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 27-MAR-2024, entry version 74.
DE RecName: Full=Nuclear distribution protein PAC1-2 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 2 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=nudF homolog 2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAC1-2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1-2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN ORFNames=POSPLDRAFT_89201;
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; 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., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
CC -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC microtubule motor protein dynein. May enhance dynein-mediated
CC microtubule sliding by targeting dynein to the microtubule plus end.
CC Required for nuclear migration during vegetative growth as well as
CC development. Required for retrograde early endosome (EE) transport from
CC the hyphal tip. Required for localization of dynein to the mitotic
CC spindle poles. Recruits additional proteins to the dynein complex at
CC SPBs. {ECO:0000255|HAMAP-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 at the hyphal tip and the mitotic spindle poles.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-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; EQ966319; EED81189.1; -; Genomic_DNA.
DR RefSeq; XP_002473604.1; XM_002473559.1.
DR STRING; 561896.B8PD53; -.
DR KEGG; ppl:POSPLDRAFT_89201; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; B8PD53; -.
DR OMA; CIRWAPP; -.
DR OrthoDB; 1798470at2759; -.
DR Proteomes; UP000001743; 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 CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19879:SF1; CANNONBALL-RELATED; 1.
DR PANTHER; PTHR19879; TRANSCRIPTION INITIATION FACTOR TFIID; 1.
DR Pfam; PF00400; WD40; 6.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 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; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..427
FT /note="Nuclear distribution protein PAC1-2"
FT /id="PRO_0000405099"
FT DOMAIN 8..40
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 106..147
FT /note="WD 1"
FT REPEAT 149..187
FT /note="WD 2"
FT REPEAT 194..233
FT /note="WD 3"
FT REPEAT 236..275
FT /note="WD 4"
FT REPEAT 278..336
FT /note="WD 5"
FT REPEAT 339..378
FT /note="WD 6"
FT REPEAT 381..420
FT /note="WD 7"
FT COILED 58..82
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
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
//
