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LIS1_CANAW
ID   LIS1_CANAW              Reviewed;         486 AA.
AC   C4YPI7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=CAWG_02388;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
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; CM000310; EEQ44126.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YPI7; -.
DR   SMR; C4YPI7; -.
DR   STRING; 5476.C4YPI7; -.
DR   EnsemblFungi; EEQ44126; EEQ44126; CAWG_02388.
DR   VEuPathDB; FungiDB:CAWG_02388; -.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   OMA; TQECKCV; -.
DR   Proteomes; UP000001429; Chromosome 3.
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:0000922; C:spindle pole; 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; 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; Repeat; Transport; WD repeat.
FT   CHAIN           1..486
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000405072"
FT   REPEAT          119..158
FT                   /note="WD 1"
FT   REPEAT          164..205
FT                   /note="WD 2"
FT   REPEAT          206..246
FT                   /note="WD 3"
FT   REPEAT          249..291
FT                   /note="WD 4"
FT   REPEAT          294..328
FT                   /note="WD 5"
FT   REPEAT          329..368
FT                   /note="WD 6"
FT   REPEAT          389..428
FT                   /note="WD 7"
FT   REPEAT          437..483
FT                   /note="WD 8"
FT   COILED          66..99
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   486 AA;  55358 MW;  166A0B449BF8A104 CRC64;
     MEKLQILTER QQTELNHAII QYLQPLCQQD NHVLLDQLSK LLNIDQSTQE SNNVEKVDNY
     LEKRWSTVLR LQKKIIDLEN EISNLNNIIN STNSDNNGII LSKDKINWIP KGAVKQSYQC
     ENIVTTVKLH PNLPLVLNGC NDGNLYIWNI SNDDNTIPEK MIKAHTRAIN KICFTYKKPY
     YLATCSSDLT IKIWDEKFNH IRTLNGHEHT VSSIQFSPVD NSILYSVSRD KNIRVWDIFQ
     GISLKSFVGH SEWCRDLDII SSDTYGDFVL TCSNDQSARL SHANSGAGVA MIVGHSHVVE
     TVKFLPSLQA NKILDEYITK NTEQFPTIPL ELLKDKTYNQ LGFKYCITAS RDNTIKLWLI
     PPPTIAPHRP PLPSKYNNSQ SWLIAELKGH SSWVKSLCVH PNGKFIISGS DDKTIKFWDL
     SGLLETGYVN VVKTIIGHDG FINDIDFARL KEASDVSEED LLKQVEKRMR CLFISGSADN
     SIKLWN
 
 
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