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LIS1_CANDC
ID   LIS1_CANDC              Reviewed;         489 AA.
AC   B9WD30;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=CD36_80490;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(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; FM992690; CAX42579.1; -; Genomic_DNA.
DR   RefSeq; XP_002418997.1; XM_002418952.1.
DR   AlphaFoldDB; B9WD30; -.
DR   SMR; B9WD30; -.
DR   STRING; 42374.XP_002418997.1; -.
DR   EnsemblFungi; CAX42579; CAX42579; CD36_80490.
DR   GeneID; 8046779; -.
DR   KEGG; cdu:CD36_80490; -.
DR   CGD; CAL0000161252; Cd36_80490.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000002605; 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..489
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000405073"
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          328..368
FT                   /note="WD 5"
FT   REPEAT          389..428
FT                   /note="WD 6"
FT   REPEAT          437..486
FT                   /note="WD 7"
FT   COILED          66..98
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   489 AA;  55663 MW;  040DA233F741574F CRC64;
     MEKLSILTER QQTELNYAII QYLQPLCQQD NHALLDQLSK ILNIDQWTQE SNNVEKVDNY
     LEKRWSTVLR LQKKIIDLEN EISNLNNIIN SSNSDNNGIV LSKDKINWIP KGTAKQSYQC
     ENIVTTVKLH PNLPLVLNGC NDGNLYIWNI SNDDNTIPEK MIKAHTRAIN KICFTYKKPY
     YLATCSSDLT IKIWDEKFNH IRTLNGHEHT VSSIQFSPID NSILYSVSRD KNIRVWDIFQ
     GISLKSFVGH SEWCRDLDIV SSDNNGDFVL TCSNDQSARL SHASSGAGLA MIVGHGHVVE
     TVKFLPALQA NKILDEYITK NIEQFPTIPL ELLKDKTYNQ LGFKYCITAS RDNTIKLWLI
     PPPKIAPHRP PLPSKYNNSQ SWMIAELRGH SSWVKCLCVH PNGRFIISGS DDKTIKFWDL
     SSLLETGSVN VVKTIIGHDG FINDIDFARL KEASDSTPTS QEDLLKEVEK RMRCLFISGS
     ADNSIKLWN
 
 
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