ID   ZW10_MOUSE              Reviewed;         779 AA.
AC   O54692; Q3TIA5; Q3ULW1; Q921H3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Centromere/kinetochore protein zw10 homolog;
GN   Name=Zw10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Kidney, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 522-779.
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC       cells from prematurely exiting mitosis. Required for the assembly of
CC       the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its
CC       function related to the spindle assembly machinery is proposed to
CC       depend on its association in the mitotic RZZ complex. Involved in
CC       regulation of membrane traffic between the Golgi and the endoplasmic
CC       reticulum (ER); the function is proposed to depend on its association
CC       in the interphase NRZ complex which is believed to play a role in SNARE
CC       assembly at the ER (By similarity). {ECO:0000250|UniProtKB:O43264}.
CC   -!- SUBUNIT: Interacts with NBAS and KNTC1/ROD; the interactions are
CC       mutually exclusive and indicative for its association in two different
CC       vesicle tethering complexes (By similarity). Component of the RZZ
CC       complex composed of KNTC1/ROD, ZW10 and ZWILCH (By similarity).
CC       Component of the NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L;
CC       NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the
CC       assembly has been described as syntaxin 18 complex) (By similarity).
CC       Interacts directly with RINT1/TIP20L bound to BNIP1/SEC20L (By
CC       similarity). Interacts with C19orf25 and ZWINT (By similarity).
CC       Interacts with ZFYVE1 (By similarity). Interacts with RAB18 and this
CC       interaction is enhanced in the presence of ZFYVE1 (By similarity).
CC       {ECO:0000250|UniProtKB:O43264}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43264}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43264};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:O43264}. Chromosome,
CC       centromere, kinetochore {ECO:0000250|UniProtKB:O43264}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000250|UniProtKB:O43264}. Lipid droplet
CC       {ECO:0000250|UniProtKB:O43264}. Note=Dynamic pattern of localization
CC       during the cell cycle. In most cells at interphase, present diffusely
CC       in the cytoplasm. In prometaphase, associated with the kinetochore. At
CC       metaphase, detected both at the kinetochores and, most prominently, at
CC       the spindle, particularly at the spindle poles. In very early anaphase,
CC       detected on segregating kinetochores. In late anaphase and telophase,
CC       accumulates at the spindle midzone. {ECO:0000250|UniProtKB:O43264}.
CC   -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
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DR   EMBL; AK145270; BAE26337.1; -; mRNA.
DR   EMBL; AK167251; BAE39372.1; -; mRNA.
DR   EMBL; AK167937; BAE39941.1; -; mRNA.
DR   EMBL; AK168479; BAE40368.1; -; mRNA.
DR   EMBL; BC012435; AAH12435.1; -; mRNA.
DR   EMBL; AF003951; AAB88256.1; -; mRNA.
DR   CCDS; CCDS23161.1; -.
DR   RefSeq; NP_036169.1; NM_012039.2.
DR   AlphaFoldDB; O54692; -.
DR   SMR; O54692; -.
DR   BioGRID; 205086; 35.
DR   IntAct; O54692; 19.
DR   MINT; O54692; -.
DR   STRING; 10090.ENSMUSP00000034803; -.
DR   GlyGen; O54692; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O54692; -.
DR   PhosphoSitePlus; O54692; -.
DR   SwissPalm; O54692; -.
DR   EPD; O54692; -.
DR   jPOST; O54692; -.
DR   MaxQB; O54692; -.
DR   PaxDb; 10090-ENSMUSP00000034803; -.
DR   PeptideAtlas; O54692; -.
DR   ProteomicsDB; 275171; -.
DR   Pumba; O54692; -.
DR   Antibodypedia; 3162; 189 antibodies from 26 providers.
DR   DNASU; 26951; -.
DR   Ensembl; ENSMUST00000034803.10; ENSMUSP00000034803.9; ENSMUSG00000032264.10.
DR   GeneID; 26951; -.
DR   KEGG; mmu:26951; -.
DR   UCSC; uc009piu.2; mouse.
DR   AGR; MGI:1349478; -.
DR   CTD; 9183; -.
DR   MGI; MGI:1349478; Zw10.
DR   VEuPathDB; HostDB:ENSMUSG00000032264; -.
DR   eggNOG; KOG2163; Eukaryota.
DR   GeneTree; ENSGT00390000016427; -.
DR   HOGENOM; CLU_012948_0_0_1; -.
DR   InParanoid; O54692; -.
DR   OMA; TWPRMSE; -.
DR   OrthoDB; 2786073at2759; -.
