ID   EID3_RAT                Reviewed;         387 AA.
AC   Q4V8G2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=EP300-interacting inhibitor of differentiation 3;
DE            Short=EID-3;
DE   AltName: Full=E1A-like inhibitor of differentiation 3;
DE   AltName: Full=EID-1-like inhibitor of differentiation 3;
DE   AltName: Full=Non-structural maintenance of chromosomes element 4 homolog B;
DE            Short=NS4EB;
DE            Short=Non-SMC element 4 homolog B;
GN   Name=Eid3 {ECO:0000312|EMBL:AAH97404.1};
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] {ECO:0000312|EMBL:AAH97404.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000312|EMBL:AAH97404.1};
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: Tissue-specific component of the SMC5-SMC6 complex, a complex
CC       involved in repair of DNA double-strand breaks by homologous
CC       recombination. The complex may promote sister chromatid homologous
CC       recombination by recruiting the SMC1-SMC3 cohesin complex to double-
CC       strand breaks. The complex is required for telomere maintenance via
CC       recombination and mediates sumoylation of shelterin complex (telosome)
CC       components (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Acts as a repressor of nuclear receptor-dependent
CC       transcription possibly by interfering with CREBBP-dependent
CC       coactivation. May function as a coinhibitor of other CREBBP/EP300-
CC       dependent transcription factors (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC       SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC       or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC       domains of the SMC5:SMC6 heterodimer. Homodimer, and heterodimer with
CC       EID2. Interacts with the C-terminal region of CREBBP (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N140}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8N140}. Chromosome, telomere {ECO:0000250}.
CC       Note=May shuttle between nucleus and cytoplasm.
CC       {ECO:0000250|UniProtKB:Q8N140}.
CC   -!- SIMILARITY: Belongs to the NSE4 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH97404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC097404; AAH97404.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001037769.2; NM_001044304.1.
DR   AlphaFoldDB; Q4V8G2; -.
DR   GeneID; 691688; -.
DR   KEGG; rno:691688; -.
DR   UCSC; RGD:1597206; rat.
DR   CTD; 493861; -.
DR   RGD; 1597206; Eid3.
DR   InParanoid; Q4V8G2; -.
DR   OrthoDB; 935469at2759; -.
DR   PhylomeDB; Q4V8G2; -.
DR   PRO; PR:Q4V8G2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; ISS:UniProtKB.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   InterPro; IPR027786; Nse4/EID.
DR   InterPro; IPR014854; Nse4_C.
DR   InterPro; IPR029225; Nse4_Nse3-bd.
DR   PANTHER; PTHR16140; PTHR16140; 1.
DR   Pfam; PF15412; Nse4-Nse3_bdg; 1.
DR   Pfam; PF08743; Nse4_C; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Cytoplasm; DNA damage; DNA recombination; DNA repair; Nucleus;
KW   Reference proteome; Repressor; Telomere; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..387
FT                   /note="EP300-interacting inhibitor of differentiation 3"
FT                   /id="PRO_0000315908"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..68
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  44785 MW;  879EF3B5E2924125 CRC64;
     MSEEKCSLTG GEEKGEELAR SLAWQHLVKQ AEEDDDDDEE ALKKEEEEEE EEEEEDEEEE
     EEGPDSSSDD LSPEAPCMHP DLLELAVDRE KCRSIRRQYR QLIYTVQQNR EDIVNTASDS
     LTEALEEANV LFDGVSRTRE AALDAQFLVL ASDLGKEKAK QLNSDMSFFN HVAFCELLLV
     FVGLNWMEEE CEELSECDES IALSFWNMLH KEATAWMLQA ETFHFIFGSF KAERSARKPR
     QEHHKRACKM EGNGDMPTKL RKLDVHANQE TTEKEVERIL GLLQTYFQKY PDTPVSYFEF
     VIDPNSFSRT VENIFYVSFI IRDGFARIRL DQDRLPILEP TNVNQVDEEN DSCSYCRKQG
     VISLSLQDWK NIVSTFEISE AMIKNSY