CENPV_MOUSE
ID CENPV_MOUSE Reviewed; 252 AA.
AC Q9CXS4; B2RWK8; B9EK22; Q5SX21; Q6PIA5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Centromere protein V;
DE Short=CENP-V;
DE AltName: Full=Proline-rich protein 6;
GN Name=Cenpv; Synonyms=Prr6;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and 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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Required for distribution of pericentromeric heterochromatin
CC in interphase nuclei and for centromere formation and organization,
CC chromosome alignment and cytokinesis. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01239};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01239};
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q7Z7K6}. Nucleus {ECO:0000250|UniProtKB:Q7Z7K6}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q7Z7K6}.
CC Note=Enriched at the nuclear periphery and around the nucleolus. In
CC mitotic cells, localizes to kinetochores from prometaphase to
CC metaphase. At anaphase onset, transfers to the spindle midzone and then
CC to the mid-body in telophase and cytokinesis.
CC {ECO:0000250|UniProtKB:Q7Z7K6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CXS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CXS4-2; Sequence=VSP_019551;
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000305}.
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DR EMBL; AK014046; BAB29130.1; -; mRNA.
DR EMBL; AL596181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466601; EDL10349.1; -; Genomic_DNA.
DR EMBL; BC038868; AAH38868.1; -; mRNA.
DR EMBL; BC147794; AAI47795.1; -; mRNA.
DR EMBL; BC147795; AAI47796.1; -; mRNA.
DR EMBL; BC147835; AAI47836.1; -; mRNA.
DR EMBL; BC147837; AAI47838.1; -; mRNA.
DR CCDS; CCDS48818.1; -. [Q9CXS4-1]
DR RefSeq; NP_082724.1; NM_028448.1. [Q9CXS4-1]
DR AlphaFoldDB; Q9CXS4; -.
DR SMR; Q9CXS4; -.
DR BioGRID; 215794; 5.
DR IntAct; Q9CXS4; 5.
DR MINT; Q9CXS4; -.
DR STRING; 10090.ENSMUSP00000018653; -.
DR iPTMnet; Q9CXS4; -.
DR PhosphoSitePlus; Q9CXS4; -.
DR SwissPalm; Q9CXS4; -.
DR EPD; Q9CXS4; -.
DR jPOST; Q9CXS4; -.
DR MaxQB; Q9CXS4; -.
DR PaxDb; Q9CXS4; -.
DR PeptideAtlas; Q9CXS4; -.
DR PRIDE; Q9CXS4; -.
DR ProteomicsDB; 283883; -. [Q9CXS4-1]
DR ProteomicsDB; 283884; -. [Q9CXS4-2]
DR Antibodypedia; 25303; 80 antibodies from 22 providers.
DR DNASU; 73139; -.
DR Ensembl; ENSMUST00000018653; ENSMUSP00000018653; ENSMUSG00000018509. [Q9CXS4-1]
DR GeneID; 73139; -.
DR KEGG; mmu:73139; -.
DR UCSC; uc007jjf.2; mouse. [Q9CXS4-1]
DR CTD; 201161; -.
DR MGI; MGI:1920389; Cenpv.
DR VEuPathDB; HostDB:ENSMUSG00000018509; -.
DR eggNOG; KOG4192; Eukaryota.
DR GeneTree; ENSGT00390000003183; -.
DR HOGENOM; CLU_087799_1_0_1; -.
DR InParanoid; Q9CXS4; -.
DR OMA; HRLSCEE; -.
DR OrthoDB; 1326510at2759; -.
DR PhylomeDB; Q9CXS4; -.
DR TreeFam; TF313636; -.
DR BioGRID-ORCS; 73139; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cenpv; mouse.
DR PRO; PR:Q9CXS4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CXS4; protein.
DR Bgee; ENSMUSG00000018509; Expressed in spermatocyte and 249 other tissues.
DR ExpressionAtlas; Q9CXS4; baseline and differential.
DR Genevisible; Q9CXS4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001667; P:ameboidal-type cell migration; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034508; P:centromere complex assembly; ISS:UniProtKB.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0033044; P:regulation of chromosome organization; ISS:UniProtKB.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF04828; GFA; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Kinetochore; Metal-binding; Methylation; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..252
FT /note="Centromere protein V"
FT /id="PRO_0000244360"
FT DOMAIN 125..237
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 39
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7K6"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..173
FT /note="MRRTRSAVATGPREQRRSGATGGLSGGESRAQRSRSRTRAGAGGGGGAVGPQ
FT PSAKPRPKPPPRAQEAAAEEPPPAVTPAASVSALDLGEQRERWETFQKRQRLSFEGAAK
FT LLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIFDCNCSICKKKQNRHFIVPASRFK
FT LLK -> MINVYLSLFSQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019551"
FT CONFLICT 30
FT /note="R -> P (in Ref. 1; BAB29130 and 4; AAH38868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 27541 MW; 8F63A72A21DAAE20 CRC64;
MRRTRSAVAT GPREQRRSGA TGGLSGGESR AQRSRSRTRA GAGGGGGAVG PQPSAKPRPK
PPPRAQEAAA EEPPPAVTPA ASVSALDLGE QRERWETFQK RQRLSFEGAA KLLLDTFEYQ
GLVKHTGGCH CGAVRFEVWA SADLHIFDCN CSICKKKQNR HFIVPASRFK LLKGAESITT
YTFNTHKAQH TFCKRCGVQS FYTPRSNPGG FGIAPHCLDE GTVRSVVTEE FNGSDWERAM
KEHKTIKNMS KE
