ID   CENPO_MOUSE             Reviewed;         298 AA.
AC   Q8K015; Q8R587; Q9CYY6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Centromere protein O;
DE            Short=CENP-O;
GN   Name=Cenpo; Synonyms=Mcm21r;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Forelimb, and 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 MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Eye, and Mammary tumor;
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).
CC   -!- FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a
CC       complex recruited to centromeres which is involved in assembly of
CC       kinetochore proteins, mitotic progression and chromosome segregation.
CC       May be involved in incorporation of newly synthesized CENPA into
CC       centromeres via its interaction with the CENPA-NAC complex. Modulates
CC       the kinetochore-bound levels of NDC80 complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK,
CC       CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex
CC       interacts with the CENPA-NAC complex, at least composed of CENPA,
CC       CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC       {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC       Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is
CC       probably recruited on centromeres by the CENPA-NAC complex (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K015-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K015-2; Sequence=VSP_020447, VSP_020448;
CC   -!- SIMILARITY: Belongs to the CENP-O/MCM21 family. {ECO:0000305}.
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DR   EMBL; AK013198; BAB28707.1; -; mRNA.
DR   EMBL; AK029226; BAC26354.1; -; mRNA.
DR   EMBL; AK134266; BAE22073.1; -; mRNA.
DR   EMBL; BC023148; AAH23148.1; -; mRNA.
DR   EMBL; BC034399; AAH34399.1; -; mRNA.
DR   CCDS; CCDS25788.1; -. [Q8K015-1]
DR   RefSeq; NP_598807.2; NM_134046.5. [Q8K015-1]
DR   RefSeq; XP_006515215.1; XM_006515152.3.
DR   RefSeq; XP_011242186.1; XM_011243884.2. [Q8K015-2]
DR   AlphaFoldDB; Q8K015; -.
DR   SMR; Q8K015; -.
DR   BioGRID; 206626; 3.
DR   ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR   CORUM; Q8K015; -.
DR   IntAct; Q8K015; 1.
DR   MINT; Q8K015; -.
DR   STRING; 10090.ENSMUSP00000119136; -.
DR   iPTMnet; Q8K015; -.
DR   PhosphoSitePlus; Q8K015; -.
DR   EPD; Q8K015; -.
DR   MaxQB; Q8K015; -.
DR   PaxDb; 10090-ENSMUSP00000119136; -.
DR   PeptideAtlas; Q8K015; -.
DR   ProteomicsDB; 281374; -. [Q8K015-1]
DR   ProteomicsDB; 281375; -. [Q8K015-2]
DR   Pumba; Q8K015; -.
DR   Antibodypedia; 27556; 195 antibodies from 30 providers.
DR   DNASU; 52504; -.
DR   Ensembl; ENSMUST00000111169.10; ENSMUSP00000106799.4; ENSMUSG00000020652.18. [Q8K015-2]
DR   Ensembl; ENSMUST00000140975.8; ENSMUSP00000119136.2; ENSMUSG00000020652.18. [Q8K015-1]
DR   GeneID; 52504; -.
DR   KEGG; mmu:52504; -.
DR   UCSC; uc007mxn.1; mouse. [Q8K015-1]
DR   AGR; MGI:1923800; -.
DR   CTD; 79172; -.
DR   MGI; MGI:1923800; Cenpo.
DR   VEuPathDB; HostDB:ENSMUSG00000020652; -.
DR   eggNOG; ENOG502RY72; Eukaryota.
DR   GeneTree; ENSGT00390000016702; -.
DR   InParanoid; Q8K015; -.
DR   OMA; MEWANDG; -.
DR   OrthoDB; 4172416at2759; -.
DR   PhylomeDB; Q8K015; -.
DR   TreeFam; TF335524; -.
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-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 52504; 29 hits in 80 CRISPR screens.
DR   ChiTaRS; Cenpo; mouse.
DR   PRO; PR:Q8K015; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8K015; Protein.
DR   Bgee; ENSMUSG00000020652; Expressed in primary oocyte and 212 other cell types or tissues.
DR   ExpressionAtlas; Q8K015; baseline and differential.
DR   GO; GO:0000939; C:inner kinetochore; ISO:MGI.
DR   GO; GO:0031511; C:Mis6-Sim4 complex; IBA:GO_Central.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0034508; P:centromere complex assembly; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; NAS:ComplexPortal.
DR   InterPro; IPR018464; CENP-O.
DR   PANTHER; PTHR14582:SF1; CENTROMERE PROTEIN O; 1.
DR   PANTHER; PTHR14582; INNER KINETOCHORE SUBUNIT MAL2; 1.
DR   Pfam; PF09496; CENP-O; 1.
DR   Genevisible; Q8K015; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Centromere; Chromosome; Coiled coil; Kinetochore;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Centromere protein O"
FT                   /id="PRO_0000249503"
FT   REGION          29..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          39..74
FT                   /evidence="ECO:0000255"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU64"
FT   VAR_SEQ         197..205
FT                   /note="SDFCDVLTG -> NWTADSPSR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020447"
FT   VAR_SEQ         206..298
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_020448"
FT   CONFLICT        30
FT                   /note="I -> V (in Ref. 2; AAH23148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="A -> T (in Ref. 2; AAH23148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="R -> S (in Ref. 2; AAH23148)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="E -> A (in Ref. 2; AAH23148)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   298 AA;  34154 MW;  6A616612463B31E9 CRC64;
     MESANTLCPG RKCKGGVLAH LERLEAQTNI SNRKSEEPAV RKKESSLRTK IRELRQQRDK
     LRAEVKQWGA RVKEPPAKED PSRTVISEQE VLEREWRNVD AILEAYRFTG LSGKLTSRGV
     CMCISTAFEG NLLDSYFVDL VIEKPLRIHH HSVPVFIPLE KIAAAHLQTD VQRFLFRLWE
     YLNAYAGRKY QADQLESDFC DVLTGPLQRN ALCNLLSFTY KVEQRCQTFS FSARLLYEDP
     TAALPTNVTV TRPGVEASSP PWEEHRASHQ MLFRTKPLHK VFASFSKETE KLHLNLVS
//