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Centromere/kinetochore protein zw10 (Mitotic 15 protein)

 ZW10_DROME              Reviewed;         721 AA.
Q9W4X9;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
05-JUL-2017, entry version 116.
RecName: Full=Centromere/kinetochore protein zw10;
AltName: Full=Mitotic 15 protein;
Name=Zw10; Synonyms=mit(1)15; ORFNames=CG9900;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
TISSUE=Imaginal disk;
PubMed=1339459; DOI=10.1083/jcb.118.4.759;
Williams B.C., Karr T.L., Montgomery J.M., Goldberg M.L.;
"The Drosophila l(1)zw10 gene product, required for accurate mitotic
chromosome segregation, is redistributed at anaphase onset.";
J. Cell Biol. 118:759-773(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[5]
IDENTIFICATION IN THE RZZ COMPLEX.
PubMed=12686595; DOI=10.1091/mbc.E02-09-0624;
Williams B.C., Li Z., Liu S., Williams E.V., Leung G., Yen T.J.,
Goldberg M.L.;
"Zwilch, a new component of the ZW10/ROD complex required for
kinetochore functions.";
Mol. Biol. Cell 14:1379-1391(2003).
[6]
FUNCTION.
PubMed=15886105; DOI=10.1016/j.cub.2005.03.052;
Buffin E., Lefebvre C., Huang J., Gagou M.E., Karess R.E.;
"Recruitment of Mad2 to the kinetochore requires the Rod/Zw10
complex.";
Curr. Biol. 15:856-861(2005).
[7]
FUNCTION.
PubMed=17576797; DOI=10.1083/jcb.200702062;
Griffis E.R., Stuurman N., Vale R.D.;
"Spindly, a novel protein essential for silencing the spindle assembly
checkpoint, recruits dynein to the kinetochore.";
J. Cell Biol. 177:1005-1015(2007).
[8]
FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION
WITH ZWILCH AND ROD.
PubMed=22685323; DOI=10.1242/jcs.099820;
Wainman A., Giansanti M.G., Goldberg M.L., Gatti M.;
"The Drosophila RZZ complex - roles in membrane trafficking and
cytokinesis.";
J. Cell Sci. 125:4014-4025(2012).
-!- FUNCTION: Essential component of the mitotic checkpoint, which
prevents cells from prematurely exiting mitosis (PubMed:15886105,
PubMed:17576797). Required for the assembly of the dynein-
dynactin, Mad2 complexes and spindly/CG15415 onto kinetochores
(PubMed:15886105, PubMed:17576797). During cytokinesis in male
meiotic cells it is required for completion of cleavage furrow
ingression, possibly in conjunction with Rint1 (PubMed:22685323).
Required for maintenance of Golgi stack number and morphology, and
acroblast assembly (PubMed:22685323). Its function related to the
spindle assembly machinery is proposed to depend on its
association in the RZZ complex (PubMed:22685323). Failure to
assemble the complex due to the absence of any one of its
components, results in the incorrect redistribution of the
remaining components to diverse membrane compartments
(PubMed:22685323). {ECO:0000269|PubMed:15886105,
ECO:0000269|PubMed:17576797, ECO:0000269|PubMed:22685323}.
-!- SUBUNIT: Component of the RZZ complex composed of rod, Zw10 and
Zwilch. {ECO:0000269|PubMed:12686595}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
kinetochore {ECO:0000269|PubMed:1339459,
ECO:0000269|PubMed:22685323}. Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:22685323}. Golgi
apparatus {ECO:0000269|PubMed:22685323}. Golgi apparatus, Golgi
stack {ECO:0000269|PubMed:22685323}. Note=Dynamic pattern of
localization during the cell cycle (PubMed:22685323). Present in
structures resembling Golgi stacks prior to their migration into
the nuclear zone during prometaphase (PubMed:1339459,
PubMed:22685323). At metaphase, detected at the kinetochores and
kinetochore microtubules (PubMed:1339459, PubMed:22685323). During
anaphase and telophase accumulates at the spindle envelope midzone
and broad areas at the cell poles where they often become
concentrated in small structures that resemble small Golgi-derived
vesicles (PubMed:22685323). In late telophase they also form
compact aggregates at the interior of the equatorial region of the
cell (PubMed:22685323). {ECO:0000269|PubMed:1339459,
ECO:0000269|PubMed:22685323}.
-!- DEVELOPMENTAL STAGE: Highest levels are found in embryo and adult.
Levels decrease during the first and second larval instar and then
decrease in third instar larvae and early pupae.
{ECO:0000269|PubMed:1339459}.
-!- DISRUPTION PHENOTYPE: In the spermatocytes the number of Golgi
structures are reduced and they appear smaller or have collapsed
Golgi stacks. In third instar larvae spermatocytes, cytokinesis is
abnormal producing multinucleated spermatids with a single large
Nebenkern. Acroblasts do not form and instead appear as an
aggregate of multiple unfused vesicles. During anaphase and early-
telophase the central spindle appears regular and acto-myosin
contractile rings form normally but during mid-telophase the rings
fail to constrict. By late-telophase the rings become fragmented,
and the central spindle appears less dense, is irregularly shaped
and eventually disassembles. Spermatocytes are unable to complete
furrow ingression due to reduced plasma membrane formation during
cytokinesis. {ECO:0000269|PubMed:22685323}.
