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LIS12_CHAGB
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   25-MAY-2022, entry version 89.
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; 38033.XP_001226803.1; -.
DR   EnsemblFungi; EAQ84862; EAQ84862; CHGG_08876.
DR   GeneID; 4395636; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; Q2GT28; -.
DR   OMA; LTHWPSG; -.
DR   OrthoDB; 995692at2759; -.
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   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; 6.
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; 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
 
 
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