LIS1_DICDI
ID LIS1_DICDI Reviewed; 419 AA.
AC Q8I0F4; Q54J15;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=DdLIS1;
GN Name=lis1; ORFNames=DDB_G0288375;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ASP-325.
RX PubMed=15800059; DOI=10.1091/mbc.e05-01-0069;
RA Rehberg M., Kleylein-Sohn J., Faix J., Ho T.-H., Schulz I., Graef R.;
RT "Dictyostelium LIS1 is a centrosomal protein required for microtubule/cell
RT cortex interactions, nucleus/centrosome linkage, and actin dynamics.";
RL Mol. Biol. Cell 16:2759-2771(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 such
CC as the maintenance of Golgi integrity, the coupling of the nucleus and
CC centrosome and dynein/dynactin-mediated interactions of microtubule
CC tips with the cell cortex. {ECO:0000255|HAMAP-Rule:MF_03141,
CC ECO:0000269|PubMed:15800059}.
CC -!- SUBUNIT: Interacts with dynein and mtaA/CP224 in the cortical
CC attachment of microtubules. Interacts with rac1A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC Rule:MF_03141, ECO:0000269|PubMed:15800059}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000255|HAMAP-
CC Rule:MF_03141, ECO:0000269|PubMed:15800059}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:15800059}.
CC Note=Localizes to microtubules and to the centrosome throughout the
CC entire cell cycle. Is part of the centrosomal corona.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ512336; CAD54457.1; -; mRNA.
DR EMBL; AJ512794; CAD55133.1; -; mRNA.
DR EMBL; AAFI02000111; EAL63213.1; -; Genomic_DNA.
DR RefSeq; XP_636715.1; XM_631623.1.
DR AlphaFoldDB; Q8I0F4; -.
DR SMR; Q8I0F4; -.
DR STRING; 44689.DDB0219930; -.
DR TCDB; 1.I.1.1.5; the nuclear pore complex (npc) family.
DR PaxDb; Q8I0F4; -.
DR EnsemblProtists; EAL63213; EAL63213; DDB_G0288375.
DR GeneID; 8626591; -.
DR KEGG; ddi:DDB_G0288375; -.
DR dictyBase; DDB_G0288375; lis1.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q8I0F4; -.
DR OMA; TQECKCV; -.
DR PhylomeDB; Q8I0F4; -.
DR PRO; PR:Q8I0F4; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0031592; C:centrosomal corona; IDA:dictyBase.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
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:0015630; C:microtubule cytoskeleton; IDA:dictyBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045504; F:dynein heavy chain binding; IPI:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IGI:dictyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051642; P:centrosome localization; IMP:dictyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
DR GO; GO:0051645; P:Golgi localization; IMP:dictyBase.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:dictyBase.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Microtubule; Mitosis; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..419
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000327783"
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 147..187
FT /note="WD 2"
FT REPEAT 188..227
FT /note="WD 3"
FT REPEAT 230..271
FT /note="WD 4"
FT REPEAT 272..341
FT /note="WD 5"
FT REPEAT 344..385
FT /note="WD 6"
FT REPEAT 387..419
FT /note="WD 7"
FT REGION 74..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..79
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 84..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 325
FT /note="D->H: Disruption of the microtubule skeleton during
FT interphase, dispersal of the Golgi apparatus, and reduction
FT of cellular F-actin content."
FT /evidence="ECO:0000269|PubMed:15800059"
SQ SEQUENCE 419 AA; 46576 MW; 88ECEAF3BEC3E8A6 CRC64;
MVLTSKQKEE LNGSILDYFE SSQYKSSFEE FKKETGTELD VKKKGLLEKK WTSVIRLQKK
VLDLEAKVAQ LEEELNSGGG RGGGRGRGKE DALPRPPEKH ILTGHRNCIN SVKFHPSFSL
MVSASEDATI KVWDFESGEF ERTLKGHTNA VQDIDFDKTG NLLASCSADL TIKLWDFQTY
DCVKTLHGHD HNVSCVRFTP SGDQLISSSR DKTIKVWEAA TGYCIKTLVG HEDWVRKITV
SEDGSCIASC SNDQTIKTWN IVKGECLATY REHSHVVECL AFSTANIIDI PGSLLSTPEG
KSKVKQGPGG NLVGQCGYLA TGSRDKTIKI WELATGRCLA TYIGHDNWVR AVRFHPCGKF
LLSVGDDKTI RVWDIAQGRC IKTINEAHTH FISCLDFCLH NPHIATGGVD DVIKVWKLQ