DR   PhylomeDB; O54692; -.
DR   TreeFam; TF105966; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 26951; 13 hits in 77 CRISPR screens.
DR   ChiTaRS; Zw10; mouse.
DR   PRO; PR:O54692; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O54692; Protein.
DR   Bgee; ENSMUSG00000032264; Expressed in gastrula and 255 other cell types or tissues.
DR   ExpressionAtlas; O54692; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0070939; C:Dsl1/NZR complex; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000776; C:kinetochore; ISS:HGNC-UCL.
DR   GO; GO:0005828; C:kinetochore microtubule; ISS:HGNC-UCL.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR   GO; GO:1990423; C:RZZ complex; ISO:MGI.
DR   GO; GO:0000922; C:spindle pole; ISS:HGNC-UCL.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:HGNC-UCL.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR   GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISO:MGI.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:HGNC-UCL.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:HGNC-UCL.
DR   GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:HGNC-UCL.
DR   GO; GO:0007096; P:regulation of exit from mitosis; ISS:HGNC-UCL.
DR   Gene3D; 1.10.357.150; -; 1.
DR   InterPro; IPR046362; Zw10/DSL1_C_sf.
DR   InterPro; IPR048343; ZW10_C.
DR   InterPro; IPR048344; Zw10_middle.
DR   InterPro; IPR009361; Zw10_N.
DR   PANTHER; PTHR12205; CENTROMERE/KINETOCHORE PROTEIN ZW10; 1.
DR   PANTHER; PTHR12205:SF0; CENTROMERE_KINETOCHORE PROTEIN ZW10 HOMOLOG; 1.
DR   Pfam; PF20666; ZW10_C; 1.
DR   Pfam; PF20665; Zw10_middle; 1.
DR   Pfam; PF06248; Zw10_N; 1.
DR   Genevisible; O54692; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW   ER-Golgi transport; Kinetochore; Lipid droplet; Membrane; Mitosis;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   CHAIN           2..779
FT                   /note="Centromere/kinetochore protein zw10 homolog"
FT                   /id="PRO_0000184958"
FT   REGION          2..317
FT                   /note="Interaction with RINT1"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   REGION          2..81
FT                   /note="Interaction with ZWINT"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   COILED          14..130
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   MOD_RES         777
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43264"
FT   CONFLICT        143
FT                   /note="E -> A (in Ref. 1; BAE26337)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="T -> A (in Ref. 1; BAE26337/BAE39941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="A -> T (in Ref. 1; BAE39941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="T -> K (in Ref. 1; BAE26337)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   779 AA;  88063 MW;  5C02CF77FDF5B13B CRC64;
     MASFVTEVLA HSGSLEKEDL GTRISRLTRR VEEIKGEVCN MISKKYSEFL PTMQSAQALV
     TQVDTLSNDI DQLKSRIETE VCRDLHISTV EFTNLKQQLE RDSVVLTLLK QLQEFSSAIE
     EYNSALAEKK YIPAARHLEE AQECLKLLKS RKCFDLKMLK SLSMELTVQK QNILYHLGED
     WQKLVVWKFP PAKDTSSLES CLQTELHLCT EQPEKEDMTP LPSISSVLLA FSILGELPTK
     LKSFGQMLLK YILKPLVTCP SLHAVIERQP SSVSICFESL TTDLEHPSPP EAFAKIRLVL
     EVLQKQLLDL PLDADLEIGK VPGIVLAEML GEGIWEDLSE CLIRNCLVYS IPTNSSKLQE
     YEEIIQSTEE FEKFLKEMRF LKGDTTDLLK YARNINSHFA NKKCQDVIVA ARNLMTSEIH
     NTVKIGPDCK EALPDLPSPD ADHKLQVQTV CKAQFTDAGN LEPETSLDPQ SFSLPTCRIS
     EAVKKLMELA YQTLLEATTS SDQCAVQLFY SVRNIFHLFH DVVPTYHKEN LRKLPQLAAI
     HHNNCMYIAH HLLTLGHQFR LRLAPILCDG TTTFVDLVPG FRRLGTECFL AQMQAQKGEL
     LERLSSARSF ANMDDEENYS AASKAVRQVL HQLRRLGIVW QDVLPVNIYC KAMGTLLNTA
     IAEMMSRITA LEDISTEDGD RLYSLCKTVM DEGPQVFAPL SDENKNKKYQ EEVPVYVSKW
     MPFKELMIML QASLQEIGDR WADGKGPLAT AFPSSEVKAL IRALFQNTER RAAALAKIK
//