-!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1, Met-44, Met-81 or Met-100
is the initiator. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X64390; CAB76122.1; -; mRNA.
EMBL; AE014298; AAF45794.1; -; Genomic_DNA.
EMBL; AL138972; CAB72295.1; -; Genomic_DNA.
EMBL; AL121804; CAB72295.1; JOINED; Genomic_DNA.
EMBL; AL121804; CAB65854.1; -; Genomic_DNA.
PIR; A43275; A43275.
RefSeq; NP_524901.2; NM_080162.4.
UniGene; Dm.1760; -.
ProteinModelPortal; Q9W4X9; -.
SMR; Q9W4X9; -.
BioGrid; 71022; 8.
IntAct; Q9W4X9; 1.
MINT; MINT-1575513; -.
STRING; 7227.FBpp0070425; -.
PaxDb; Q9W4X9; -.
PRIDE; Q9W4X9; -.
GeneID; 47874; -.
KEGG; dme:Dmel_CG9900; -.
CTD; 9183; -.
FlyBase; FBgn0004643; Zw10.
eggNOG; KOG2163; Eukaryota.
eggNOG; ENOG410XQ7J; LUCA.
InParanoid; Q9W4X9; -.
KO; K11578; -.
OrthoDB; EOG091G026L; -.
PhylomeDB; Q9W4X9; -.
Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
GenomeRNAi; 47874; -.
PRO; PR:Q9W4X9; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004643; -.
Genevisible; Q9W4X9; DM.
GO; GO:0036063; C:acroblast; IDA:FlyBase.
GO; GO:0000940; C:condensed chromosome outer kinetochore; NAS:FlyBase.
GO; GO:0070939; C:Dsl1/NZR complex; ISS:FlyBase.
GO; GO:0005783; C:endoplasmic reticulum; ISS:FlyBase.
GO; GO:0005795; C:Golgi stack; IDA:FlyBase.
GO; GO:0000776; C:kinetochore; IDA:FlyBase.
GO; GO:0005828; C:kinetochore microtubule; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:1990423; C:RZZ complex; IDA:FlyBase.
GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
GO; GO:0017137; F:Rab GTPase binding; IPI:FlyBase.
GO; GO:0036090; P:cleavage furrow ingression; IMP:FlyBase.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
GO; GO:0048193; P:Golgi vesicle transport; ISS:FlyBase.
GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
GO; GO:0007107; P:membrane addition at site of cytokinesis; IMP:FlyBase.
GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:FlyBase.
InterPro; IPR009361; RZZ-complex_Zw10.
Pfam; PF06248; Zw10; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Centromere; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; Golgi apparatus; Kinetochore; Meiosis;
Mitosis; Nucleus; Reference proteome.
CHAIN 1 721 Centromere/kinetochore protein zw10.
/FTId=PRO_0000184960.
CONFLICT 58 58 L -> M (in Ref. 1; CAB76122).
{ECO:0000305}.
CONFLICT 203 203 D -> A (in Ref. 1; CAB76122).
{ECO:0000305}.
CONFLICT 248 248 C -> A (in Ref. 4; CAB72295).
{ECO:0000305}.
CONFLICT 293 294 HV -> QL (in Ref. 2; AAF45794).
{ECO:0000305}.
CONFLICT 366 366 V -> A (in Ref. 1; CAB76122).
{ECO:0000305}.
CONFLICT 626 626 D -> H (in Ref. 4; CAB72295/CAB65854).
{ECO:0000305}.
SEQUENCE 721 AA; 82263 MW; 1341BC2BF752188D CRC64;
MEEEAPRFNV LEEAFNGNGN GCANVEATQS AILKVLTRVN RFQMRVRKHI EDNYTEFLPN
NTSPDIFLEE SGSLNREIHD MLENLGSEGL DALDEANVKM AGNGRQLREI LLGLGVSEHV
LRIDELFQCV EEAKATKDYL VLLDLVGRLR AFIYGDDSVD GDAQVATPEV RRIFKALECY
ETIKVKYHVQ AYMLQQSLQE RFDRLVQLQC KSFPTSRCVT LQVSRDQTQL QDIVQALFQE
PYNPARLCEF LLDNCIEPVI MRPVMADYSE EADGGTYVRL SLSYATKEPS SAHVRPNYKQ
VLENLRLLLH TLAGINCSVS RDQHVFGIIG DHVKDKMLKL LVDECLIPAV PESTEEYQTS
TLCEDVAQLE QLLVDSFIIN PEQDRALGQF VEKYETYYRN RMYRRVLETA REIIQRDLQD
MVLVAPNNHS AEVANDPFLF PRCMISKSAQ DFVKLMDRIL RQPTDKLGDQ EADPIAGVIS
IMLHTYINEV PKVHRKLLES IPQQAVLFHN NCMFFTHWVA QHANKGIESL AALAKTLQAT
GQQHFRVQVD YQSSILMGIM QEFEFESTHT LGSGPLKLVR QCLRQLELLK NVWANVLPET
VYNATFCELI NTFVAELIRR VFTLRDISAQ MACELSDLID VVLQRAPTLF REPNEVVQVL
SWLKLQQLKA MLNASLMEIT ELWGDGVGPL TASYKSDEIK HLIRALFQDT DWRAKAITQI
V


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