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LIS1_PICGU
ID   LIS1_PICGU              Reviewed;         507 AA.
AC   A5DJX5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
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=PGUG_03576;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408158; EDK39478.2; -; Genomic_DNA.
DR   RefSeq; XP_001484195.1; XM_001484145.1.
DR   AlphaFoldDB; A5DJX5; -.
DR   SMR; A5DJX5; -.
DR   STRING; 4929.XP_001484195.1; -.
DR   EnsemblFungi; EDK39478; EDK39478; PGUG_03576.
DR   GeneID; 5125928; -.
DR   KEGG; pgu:PGUG_03576; -.
DR   VEuPathDB; FungiDB:PGUG_03576; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; A5DJX5; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000001997; 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: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; -; 3.
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; 6.
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; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
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..507
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000405093"
FT   REPEAT          125..164
FT                   /note="WD 1"
FT   REPEAT          170..222
FT                   /note="WD 2"
FT   REPEAT          225..265
FT                   /note="WD 3"
FT   REPEAT          268..312
FT                   /note="WD 4"
FT   REPEAT          315..389
FT                   /note="WD 5"
FT   REPEAT          410..449
FT                   /note="WD 6"
FT   REPEAT          474..507
FT                   /note="WD 7"
FT   COILED          72..98
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   507 AA;  56288 MW;  5737269C9B50B9A1 CRC64;
     MSILSPRQQQ ELNRAIVQYI GKIISDNSEN LEHGEKNGVL QHQDLVDKVA NLLDVPTSSE
     DLTTNYLEKK WSTVLRLQRK IMDLTDEVSN LKTIIEAKHA NGGSEISKDK INWLPTSVFK
     TFPTQTHQSV NTVAVHPYLP LIMAGCSDGT LSVWNIANDD PSIPEKSIRA HSRAVNRIRW
     SNSPVELSVK AGASNKSYIF ASCSSDLSIK IWDGNSNSQI RILTGHDHTV SSIAFSPSKP
     SILYSVSRDK TTKIWDSTNG YCTRTFIGHS DWVRDLDVIA AKQKSLGDFI LTCSNDQSVR
     LSHADSGTGL CLLVGHSHVI ESVRFLPMHS NAHIDKYLKE NSDRFPSMPP ELVSAPIYDD
     VLGYKYCVSA GRDNIVKLWL MPPAVVRPNA HPLPAATNNS QGWHIADLTG HQSWVKTLQV
     HPNGRFIFSA GDDKSIRVWD LSTLATGGRV TEVKKLMKHE GFVNDINAAP LSEPKDTTNE
     DILQDIESRM RCVFVSGGTD NTVRLWS
 
 
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