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ZW10_CAEEL
ID   ZW10_CAEEL              Reviewed;         778 AA.
AC   Q19642;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Centromere/kinetochore protein zw10 homolog {ECO:0000305};
GN   Name=czw-1 {ECO:0000303|PubMed:9298984, ECO:0000312|WormBase:F20D12.4};
GN   ORFNames=F20D12.4 {ECO:0000312|WormBase:F20D12.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9298984; DOI=10.1083/jcb.138.6.1289;
RA   Starr D.A., Williams B.C., Li Z., Etemad-Moghadam B., Dawe R.K.,
RA   Goldberg M.L.;
RT   "Conservation of the centromere/kinetochore protein ZW10.";
RL   J. Cell Biol. 138:1289-1301(1997).
RN   [3] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN RZZ COMPLEX, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18765790; DOI=10.1101/gad.1687508;
RA   Gassmann R., Essex A., Hu J.-S., Maddox P.S., Motegi F., Sugimoto A.,
RA   O'Rourke S.M., Bowerman B., McLeod I., Yates J.R. III, Oegema K.,
RA   Cheeseman I.M., Desai A.;
RT   "A new mechanism controlling kinetochore-microtubule interactions revealed
RT   by comparison of two dynein-targeting components: SPDL-1 and the
RT   Rod/Zwilch/Zw10 complex.";
RL   Genes Dev. 22:2385-2399(2008).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18936247; DOI=10.1083/jcb.200805185;
RA   Yamamoto T.G., Watanabe S., Essex A., Kitagawa R.;
RT   "SPDL-1 functions as a kinetochore receptor for MDF-1 in Caenorhabditis
RT   elegans.";
RL   J. Cell Biol. 183:187-194(2008).
RN   [5] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19109417; DOI=10.1091/mbc.e08-10-1047;
RA   Essex A., Dammermann A., Lewellyn L., Oegema K., Desai A.;
RT   "Systematic analysis in Caenorhabditis elegans reveals that the spindle
RT   checkpoint is composed of two largely independent branches.";
RL   Mol. Biol. Cell 20:1252-1267(2009).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=24231804; DOI=10.1126/science.1246232;
RA   Cheerambathur D.K., Gassmann R., Cook B., Oegema K., Desai A.;
RT   "Crosstalk between microtubule attachment complexes ensures accurate
RT   chromosome segregation.";
RL   Science 342:1239-1242(2013).
CC   -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC       cells from prematurely exiting mitosis (PubMed:9298984). Required for
CC       the assembly of the dynein-dynactin and mdf-1-mdf-2 complexes onto
CC       kinetochores (PubMed:18936247). Its function related to the spindle
CC       assembly machinery and kinetochore-microtubule attachments likely
CC       depends on its association in the mitotic RZZ complex
CC       (PubMed:18936247). The RZZ complex recruits the spindly-like protein
CC       spdl-1 to kinetochores (PubMed:18765790, PubMed:18936247). To prevent
CC       irregular chromosome segregation, the complex also inhibits the
CC       attachment of the kinetochore-associated NDC80 complex to microtubules
CC       (PubMed:24231804). The recruitment of spdl-1 to kinetochores relieves
CC       this inhibition (PubMed:24231804). Required for embryonic development
CC       (PubMed:9298984). {ECO:0000269|PubMed:18765790,
CC       ECO:0000269|PubMed:18936247, ECO:0000269|PubMed:9298984,
CC       ECO:0000305|PubMed:24231804}.
CC   -!- SUBUNIT: Component of the RZZ complex composed of rod-1, czw-1 and zwl-
CC       1. {ECO:0000269|PubMed:18765790}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Note=Localizes to
CC       the kinetochore during nuclear envelope breakdown and remains there
CC       until the metaphase-anaphase transition. Localization of the RZZ
CC       complex to kinetochores is dependent upon knl-1.
CC       {ECO:0000269|PubMed:18765790}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown largely results in
CC       sterility (PubMed:9298984, PubMed:18765790, PubMed:19109417). RNAi-
CC       mediated knockdown also results in a high incidence of embryonic
CC       lethality in the embryos produced and defects in mitosis which include
CC       the formation of chromatin bridges in between sister chromatids during
CC       anaphase (PubMed:9298984). In addition, there is reduced localization
CC       of the spindly-like protein spdl-1 to kinetochores, but not to
CC       microtubules (PubMed:18936247). {ECO:0000269|PubMed:18765790,
CC       ECO:0000269|PubMed:18936247, ECO:0000269|PubMed:19109417,
CC       ECO:0000269|PubMed:9298984}.
