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LIS1_CANTT
ID   LIS1_CANTT              Reviewed;         490 AA.
AC   C5MJE8;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Nuclear distribution protein PAC1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE   AltName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE            Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE   AltName: Full=nudF homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Name=PAC1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Synonyms=LIS1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=CTRG_06191;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC       microtubule motor protein dynein. Plays a central role in positioning
CC       the mitotic spindle at the bud neck during cell division. Targets
CC       cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-
CC       mediated microtubule sliding along the bud cortex and consequently the
CC       movement of the mitotic spindle to the bud neck. {ECO:0000255|HAMAP-
CC       Rule:MF_03141}.
CC   -!- SUBUNIT: Self-associates. Interacts with NDL1 and dynein.
CC       {ECO:0000255|HAMAP-Rule:MF_03141}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus ends of
CC       microtubules and the mitotic spindle poles. {ECO:0000255|HAMAP-
CC       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; GG692406; EER30151.1; -; Genomic_DNA.
DR   RefSeq; XP_002546713.1; XM_002546667.1.
DR   AlphaFoldDB; C5MJE8; -.
DR   SMR; C5MJE8; -.
DR   STRING; 5482.XP_002546713.1; -.
DR   EnsemblFungi; EER30151; EER30151; CTRG_06191.
DR   GeneID; 8300052; -.
DR   KEGG; ctp:CTRG_06191; -.
DR   VEuPathDB; FungiDB:CTRG_06191; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IEA:EnsemblFungi.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0051010; F:microtubule plus-end binding; IEA:EnsemblFungi.
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   GO; GO:0030473; P:nuclear migration along microtubule; IEA:EnsemblFungi.
DR   GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IEA:EnsemblFungi.
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; 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; PF00400; WD40; 5.
DR   PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF109925; SSF109925; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
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..490
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000405075"
FT   REPEAT          118..157
FT                   /note="WD 1"
FT   REPEAT          163..204
FT                   /note="WD 2"
FT   REPEAT          205..245
FT                   /note="WD 3"
FT   REPEAT          251..290
FT                   /note="WD 4"
FT   REPEAT          293..327
FT                   /note="WD 5"
FT   REPEAT          328..367
FT                   /note="WD 6"
FT   REPEAT          388..427
FT                   /note="WD 7"
FT   REPEAT          436..487
FT                   /note="WD 8"
FT   COILED          65..96
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   490 AA;  55618 MW;  D5AA21D6B17108B7 CRC64;
     MMERSQILTE RQQSELNKAI IQYLQPICSQ ENNEVLDKLT SMLKIESTEL DGSDIVDNYL
     EKKWSTVLRL QKKIIDLENE IHNLTNIINT TNSETNGVVL SKDKINWIPK GASKQTYQCE
     NVVATVRLHP NLPLVFNGCN DGNLYIWNLT NDDNTIPEKR IKAHTRSINK MCFSYRKPYY
     LATCSSDLTI KIWDEKFNHI RTLNGHEHTV SSVKFSPSDS NILYSVSRDK NIRVWDISQG
     VCLKSFVGHS EWCRDLDAVA SETQGDFVLT CSNDQSARLS HINSGVGVAM FVGHTHVVES
     VKFLPKIQAN ELIDEYITKN IDQFPSIPSE LLKDPIYDEL GFKYCVSASR DNTIKLWLIP
     PPTLIPHRSP LPSKYNNSQG WLIAEFKGHS SWVKCLSVHP NGKFIISGSD DKTIKFWDLS
     GLIETGSVTA IKTISGHEGF INDIDFARLT DSESNTDKEL TSEEYLKDVE KRMRCLFISG
     SADNSIKLWS
 
 
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