ZW10_DROME
ID ZW10_DROME Reviewed; 721 AA.
AC Q9W4X9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Centromere/kinetochore protein zw10;
DE AltName: Full=Mitotic 15 protein;
GN Name=Zw10; Synonyms=mit(1)15; ORFNames=CG9900;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Imaginal disk;
RX PubMed=1339459; DOI=10.1083/jcb.118.4.759;
RA Williams B.C., Karr T.L., Montgomery J.M., Goldberg M.L.;
RT "The Drosophila l(1)zw10 gene product, required for accurate mitotic
RT chromosome segregation, is redistributed at anaphase onset.";
RL J. Cell Biol. 118:759-773(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP IDENTIFICATION IN THE RZZ COMPLEX.
RX PubMed=12686595; DOI=10.1091/mbc.e02-09-0624;
RA Williams B.C., Li Z., Liu S., Williams E.V., Leung G., Yen T.J.,
RA Goldberg M.L.;
RT "Zwilch, a new component of the ZW10/ROD complex required for kinetochore
RT functions.";
RL Mol. Biol. Cell 14:1379-1391(2003).
RN [6]
RP FUNCTION.
RX PubMed=15886105; DOI=10.1016/j.cub.2005.03.052;
RA Buffin E., Lefebvre C., Huang J., Gagou M.E., Karess R.E.;
RT "Recruitment of Mad2 to the kinetochore requires the Rod/Zw10 complex.";
RL Curr. Biol. 15:856-861(2005).
RN [7]
RP FUNCTION.
RX PubMed=17576797; DOI=10.1083/jcb.200702062;
RA Griffis E.R., Stuurman N., Vale R.D.;
RT "Spindly, a novel protein essential for silencing the spindle assembly
RT checkpoint, recruits dynein to the kinetochore.";
RL J. Cell Biol. 177:1005-1015(2007).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP ZWILCH AND ROD.
RX PubMed=22685323; DOI=10.1242/jcs.099820;
RA Wainman A., Giansanti M.G., Goldberg M.L., Gatti M.;
RT "The Drosophila RZZ complex - roles in membrane trafficking and
RT cytokinesis.";
RL J. Cell Sci. 125:4014-4025(2012).
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis (PubMed:15886105,
CC PubMed:17576797). Required for the assembly of the dynein-dynactin,
CC Mad2 complexes and spindly/CG15415 onto kinetochores (PubMed:15886105,
CC PubMed:17576797). During cytokinesis in male meiotic cells it is
CC required for completion of cleavage furrow ingression, possibly in
CC conjunction with Rint1 (PubMed:22685323). Required for maintenance of
CC Golgi stack number and morphology, and acroblast assembly
CC (PubMed:22685323). Its function related to the spindle assembly
CC machinery is proposed to depend on its association in the RZZ complex
CC (PubMed:22685323). Failure to assemble the complex due to the absence
CC of any one of its components, results in the incorrect redistribution
CC of the remaining components to diverse membrane compartments
CC (PubMed:22685323). {ECO:0000269|PubMed:15886105,
CC ECO:0000269|PubMed:17576797, ECO:0000269|PubMed:22685323}.
CC -!- SUBUNIT: Component of the RZZ complex composed of rod, Zw10 and Zwilch.
CC {ECO:0000269|PubMed:12686595}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
CC kinetochore {ECO:0000269|PubMed:1339459, ECO:0000269|PubMed:22685323}.
CC Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:22685323}. Golgi apparatus
CC {ECO:0000269|PubMed:22685323}. Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:22685323}. Note=Dynamic pattern of localization
CC during the cell cycle (PubMed:22685323). Present in structures
CC resembling Golgi stacks prior to their migration into the nuclear zone
CC during prometaphase (PubMed:1339459, PubMed:22685323). At metaphase,
CC detected at the kinetochores and kinetochore microtubules
CC (PubMed:1339459, PubMed:22685323). During anaphase and telophase
CC accumulates at the spindle envelope midzone and broad areas at the cell
CC poles where they often become concentrated in small structures that
CC resemble small Golgi-derived vesicles (PubMed:22685323). In late
CC telophase they also form compact aggregates at the interior of the
CC equatorial region of the cell (PubMed:22685323).
CC {ECO:0000269|PubMed:1339459, ECO:0000269|PubMed:22685323}.
CC -!- DEVELOPMENTAL STAGE: Highest levels are found in embryo and adult.
