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Database: UniProt
Entry: B8PD53
LinkDB: B8PD53
Original site: B8PD53 
ID   LIS12_POSPM             Reviewed;         427 AA.
AC   B8PD53;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-SEP-2014, entry version 35.
DE   RecName: Full=Nuclear distribution protein PAC1-2;
DE   AltName: Full=Lissencephaly-1 homolog 2;
DE            Short=LIS-1 2;
DE   AltName: Full=nudF homolog 2;
GN   Name=PAC1-2; Synonyms=LIS1-2; ORFNames=POSPLDRAFT_89201;
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Postia.
OX   NCBI_TaxID=561896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T.,
RA   Kersten P., Hammel K.E., Vanden Wymelenberg A., Gaskell J.,
RA   Lindquist E., Sabat G., Splinter BonDurant S., Larrondo L.F.,
RA   Canessa P., Vicuna R., Yadav J., Doddapaneni H., Subramanian V.,
RA   Pisabarro A.G., Lavin J.L., Oguiza J.A., Master E., Henrissat B.,
RA   Coutinho P.M., Harris P., Magnuson J.K., Baker S.E., Bruno K.,
RA   Kenealy W., Hoegger P.J., Kuees U., Ramaiya P., Lucas S., Salamov A.,
RA   Shapiro H., Tu H., Chee C.L., Misra M., Xie G., Teter S., Yaver D.,
RA   James T., Mokrejs M., Pospisek M., Grigoriev I.V., Brettin T.,
RA   Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus
RT   Postia placenta supports unique mechanisms of lignocellulose
RT   conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC   -!- FUNCTION: Positively regulates the activity of the minus-end
CC       directed microtubule motor protein dynein. May enhance dynein-
CC       mediated microtubule sliding by targeting dynein to the
CC       microtubule plus end. Required for nuclear migration during
CC       vegetative growth as well as development. Required for retrograde
CC       early endosome (EE) transport from the hyphal tip. Required for
CC       localization of dynein to the mitotic spindle poles. Recruits
CC       additional proteins to the dynein complex at SPBs (By similarity).
CC   -!- SUBUNIT: Self-associates (By similarity). Interacts with NDL1 and
CC       dynein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cytoplasm, cytoskeleton, spindle pole (By similarity).
CC       Note=Localizes to the plus ends of microtubules at the hyphal tip
CC       and the mitotic spindle poles (By similarity).
CC   -!- DOMAIN: Dimerization mediated by the LisH domain may be required
CC       to activate dynein (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC   -!- SIMILARITY: Contains 1 LisH domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; EQ966319; EED81189.1; -; Genomic_DNA.
DR   RefSeq; XP_002473604.1; XM_002473559.1.
DR   ProteinModelPortal; B8PD53; -.
DR   STRING; 104341.JGI89201; -.
DR   GeneID; 8140021; -.
DR   KEGG; ppl:POSPLDRAFT_89201; -.
DR   eggNOG; COG2319; -.
DR   OMA; VANPETK; -.
DR   OrthoDB; EOG715QD8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0006928; P:cellular component movement; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
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; IPR006594; LisH_dimerisation.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
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; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Microtubule; Mitosis; Repeat; Transport; WD repeat.
FT   CHAIN         1    427       Nuclear distribution protein PAC1-2.
FT                                /FTId=PRO_0000405099.
FT   DOMAIN        8     40       LisH.
FT   REPEAT      106    147       WD 1.
FT   REPEAT      149    187       WD 2.
FT   REPEAT      194    233       WD 3.
FT   REPEAT      236    275       WD 4.
FT   REPEAT      278    336       WD 5.
FT   REPEAT      339    378       WD 6.
FT   REPEAT      381    420       WD 7.
FT   COILED       58     82       Potential.
SQ   SEQUENCE   427 AA;  47542 MW;  D7AFF35284418C2E CRC64;
     MSILSERQKD DLNKSIAEYL YAQDLTEIAD SLCARLSLDY KSEPNSKYAG LLEKKWVSVI
     RLQKKLIESE NRYTALQEDI AAGPARRRDA QVDWLPTAPA RYTLTSHRAP ITRVAFHPTF
     SLLASASEDT TVKIWDWETG SFERTLKGHT REVWGVDFDS KGSFLATCSS DLSIKVWDTQ
     QWDNAGYSGK TLRGHEHTVS TVKFLPGDDL IASASRDKTI RIWEVATTFC IRTITGHEDW
     VRMTVPSTDG TLLGSCSSDN TARVWDPTSG VMKMEFRGHG HIVEVIAFAP LASYAAIREL
     AGLKAATKAP GAYIATGSRD KTVKIWDVHS GQELRTVSGH NDWIRGLVFH PSGKHLLSAS
     DDKTIRVWEL STGRCMXVVE AHSHFITCLA WGPPVSAVAR VELPRTPFCG DPKPIASRIM
     EEFNPRP
//
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