ID LIS12_CHAGB Reviewed; 453 AA.
AC Q2GT28;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
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}; ORFNames=CHGG_08876;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408034; EAQ84862.1; -; Genomic_DNA.
DR RefSeq; XP_001226803.1; XM_001226802.1.
DR AlphaFoldDB; Q2GT28; -.
DR SMR; Q2GT28; -.
DR STRING; 306901.Q2GT28; -.
DR GeneID; 4395636; -.
DR VEuPathDB; FungiDB:CHGG_08876; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q2GT28; -.
DR OMA; RGTCLMT; -.
DR OrthoDB; 1798470at2759; -.
DR Proteomes; UP000001056; 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; PTHR44129:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA; 1.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF00400; WD40; 6.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
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; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
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..453
FT /note="Nuclear distribution protein PAC1-2"
FT /id="PRO_0000405077"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 113..154
FT /note="WD 1"
FT REPEAT 156..196
FT /note="WD 2"
FT REPEAT 200..243
FT /note="WD 3"
FT REPEAT 246..285
FT /note="WD 4"
FT REPEAT 290..350
FT /note="WD 5"
FT REPEAT 352..391
FT /note="WD 6"
FT REPEAT 396..448
FT /note="WD 7"
FT REGION 84..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..87
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 453 AA; 49435 MW; 902CE67C01DEEAF8 CRC64;
MNPVLTSRQA DELHKSIVAY LTANNLSTTA ATLREELSLG EDVFDAEKTA KYQSLLEKKW
TSVVRLQKKV MDLESRSVAL QSELEHSTPA SLSKRKDPTS WLPRSPPRHS LESHQAIVNC
LAFHPVFSSL ASGSDDSTVK IWDWELGELE RTLKGHTRAV LDIDFGGPRG AILLASCSSD
STIKLWDPAD EYKNTRTLTG HDHSVSAVRF VTSRPRSENL LVSASGDKTL KVWDITAGYC
IKTLQGHTGW VRDVVPSLDG RFLLSSGTDQ TARLWDISAA DPESKLVMVG HENGIRCCAF
APPASYVHMA ALAGLKKPPP STSTAEFMAT GSRDKTIKLW NSTGTCIKTL VGHDNWVSGL
VFHPGGKYLL SVADDKTLRC WDLGDDGRCV KVLADAHGQF ITCLRWAPGI VKKGADQGAE
DTGPLEKTAP SEVQIRCLVA TTSVDKVVRI FAD
//
