LIS1_YEAST
ID LIS1_YEAST Reviewed; 494 AA.
AC P39946; D6W2W9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 192.
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}; OrderedLocusNames=YOR269W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9201714; DOI=10.1091/mbc.8.6.1035;
RA Geiser J.R., Schott E.J., Kingsbury T.J., Cole N.B., Totis L.J.,
RA Bhattacharyya G., He L., Hoyt M.A.;
RT "Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded
RT spindle motor act in functionally diverse mitotic pathways.";
RL Mol. Biol. Cell 8:1035-1050(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12566428; DOI=10.1083/jcb.200209022;
RA Lee W.-L., Oberle J.R., Cooper J.A.;
RT "The role of the lissencephaly protein Pac1 during nuclear migration in
RT budding yeast.";
RL J. Cell Biol. 160:355-364(2003).
RN [7]
RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH NDL1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15965467; DOI=10.1038/ncb1273;
RA Li J., Lee W.-L., Cooper J.A.;
RT "NudEL targets dynein to microtubule ends through LIS1.";
RL Nat. Cell Biol. 7:686-690(2005).
RN [8]
RP FUNCTION.
RX PubMed=19185494; DOI=10.1016/j.cub.2008.12.047;
RA Markus S.M., Punch J.J., Lee W.L.;
RT "Motor- and tail-dependent targeting of dynein to microtubule plus ends and
RT the cell cortex.";
RL Curr. Biol. 19:196-205(2009).
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. Following plus end
CC binding, dynein may be offloaded to the cortex by NUM1. Required for
CC viability in the absence of the kinesin-related microtubule-dependent
CC motor protein CIN8. {ECO:0000255|HAMAP-Rule:MF_03141,
CC ECO:0000269|PubMed:12566428, ECO:0000269|PubMed:15965467,
CC ECO:0000269|PubMed:19185494}.
CC -!- SUBUNIT: Self-associates. Interacts with NDL1. May form a complex with
CC dynein. {ECO:0000269|PubMed:15965467}.
CC -!- INTERACTION:
CC P39946; P38853: KEL1; NbExp=3; IntAct=EBI-12838, EBI-9619;
CC P39946; P47149: NNF1; NbExp=3; IntAct=EBI-12838, EBI-12098;
CC P39946; P39946: PAC1; NbExp=3; IntAct=EBI-12838, EBI-12838;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC spindle pole. Nucleus. Note=Localizes to the plus ends of cytoplasmic
CC microtubules.
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; U16827; AAB00685.1; -; Genomic_DNA.
DR EMBL; X89633; CAA61775.1; -; Genomic_DNA.
DR EMBL; Z75177; CAA99493.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11035.1; -; Genomic_DNA.
DR PIR; S67166; S67166.
DR RefSeq; NP_014912.1; NM_001183688.1.
DR PDB; 5VH9; EM; 7.70 A; B=140-493.
DR PDB; 5VLJ; EM; 10.50 A; B/C=140-493.
DR PDB; 7MGM; EM; 3.10 A; B/C=1-494.
DR PDBsum; 5VH9; -.
DR PDBsum; 5VLJ; -.
DR PDBsum; 7MGM; -.
DR AlphaFoldDB; P39946; -.
DR SMR; P39946; -.
DR BioGRID; 34658; 369.
DR DIP; DIP-1485N; -.
DR IntAct; P39946; 14.
DR MINT; P39946; -.
DR STRING; 4932.YOR269W; -.
DR MaxQB; P39946; -.
DR PaxDb; P39946; -.
DR PRIDE; P39946; -.
DR EnsemblFungi; YOR269W_mRNA; YOR269W; YOR269W.
DR GeneID; 854443; -.
DR KEGG; sce:YOR269W; -.
DR SGD; S000005795; PAC1.
DR VEuPathDB; FungiDB:YOR269W; -.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; P39946; -.
DR OMA; LTHWPSG; -.
DR BioCyc; YEAST:G3O-33759-MON; -.
DR PRO; PR:P39946; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P39946; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:SGD.
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:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:SGD.
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:0030473; P:nuclear migration along microtubule; IMP:SGD.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IDA:SGD.
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; 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; 4.
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; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..494
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000051113"
FT DOMAIN 14..46
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 153..192
FT /note="WD 1"
FT REPEAT 196..244
FT /note="WD 2"
FT REPEAT 251..292
FT /note="WD 3"
FT REPEAT 295..334
FT /note="WD 4"
FT REPEAT 347..395
FT /note="WD 5"
FT REPEAT 415..454
FT /note="WD 6"
FT REPEAT 457..492
FT /note="WD 7"
FT COILED 90..123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:7MGM"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:7MGM"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 309..317
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:7MGM"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:7MGM"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:7MGM"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 429..434
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:7MGM"
FT TURN 444..447
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 478..484
FT /evidence="ECO:0007829|PDB:7MGM"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:7MGM"
SQ SEQUENCE 494 AA; 56901 MW; E667E4BA7602FB3B CRC64;
MTNWQQQLPL TDTQKNELDK SVLRYLNWNY KQTVRHEHAQ DYESVRHAIV TLSGFLLQES
VDRQEFISNN DTSNESMVDI DELLLPKKWN SIVRLQKKII ELEQNTETLV SQIKDLNTQV
SELAQFKPTT SNGTSAHNVL KWIPRNLPSC LINVESSVTS VKLHPNLPIV FVATDHGKLY
AFDLFNYTIP LASLQSHTKA ITSMDVLFTN YTNSSKKNYL VIVTASKDLQ IHVFKWVSEE
CKFQQIRSLL GHEHIVSAVK IWQKNNDVHI ASCSRDQTVK IWDFHNGWSL KTFQPHSQWV
RSIDVLGDYI ISGSHDTTLR LTHWPSGNGL SVGTGHEFPI EKVKFIHFIE DSPEIRFRTP
STDRYKNWGM QYCVSASRDR TIKIWEIPLP TLMAHRAPIP NPTDSNFRCV LTLKGHLSWV
RDISIRGQYL FSCADDKSVR CWDLNTGQCL HVWEKLHTGF VNCLDLDVDF DSNVTPRQMM
VTGGLDCKSN VFMR
