LIS1_CRYNJ
ID LIS1_CRYNJ Reviewed; 433 AA.
AC P0CS42; Q55TS8; Q5KIK9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 58.
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};
GN OrderedLocusNames=CND02590;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW43166.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE017344; AAW43166.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_570473.1; XM_570473.1.
DR AlphaFoldDB; P0CS42; -.
DR SMR; P0CS42; -.
DR STRING; 5207.AAW43166; -.
DR PaxDb; P0CS42; -.
DR EnsemblFungi; AAW43166; AAW43166; CND02590.
DR GeneID; 3257176; -.
DR KEGG; cne:CND02590; -.
DR eggNOG; KOG0295; Eukaryota.
DR InParanoid; P0CS42; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000002149; Chromosome 4.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
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; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
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; 7.
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; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
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..433
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000240424"
FT DOMAIN 8..40
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 103..144
FT /note="WD 1"
FT REPEAT 146..184
FT /note="WD 2"
FT REPEAT 188..227
FT /note="WD 3"
FT REPEAT 230..269
FT /note="WD 4"
FT REPEAT 272..336
FT /note="WD 5"
FT REPEAT 339..378
FT /note="WD 6"
FT REPEAT 381..429
FT /note="WD 7"
FT COILED 57..84
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 433 AA; 47598 MW; 9DFA640D53FF641E CRC64;
MAALSDRQKD ELHRAMLAYL HAAGMHNAYA ALQHDAALAD VDPRDRAVGL LEKKWTSVIR
LQKKVIDLEN RNAALLAELA AAARPAAPGP FLPRPPPRHT LASHRAPVTR LAFHPTWTLL
ASASEDATVK LWDWEAGDME RTLKGHTKAV MDVDFDPRGG LMATCSSDLT LKLWDTANQY
TNVKTLHGHD HSVSSVRFMP DGETLVSASR DKTIRVWQVS SGYCIKTFSG HAEWVREAVP
SEDGRWLVSA SNDQTSRIWD FSTGETKMEL RGHEHVVECA VFAPVNAYPA IRELAGLKPP
APRDTRAKSP GVYAATGSRD KTIKLWDALS GQCLRTLVGH DNWIRALVFH PSGKYLLSAS
DDKTIKVWDL ANGRCTKTIE AHSHFVTSMT WGRAVGASGG IEKVNGDASS KEPRRINVLA
TGSVDQTIKV WTP
