EID3_MOUSE
ID EID3_MOUSE Reviewed; 375 AA.
AC Q3V124; Q3TTL4; Q4KL03; Q8CF34; Q9CVN8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=EP300-interacting inhibitor of differentiation 3;
DE Short=EID-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|MGI:MGI:1913591};
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] {ECO:0000312|EMBL:BAE21329.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21329.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAE21329.1};
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] {ECO:0000312|EMBL:AAH99545.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH99545.1};
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).
RN [3]
RP SUBUNIT.
RX PubMed=15970276; DOI=10.1016/j.bbrc.2005.06.013;
RA Sasajima Y., Tanaka H., Miyake S., Yuasa Y.;
RT "A novel EID family member, EID-3, inhibits differentiation and forms a
RT homodimer or heterodimer with EID-2.";
RL Biochem. Biophys. Res. Commun. 333:969-975(2005).
RN [4]
RP INTERACTION WITH NSMCE2 AND SMC6, AND IDENTIFICATION IN THE SMC5-SMC6
RP COMPLEX.
RX PubMed=21364888; DOI=10.1371/journal.pone.0017270;
RA Hudson J.J., Bednarova K., Kozakova L., Liao C., Guerineau M., Colnaghi R.,
RA Vidot S., Marek J., Bathula S.R., Lehmann A.R., Palecek J.;
RT "Interactions between the Nse3 and Nse4 components of the SMC5-6 complex
RT identify evolutionarily conserved interactions between MAGE and EID
RT Families.";
RL PLoS ONE 6:E17270-E17270(2011).
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; EID3 seems to
CC be a testis-specific subunit. NSMCE1, NSMCE4A or EID3 and NSMCE3
CC probably form a subcomplex that bridges the head domains of the
CC SMC5:SMC6 heterodimer. Homodimer, and heterodimer with EID2. Interacts
CC with the C-terminal region of CREBBP (By similarity). {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=AAH99545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK006438; BAC25142.1; ALT_INIT; mRNA.
DR EMBL; AK007194; BAB24893.3; -; mRNA.
DR EMBL; AK132745; BAE21329.1; -; mRNA.
DR EMBL; AK161275; BAE36286.1; -; mRNA.
DR EMBL; AK161307; BAE36311.1; -; mRNA.
DR EMBL; BC099545; AAH99545.1; ALT_INIT; mRNA.
DR CCDS; CCDS83739.1; -.
DR RefSeq; NP_079775.2; NM_025499.2.
DR AlphaFoldDB; Q3V124; -.
DR SMR; Q3V124; -.
DR BioGRID; 211398; 2.
DR IntAct; Q3V124; 2.
DR iPTMnet; Q3V124; -.
DR PhosphoSitePlus; Q3V124; -.
DR PRIDE; Q3V124; -.
DR ProteomicsDB; 277844; -.
DR Antibodypedia; 54643; 75 antibodies from 16 providers.
DR Ensembl; ENSMUST00000211623; ENSMUSP00000147261; ENSMUSG00000109864.
DR GeneID; 66341; -.
DR KEGG; mmu:66341; -.
DR UCSC; uc007gkc.1; mouse.
DR CTD; 493861; -.
DR MGI; MGI:1913591; Eid3.
DR VEuPathDB; HostDB:ENSMUSG00000109864; -.
DR GeneTree; ENSGT00940000165197; -.
DR InParanoid; Q3V124; -.
DR OMA; TPVSYFE; -.
DR PhylomeDB; Q3V124; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR BioGRID-ORCS; 66341; 0 hits in 53 CRISPR screens.
DR PRO; PR:Q3V124; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3V124; protein.
DR Bgee; ENSMUSG00000109864; Expressed in seminiferous tubule of testis and 36 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 1: Evidence at protein level;
KW Chromosome; Coiled coil; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; Nucleus; Reference proteome; Repressor; Telomere;
KW Transcription; Transcription regulation.
FT CHAIN 1..375
FT /note="EP300-interacting inhibitor of differentiation 3"
FT /id="PRO_0000315907"
FT REGION 30..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..51
FT /evidence="ECO:0000255"
FT COMPBIAS 38..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1
FT /note="M -> L (in Ref. 1; BAC25142)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="D -> N (in Ref. 1; BAC25142)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="D -> E (in Ref. 1; BAC25142)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> A (in Ref. 1; BAC25142)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="V -> L (in Ref. 1; BAE36311/BAE36286)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="N -> K (in Ref. 1; BAC25142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 43308 MW; 9637798934ADDF24 CRC64;
MSKEKCSLTG GKEKRGELVR SLAWQHLVKQ EEEEAVKKEE KEEGEDEEEE GSDSSSDDPN
PEPPCMHPDL LELVVDREKC RKIRRQYRQL IYTVQQNRED IVNTASDTLS EALEEANVLF
DGVSRTREAA LDAQFLVLAS DLGKEKAKQL NTDMNFFNPI AFCDLLLLFV GFNWVEEECK
EFSDCDDSIV LSFWGMLHEE ATSWMLQAET FHFIFGSFKA ERSARKPRLG CHKRACKMEG
SGDMPTKLRR LDVHANQETT EKEVERILGL LQTYFQKYPD TPVSYFEFVI DPNSFSRTVE
NIFYVSFIIR DGFARIRLDQ DRLPILEPTN VSQVDDESDS YSYCRKQGVI SLSLQDWKNI
VSTFEISEAM IKNSY
