CYREN_RAT
ID CYREN_RAT Reviewed; 160 AA.
AC Q6AYH4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cell cycle regulator of non-homologous end joining {ECO:0000250|UniProtKB:Q9BWK5};
DE Short=Cell cycle regulator of NHEJ {ECO:0000250|UniProtKB:Q9BWK5};
DE AltName: Full=Modulator of retrovirus infection homolog {ECO:0000250|UniProtKB:Q09HN1};
GN Name=Cyren {ECO:0000312|RGD:1563238};
GN Synonyms=Mri {ECO:0000250|UniProtKB:Q09HN1};
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: Cell-cycle-specific regulator of classical non-homologous end
CC joining (NHEJ) of DNA double-strand break (DSB) repair, which can act
CC both as an activator or inhibitor of NHEJ, depending on the cell cycle
CC phase (By similarity). Acts as a regulator of DNA repair pathway choice
CC by specifically inhibiting classical NHEJ during the S and G2 phases,
CC thereby promoting error-free repair by homologous recombination during
CC cell cycle phases when sister chromatids are present. Preferentially
CC protects single-stranded overhangs at break sites by inhibiting
CC classical NHEJ, thereby creating a local environment that favors
CC homologous recombination. Acts via interaction with XRCC5/Ku80 and
CC XRCC6/Ku70 (By similarity). In contrast, acts as an activator of NHEJ
CC during G1 phase of the cell cycle: promotes classical NHEJ in G1 phase
CC cells via multivalent interactions that increase the affinity of DNA
CC damage response proteins for DSB-associated chromatin. Also involved in
CC immunoglobulin V(D)J recombination (By similarity). May also act as an
CC indirect regulator of proteasome (By similarity).
CC {ECO:0000250|UniProtKB:Q09HN1, ECO:0000250|UniProtKB:Q8BHZ5,
CC ECO:0000250|UniProtKB:Q9BWK5}.
CC -!- SUBUNIT: Interacts (via KBM motif) with XRCC5/Ku80 and XRCC6/Ku70
CC heterodimer. Interacts (via XLF motif) with TRIM28/KAP1, ATM, MRE11,
CC NBN and RAD50. {ECO:0000250|UniProtKB:Q8BHZ5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BWK5}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BWK5}. Chromosome
CC {ECO:0000250|UniProtKB:Q8BHZ5}. Note=Nuclear localization may depend
CC upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer (By
CC similarity). Localizes to DNA damage sites (By similarity).
CC {ECO:0000250|UniProtKB:Q8BHZ5, ECO:0000250|UniProtKB:Q9BWK5}.
CC -!- DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80
CC and XRCC6/Ku70 and recruitment to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q8BHZ5}.
CC -!- DOMAIN: The XLM (XLF-like motif) mediates interaction with DNA damage
CC response proteins TRIM28/KAP1, ATM and members of the MRN complex
CC (MRE11, NBN and RAD50). {ECO:0000250|UniProtKB:Q8BHZ5}.
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DR EMBL; BC079043; AAH79043.1; -; mRNA.
DR RefSeq; NP_001019496.1; NM_001024325.1.
DR AlphaFoldDB; Q6AYH4; -.
DR STRING; 10116.ENSRNOP00000034483; -.
DR PaxDb; Q6AYH4; -.
DR Ensembl; ENSRNOT00000029818; ENSRNOP00000034483; ENSRNOG00000026958.
DR GeneID; 500077; -.
DR KEGG; rno:500077; -.
DR UCSC; RGD:1563238; rat.
DR CTD; 78996; -.
DR RGD; 1563238; Cyren.
DR eggNOG; ENOG502SEX2; Eukaryota.
DR GeneTree; ENSGT00390000013192; -.
DR HOGENOM; CLU_126072_0_0_1; -.
DR InParanoid; Q6AYH4; -.
DR OMA; AKAPKRM; -.
DR OrthoDB; 1349796at2759; -.
DR PhylomeDB; Q6AYH4; -.
DR TreeFam; TF336925; -.
DR PRO; PR:Q6AYH4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000026958; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; ISS:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR InterPro; IPR028278; MRI.
DR PANTHER; PTHR14566; PTHR14566; 1.
DR Pfam; PF15325; MRI; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Cytoplasm; DNA damage; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..160
FT /note="Cell cycle regulator of non-homologous end joining"
FT /id="PRO_0000320950"
FT REGION 78..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..21
FT /note="KBM"
FT /evidence="ECO:0000250|UniProtKB:Q9BWK5"
FT MOTIF 150..160
FT /note="XLM"
FT /evidence="ECO:0000250|UniProtKB:Q9BWK5"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWK5"
SQ SEQUENCE 160 AA; 17487 MW; 71E404D667390822 CRC64;
METLKSDNKK RVLPSWMTAP GNERKVVSVK TAKRKQTAAI RVGAATRAPA KETVYCMNEA
EMVDVALGIL IEGRKQEKPW EQPSLVAPDK LQLSPPCSES PHTSSPGSSS EEEDSRTDSP
ALGLSPARGP EASNSPCSRS PEEGKEEEDE LKYVREIFFS
