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LIS1_CRYNB
ID   LIS1_CRYNB              Reviewed;         433 AA.
AC   P0CS43; 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=CNBD3750;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
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}.
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DR   EMBL; AAEY01000020; EAL21321.1; -; Genomic_DNA.
DR   RefSeq; XP_775968.1; XM_770875.1.
DR   AlphaFoldDB; P0CS43; -.
DR   SMR; P0CS43; -.
DR   EnsemblFungi; AAW43166; AAW43166; CND02590.
DR   EnsemblFungi; EAL21321; EAL21321; CNBD3750.
DR   GeneID; 4935764; -.
DR   KEGG; cnb:CNBD3750; -.
DR   VEuPathDB; FungiDB:CNBD3750; -.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
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   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; Repeat; Transport; WD repeat.
FT   CHAIN           1..433
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000410334"
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
 
 
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