CC   -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
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DR   EMBL; BX284604; CCD67719.1; -; Genomic_DNA.
DR   PIR; T16111; T16111.
DR   RefSeq; NP_501327.1; NM_068926.4.
DR   AlphaFoldDB; Q19642; -.
DR   SMR; Q19642; -.
DR   ComplexPortal; CPX-810; Rzz complex.
DR   STRING; 6239.F20D12.4.1; -.
DR   EPD; Q19642; -.
DR   PaxDb; Q19642; -.
DR   PeptideAtlas; Q19642; -.
DR   EnsemblMetazoa; F20D12.4.1; F20D12.4.1; WBGene00017643.
DR   EnsemblMetazoa; F20D12.4.2; F20D12.4.2; WBGene00017643.
DR   GeneID; 177587; -.
DR   KEGG; cel:CELE_F20D12.4; -.
DR   UCSC; F20D12.4.1; c. elegans.
DR   CTD; 177587; -.
DR   WormBase; F20D12.4; CE04434; WBGene00017643; czw-1.
DR   eggNOG; KOG2163; Eukaryota.
DR   GeneTree; ENSGT00390000016427; -.
DR   HOGENOM; CLU_012948_0_0_1; -.
DR   InParanoid; Q19642; -.
DR   OMA; MMNASLK; -.
DR   OrthoDB; 422807at2759; -.
DR   PhylomeDB; Q19642; -.
DR   Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q19642; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00017643; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:1990423; C:RZZ complex; IDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0034501; P:protein localization to kinetochore; IDA:ComplexPortal.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IC:ComplexPortal.
DR   Gene3D; 1.10.357.150; -; 1.
DR   InterPro; IPR009361; RZZ-complex_Zw10.
DR   InterPro; IPR046362; Zw10/DSL1_C_sf.
DR   Pfam; PF06248; Zw10; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis;
KW   Reference proteome.
FT   CHAIN           1..778
FT                   /note="Centromere/kinetochore protein zw10 homolog"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438725"
FT   COILED          47..99
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   778 AA;  87993 MW;  183629EA2708B34B CRC64;
     MASSEGSYRD LEKKLKNGLT SISQDIVDKY GNLKVSLNVN ATAKLIFDRL ENLEDIAEMS
     TRNLSNLIDQ TAKDSPEMLA EIKSQAQSCE NLVEFLQSMK NVEEQLIIMR SKTTNRVEWG
     TAILACKDFL NDTNMLLEGI GRDGFDMSVP LKHFAAEYSV LSYNCRYQLS ADYERAMNVP
     KLSKQKCGDR TNVSFSVFNV GSVEDQKMLN ETLSAMNMIG QLPERLDAWK IVILNVFCEA
     IVASRDGVDV YIVDNPTPDQ TRFLINQKPR GKKDKTIDVA KVLESMEVFF TKLHSVLHSH
     ELLDATGKTF TSMIGSVIEE QLITMILKDV IAIAAPVTET ADEDQEMFIN LLQIGEVFVE
     RMKELGFFSQ KAKLLFTLDT DTIFVTRRCF AIVSKANKLI NETYDKLVTV GVDDSAIKDI
     DLLAKAHTHA EHFAKEYGKD LGRLWSHNED SQFPSFFAFQ KCTVSESTIN FVNLLRDNVK
     AAFACEDEGA RAKLALTAEN IVRLYVILTP RKHAELFSSI PNMAAIFYNN CHYISHCIMT
     MSFEASGDNQ KTLLEPLLLD SVIRLRTVAA DCMEKTLTRC RREMTAYLED HSIFEHLPAS
     YKTTKNTFAA AEEMSESADI LVPREEPKII KCLAACLLHI RLIAKNLREP LTEVVYCKVI
     GSLVSFLLDS LVRHVVTTSD FRENDANVMA DVFKRLLEVV ANIVAYKEQT KVTDFCAREY
     FRLNEIVFVL GNRMQDIEHR WFNAKGPMAE HLSRSEVVGL IKALFADSQH RSDLIARL
 
 
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