT /note="WD 4"
FT REPEAT 275..334
FT /note="WD 5"
FT REPEAT 337..376
FT /note="WD 6"
FT REPEAT 379..411
FT /note="WD 7"
FT COILED 56..83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 411 AA; 46497 MW; D3EC3E46FB8B0019 CRC64;
MKMVLSQRQR EELNQAIADY LGSNGYSSAL EAFRKEADIS GEAERKIVGL LEKKWTSVIR
LQKKVMELEA KLSEAEKEVI EGAPSRAKRS PGEWIPRPPE KFSLSGHRAS ITRVIFHPTY
SLMLSASEDA VIKIWDFETG EYERSLKGHT SSVQDIAFDS QGKLLASCSA DLSIKLWDFQ
QSYDCVKTML GHDHNVSSVA FVPAGDYVLS ASRDQTIKMW EVATGYCVKT YSGHREWIRM
VRVHMDGNIF ASCSIDHSIR IWSINSRDCK AELRAHDHTV ECIAWAPDIS TTHINEAAGS
DNKKGHHQGP FLASGSRDKT IRVWDVGVGL CLFVLTGHDN WVRELTFHPG GKYLVSASDD
KTIRVWDLRN KRFMKTLYAH QHFCTSVDFH KKLPYVISGS VDNTVKVWEC R