ID   CENPQ_RAT               Reviewed;         270 AA.
AC   Q66H02;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Centromere protein Q;
DE            Short=CENP-Q;
GN   Name=Cenpq;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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. Plays an
CC       important role in chromosome congression and in the recruitment of
CC       CENP-O complex (which comprises CENPO, CENPP, CENPQ and CENPU), CENPE
CC       and PLK1 to the kinetochores. {ECO:0000250|UniProtKB:Q7L2Z9}.
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.
CC       {ECO:0000250|UniProtKB:Q7L2Z9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7L2Z9}.
CC       Chromosome, centromere {ECO:0000250|UniProtKB:Q7L2Z9}. Note=Localizes
CC       exclusively in the centromeres. The CENPA-CAD complex is probably
CC       recruited on centromeres by the CENPA-NAC complex.
CC       {ECO:0000250|UniProtKB:Q7L2Z9}.
CC   -!- PTM: Phosphorylation at Ser-52 is essential for CENPE recruitment to
CC       kinetochores and orderly chromosome congression.
CC       {ECO:0000250|UniProtKB:Q7L2Z9}.
CC   -!- SIMILARITY: Belongs to the CENP-Q/OKP1 family. {ECO:0000305}.
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DR   EMBL; BC082113; AAH82113.1; -; mRNA.
DR   RefSeq; NP_001014237.1; NM_001014215.1.
DR   AlphaFoldDB; Q66H02; -.
DR   SMR; Q66H02; -.
DR   iPTMnet; Q66H02; -.
DR   PhosphoSitePlus; Q66H02; -.
DR   DNASU; 363198; -.
DR   GeneID; 363198; -.
DR   KEGG; rno:363198; -.
DR   UCSC; RGD:1359451; rat.
DR   CTD; 55166; -.
DR   RGD; 1359451; Cenpq.
DR   InParanoid; Q66H02; -.
DR   OrthoDB; 1159538at2759; -.
DR   PhylomeDB; Q66H02; -.
DR   Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-RNO-68877; Mitotic Prometaphase.
DR   Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR   PRO; PR:Q66H02; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031511; C:Mis6-Sim4 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR   GO; GO:1905342; P:positive regulation of protein localization to kinetochore; ISS:UniProtKB.
DR   InterPro; IPR025212; CAD_CENP-Q.
DR   PANTHER; PTHR31345; PTHR31345; 1.
DR   Pfam; PF13094; CENP-Q; 1.
PE   2: Evidence at transcript level;
KW   Centromere; Chromosome; Coiled coil; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..270
FT                   /note="Centromere protein Q"
FT                   /id="PRO_0000089536"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          143..205
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        19..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L2Z9"
SQ   SEQUENCE   270 AA;  31002 MW;  1434D98DF2B784CD CRC64;
     MSGKANTSKK KSQRVKRNVK QRADKEDEEL DSPENKVGNR AKRNRSHAGH LSSKEQTKCV
     HLKRVKISSN KRTAWQPLPK NTEEYLQSMM DSAILGILNK NIKRKEQIQY HLDQLKKRFL
     QQCATLKVPP GKLNYLRDMS KLLKVEREQE RANEESLASL QEEIDKIVET TESMTENIES
     LKTKIEILTN EVEKEEEEMK EVFHIDSNKV LALPELSQKS LKAPILQKEI LTLIPNQNAL
     LKDLDVLQNS APGKNMAAFI QEAYMKLNGS