ID A0A1J8R1X1_9AGAM Unreviewed; 722 AA.
AC A0A1J8R1X1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-OCT-2025, entry version 33.
DE RecName: Full=Nuclear distribution protein PAC1 {ECO:0000256|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog {ECO:0000256|HAMAP-Rule:MF_03141};
DE Short=LIS-1 {ECO:0000256|HAMAP-Rule:MF_03141};
DE AltName: Full=nudF homolog {ECO:0000256|HAMAP-Rule:MF_03141};
GN Name=PAC1 {ECO:0000256|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1 {ECO:0000256|HAMAP-Rule:MF_03141};
GN ORFNames=AZE42_05257 {ECO:0000313|EMBL:OJA15746.1};
OS Rhizopogon vesiculosus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=180088 {ECO:0000313|EMBL:OJA15746.1, ECO:0000313|Proteomes:UP000183567};
RN [1] {ECO:0000313|EMBL:OJA15746.1, ECO:0000313|Proteomes:UP000183567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-056 {ECO:0000313|EMBL:OJA15746.1,
RC ECO:0000313|Proteomes:UP000183567};
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03141}.
CC -!- SUBUNIT: Self-associates. Interacts with NDL1 and dynein.
CC {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000256|HAMAP-Rule:MF_03141}. Note=Localizes to the plus ends of
CC microtubules at the hyphal tip and the mitotic spindle poles.
CC {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000256|HAMAP-Rule:MF_03141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJA15746.1}.
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DR EMBL; LVVM01002902; OJA15746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J8R1X1; -.
DR STRING; 180088.A0A1J8R1X1; -.
DR OrthoDB; 10264588at2759; -.
DR Proteomes; UP000183567; 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:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007154; P:cell communication; IEA:UniProtKB-ARBA.
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 GO; GO:0023052; P:signaling; IEA:UniProtKB-ARBA.
DR CDD; cd00200; WD40; 1.
DR FunFam; 2.130.10.10:FF:000342; Nuclear distribution protein PAC1; 1.
DR FunFam; 1.20.960.30:FF:000002; Platelet-activating factor acetylhydrolase ib; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.5.460; Single helix bin; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03141; lis1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017252; Dynein_regulator_LIS1.
DR InterPro; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR056795; PAC1-like_LisH-like_dom.
DR InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom.
DR InterPro; IPR009215; TIM-br_IGPS-like.
DR InterPro; IPR051353; Tobamovirus_resist_UPF0261.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR020472; WD40_PAC1.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR31862; UPF0261 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G10120); 1.
DR PANTHER; PTHR31862:SF1; UPF0261 DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_1G10120); 1.
DR Pfam; PF24951; LisH_PAC1; 1.
DR Pfam; PF09370; PEP_hydrolase; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03141};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|HAMAP-
KW Rule:MF_03141};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776, ECO:0000256|HAMAP-Rule:MF_03141};
KW Reference proteome {ECO:0000313|Proteomes:UP000183567};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_03141};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 11..277
FT /note="TIM-barrel"
FT /evidence="ECO:0000259|Pfam:PF09370"
FT DOMAIN 298..332
FT /note="PAC1-like LisH-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF24951"
FT REPEAT 396..437
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 438..470
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 481..522
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 523..564
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 601..626
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 627..668
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 722 AA; 79238 MW; 41EEA5B27AC31779 CRC64;
MGEKTTSKRQ QVLRRLKESI SQGRAIVGGG AGVGLSAKTQ EAGGIDLIIL YNSGRYRMAG
RGSLAGLMPY GDANAIMLEM ARETLTIVKN TAVLAGICGT DPFRDMSQLL KEVKDLGFAG
VQNFPTVGLI DGVFRQNLEE TGMSYEKEVE MIKLAHEFDL LTTPYVFNVN EAERMTRAGA
DVIVAHMGLT TSGTIGAQTT LTLDDCVVRI KEILDAAVKI NPEIIVLCHG GPIATPSEAK
YVIERVNGIH GFFGASSLER LPVEVAMKEV TQEFKSIRLP ARLAAPRVVE IEMAHLSDRQ
REELHKSMLE YLHGSNFTAA YNALKQDTGV EYTPDPKAKY AGLLEKKWTS VIRLQKKIMD
LETRNASLQE ELSIAPSKRA AMQADWVPRA PAAHVLTGHR GHITRVAFHP QYSILASASE
DATVKIWDWE TGEFERTLKG HQRAVHDVDF DHKGHLLVTC SSDLFIKIWD SENEWKNTKT
LVGHEHSVSS VRFMPGDQFI VSASRDSTIR VFDVASTHLV RTISGHSEWV RCAVPSEDGH
LLASASKDKT AKLWDPRTGE CKGELRGHDN ELEAVCFAPV AAYAAIRELA GLPITGSKDP
GAYVATGSRD KNIKLWDVHS GQMIKNLAGH DNWVRALVFH PSGKLLLSAA DDKSIRVWEL
STGRCMKTIE AHSHFVATLA WGRQKISTAK SNGADAKTGE LEKLVNVVAS AGVDQTIKIW
LP
//