CC Levels decrease during the first and second larval instar and then
CC decrease in third instar larvae and early pupae.
CC {ECO:0000269|PubMed:1339459}.
CC -!- DISRUPTION PHENOTYPE: In the spermatocytes the number of Golgi
CC structures are reduced and they appear smaller or have collapsed Golgi
CC stacks. In third instar larvae spermatocytes, cytokinesis is abnormal
CC producing multinucleated spermatids with a single large Nebenkern.
CC Acroblasts do not form and instead appear as an aggregate of multiple
CC unfused vesicles. During anaphase and early-telophase the central
CC spindle appears regular and acto-myosin contractile rings form normally
CC but during mid-telophase the rings fail to constrict. By late-telophase
CC the rings become fragmented, and the central spindle appears less
CC dense, is irregularly shaped and eventually disassembles. Spermatocytes
CC are unable to complete furrow ingression due to reduced plasma membrane
CC formation during cytokinesis. {ECO:0000269|PubMed:22685323}.
CC -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-44, Met-81 or Met-100 is
CC the initiator. {ECO:0000305}.
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DR EMBL; X64390; CAB76122.1; -; mRNA.
DR EMBL; AE014298; AAF45794.1; -; Genomic_DNA.
DR EMBL; AL138972; CAB72295.1; -; Genomic_DNA.
DR EMBL; AL121804; CAB72295.1; JOINED; Genomic_DNA.
DR EMBL; AL121804; CAB65854.1; -; Genomic_DNA.
DR PIR; A43275; A43275.
DR RefSeq; NP_524901.2; NM_080162.4.
DR AlphaFoldDB; Q9W4X9; -.
DR SMR; Q9W4X9; -.
DR BioGRID; 71022; 19.
DR IntAct; Q9W4X9; 1.
DR STRING; 7227.FBpp0070425; -.
DR PaxDb; Q9W4X9; -.
DR PRIDE; Q9W4X9; -.
DR EnsemblMetazoa; FBtr0070441; FBpp0070425; FBgn0004643.
DR GeneID; 47874; -.
DR KEGG; dme:Dmel_CG9900; -.
DR CTD; 9183; -.
DR FlyBase; FBgn0004643; Zw10.
DR VEuPathDB; VectorBase:FBgn0004643; -.
DR eggNOG; KOG2163; Eukaryota.
DR GeneTree; ENSGT00390000016427; -.
DR HOGENOM; CLU_012948_0_0_1; -.
DR InParanoid; Q9W4X9; -.
DR PhylomeDB; Q9W4X9; -.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 47874; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 47874; -.
DR PRO; PR:Q9W4X9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004643; Expressed in secondary oocyte and 35 other tissues.
DR ExpressionAtlas; Q9W4X9; baseline and differential.
DR Genevisible; Q9W4X9; DM.
DR GO; GO:0036063; C:acroblast; IDA:FlyBase.
DR GO; GO:0070939; C:Dsl1/NZR complex; ISS:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:FlyBase.
DR GO; GO:0005795; C:Golgi stack; IDA:FlyBase.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990423; C:RZZ complex; IDA:FlyBase.
DR GO; GO:0051233; C:spindle midzone; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0036090; P:cleavage furrow ingression; IMP:FlyBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR GO; GO:0048193; P:Golgi vesicle transport; ISS:FlyBase.
DR GO; GO:0007060; P:male meiosis chromosome segregation; IMP:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007107; P:membrane addition at site of cytokinesis; IMP:FlyBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:FlyBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:FlyBase.
DR Gene3D; 1.10.357.150; -; 1.
DR InterPro; IPR009361; RZZ-complex_Zw10.
DR InterPro; IPR046362; Zw10/DSL1_C_sf.
DR Pfam; PF06248; Zw10; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Kinetochore; Meiosis; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..721
FT /note="Centromere/kinetochore protein zw10"
FT /id="PRO_0000184960"
FT CONFLICT 58
FT /note="L -> M (in Ref. 1; CAB76122)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="D -> A (in Ref. 1; CAB76122)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="C -> A (in Ref. 4; CAB72295)"
FT /evidence="ECO:0000305"
FT CONFLICT 293..294
FT /note="HV -> QL (in Ref. 2; AAF45794)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="V -> A (in Ref. 1; CAB76122)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="D -> H (in Ref. 4; CAB72295/CAB65854)"
FT /evidence="ECO:0000305"
SQ 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
