CENPR_RAT
ID CENPR_RAT Reviewed; 176 AA.
AC Q5U1Z7;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Centromere protein R;
DE Short=CENP-R;
DE AltName: Full=Nuclear receptor-interacting factor 3;
GN Name=Itgb3bp; Synonyms=Cenpr, Nrif3;
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=Ovary;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription coregulator that can have both coactivator and
CC corepressor functions. Involved in the coactivation of nuclear
CC receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-
CC dependent fashion. In contrast, it does not coactivate nuclear
CC receptors for retinoic acid, vitamin D, progesterone receptor, nor
CC glucocorticoid. Acts as a coactivator for estrogen receptor alpha. Acts
CC as a transcriptional corepressor via its interaction with the NFKB1 NF-
CC kappa-B subunit, possibly by interfering with the transactivation
CC domain of NFKB1. Induces apoptosis in breast cancer cells, but not in
CC other cancer cells, via a caspase-2 mediated pathway that involves
CC mitochondrial membrane permeabilization but does not require other
CC caspases. May also act as an inhibitor of cyclin A-associated kinase.
CC Also acts a 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; mediated by the coiled coil domain. Interacts with
CC CCNA2 and MTA1. Interacts with NFKB1 NF-kappa-B subunit. Component of
CC the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP,
CC CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-
CC NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN,
CC CENPT and CENPU (By similarity). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:Q13352, ECO:0000250|UniProtKB:Q9CQ82}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC -!- DOMAIN: The DD1 domain (also called RepD1 domain) mediates the
CC corepressor function and is essential in the triggering of apoptosis.
CC {ECO:0000250}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, a motif known
CC to be important for the association with nuclear receptors.
CC {ECO:0000250}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, which is
CC essential for the association with nuclear receptors. {ECO:0000250}.
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DR EMBL; BC086363; AAH86363.1; -; mRNA.
DR RefSeq; NP_001013231.1; NM_001013213.1.
DR AlphaFoldDB; Q5U1Z7; -.
DR SMR; Q5U1Z7; -.
DR STRING; 10116.ENSRNOP00000012947; -.
DR iPTMnet; Q5U1Z7; -.
DR PhosphoSitePlus; Q5U1Z7; -.
DR PaxDb; Q5U1Z7; -.
DR GeneID; 362548; -.
DR KEGG; rno:362548; -.
DR UCSC; RGD:1310044; rat.
DR CTD; 23421; -.
DR RGD; 1310044; Itgb3bp.
DR VEuPathDB; HostDB:ENSRNOG00000009116; -.
DR eggNOG; ENOG502S4AR; Eukaryota.
DR HOGENOM; CLU_122442_0_0_1; -.
DR InParanoid; Q5U1Z7; -.
DR OMA; TRQMSPF; -.
DR OrthoDB; 1343610at2759; -.
DR PhylomeDB; Q5U1Z7; -.
DR TreeFam; TF336291; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-205043; NRIF signals cell death from the nucleus.
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:Q5U1Z7; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009116; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q5U1Z7; baseline and differential.
DR Genevisible; Q5U1Z7; RN.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR009601; CENP-R.
DR PANTHER; PTHR15581; PTHR15581; 1.
DR Pfam; PF06729; CENP-R; 1.
DR PIRSF; PIRSF011860; NRIF3_coact_rcpt; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Isopeptide bond; Kinetochore; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..176
FT /note="Centromere protein R"
FT /id="PRO_0000249512"
FT REGION 20..50
FT /note="DD1"
FT /evidence="ECO:0000250"
FT REGION 34..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..112
FT /evidence="ECO:0000255"
FT MOTIF 63..66
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 118..122
FT /note="LXXLL motif"
FT MOTIF 171..175
FT /note="LXXIL motif"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13352"
SQ SEQUENCE 176 AA; 19917 MW; 3689888C1BEFF6A6 CRC64;
MPVKRSLKLD DQFEENSFGP SKIMRKKSIT AFSPTTGTYQ LSPFSSPRTP KEQEHRDGPS
NGTRKWSVLS SPARQDSTVK GSDGFMMLLS KIERSSEKTM EIMKNLSSLQ ALEGNRQLED
LLGVSLVPCS LKSEAKKTKE LMTKVMKQKL FEKKNSRIPP KEHHPNSFEF LKAILN
