RERE_MOUSE
ID RERE_MOUSE Reviewed; 1558 AA.
AC Q80TZ9; A2A7T4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Arginine-glutamic acid dipeptide repeats protein;
DE AltName: Full=Atrophin-2;
GN Name=Rere; Synonyms=Atr2, Kiaa0458;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 673-1558.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP FUNCTION, INTERACTION WITH ATN1 AND HDAC1, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14645126; DOI=10.1242/dev.00908;
RA Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.;
RT "Atrophin 2 recruits histone deacetylase and is required for the function
RT of multiple signaling centers during mouse embryogenesis.";
RL Development 131:3-14(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-679, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-142; THR-593;
RP SER-594; SER-600; SER-675; SER-679; SER-1098; SER-1105 AND SER-1107, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1150, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Plays a role as a transcriptional repressor during
CC development. May play a role in the control of cell survival.
CC {ECO:0000269|PubMed:14645126}.
CC -!- SUBUNIT: Interacts with HDAC1 and ATN1. Interaction with ATN1 is
CC improved when the poly-Gln region of ATN1 is extended. Interacts with
CC FAT1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Note=Localized
CC in nuclear bodies of variables size. Colocalized with PML and BAX in
CC nuclear PODs (By similarity). {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 8.25 dpc expression is strongly elevated in the
CC anterior midline. At 8.5 dpc expression is elevated throughout the
CC anteroposterior extent of the notochord and is down-regulated in the
CC heart. At 8.75 dpc expression is increased in the ventral brain. At 9.5
CC dpc strong expression appears besides the notochord including the
CC apical ectodermal ridge (AER), the isthmus and the ventral
CC diencephalon. At 10.5 dpc expression increases in the notochord, the
CC AER and spinal and brain neurons. {ECO:0000269|PubMed:14645126}.
CC -!- DOMAIN: The interaction with ATN1 is mediated by the coiled domain.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice embryos exhibit a variety of patterning
CC defects that first appear at 8.0 dpc. Defects include a specific
CC failure in ventralization of the anterior neural plate, loss of heart
CC looping and irregular partitioning of somites. In mutant embryos, Shh
CC expression fails to initiate along the anterior midline at 8.0 dpc, and
CC Fgf8 is delocalized from the anterior neural ridge at 8.5 dpc.
CC {ECO:0000269|PubMed:14645126}.
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DR EMBL; AL606982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122287; BAC65569.1; -; Transcribed_RNA.
DR CCDS; CCDS38979.1; -.
DR RefSeq; NP_001078961.1; NM_001085492.1.
DR AlphaFoldDB; Q80TZ9; -.
DR SMR; Q80TZ9; -.
DR BioGRID; 213002; 4.
DR IntAct; Q80TZ9; 3.
DR STRING; 10090.ENSMUSP00000101307; -.
DR iPTMnet; Q80TZ9; -.
DR PhosphoSitePlus; Q80TZ9; -.
DR EPD; Q80TZ9; -.
DR jPOST; Q80TZ9; -.
DR MaxQB; Q80TZ9; -.
DR PaxDb; Q80TZ9; -.
DR PeptideAtlas; Q80TZ9; -.
DR PRIDE; Q80TZ9; -.
DR ProteomicsDB; 255287; -.
DR Antibodypedia; 13215; 162 antibodies from 24 providers.
DR DNASU; 68703; -.
DR Ensembl; ENSMUST00000105682; ENSMUSP00000101307; ENSMUSG00000039852.
DR GeneID; 68703; -.
DR KEGG; mmu:68703; -.
DR UCSC; uc008vxr.1; mouse.
DR CTD; 473; -.
DR MGI; MGI:2683486; Rere.
DR VEuPathDB; HostDB:ENSMUSG00000039852; -.
DR eggNOG; KOG2133; Eukaryota.
DR GeneTree; ENSGT00940000153615; -.
DR HOGENOM; CLU_005292_1_0_1; -.
DR InParanoid; Q80TZ9; -.
DR OMA; HAYPGYA; -.
DR OrthoDB; 136778at2759; -.
DR PhylomeDB; Q80TZ9; -.
DR TreeFam; TF328554; -.
DR BioGRID-ORCS; 68703; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Rere; mouse.
DR PRO; PR:Q80TZ9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80TZ9; protein.
DR Bgee; ENSMUSG00000039852; Expressed in vestibular membrane of cochlear duct and 270 other tissues.
DR ExpressionAtlas; Q80TZ9; baseline and differential.
DR Genevisible; Q80TZ9; MM.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:MGI.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:MGI.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IMP:MGI.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IPI:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR InterPro; IPR002951; Atrophin-like.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR Pfam; PF03154; Atrophin-1; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Developmental protein; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1558
FT /note="Arginine-glutamic acid dipeptide repeats protein"
FT /id="PRO_0000083505"
FT DOMAIN 103..283
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 284..387
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 391..443
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 507..532
FT /note="GATA-type"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1148..1203
FT /evidence="ECO:0000255"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..781
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..841
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1003
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 1150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1251
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 1258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT CROSSLNK 560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT CROSSLNK 637
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT CONFLICT 840
FT /note="S -> G (in Ref. 2; BAC65569)"
FT /evidence="ECO:0000305"
FT CONFLICT 1236..1239
FT /note="Missing (in Ref. 2; BAC65569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1558 AA; 171755 MW; 723A76184971CAA3 CRC64;
MTADKDKDKD KEKDRDRDRD RERDKRDKAR ESENARPRRS CTLEGGAKNY AESDHSEDED
NDNNSATTEE SNKKSRKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT
PYFICSIQDF KLVHSSQACC RSPAPAFCDP PACSLPVAPQ PPQHLSEAGR GPGGSKRDHL
LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA
LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ
PFPSPDGDTV TQHEELVWMP GVSDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD
TTLNALNTLH ESSYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK
ELLPSKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS
EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG
ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPTSPDGRAS
PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA ASPLKSTKRQ REKVASDTED
TDRITSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD
NESDSDSSAQ QQMLQAQPPA LQAPSGAASA PSTAPPGTPQ LPTQGPTPSA TAVPPQGSPA
TSQPPNQTQS TVAPAAHTHI QQAPTLHPPR LPSPHPPLQP MTAPPSQSSA QPHPQPSLHS
QGPPGPHSLQ TGPLLQHPGP PQPFGLPSQP SQGQGPLGPS PAAAHPHSTI QLPASQSALQ
PQQPPREQPL PPAPLAMPHI KPPPTTPIPQ LPAPQAHKHP PHLSGPSPFS LNANLPPPPA
LKPLSSLSTH HPPSAHPPPL QLMPQSQPLP SSPAQPPGLT QSQSLPPPAA SHPTTGLHQV
PSQSPFPQHP FVPGGPPPIT PPSCPPTSTP PAGPSSSSQP PCSAAVSSGG SVPGAPSCPL
PAVQIKEEAL DEAEEPESPP PPPRSPSPEP TVVDTPSHAS QSARFYKHLD RGYNSCARTD
LYFMPLAGSK LAKKREEAIE KAKREAEQKA REEREREKEK EKERERERER EREAERAAKA
SSSAHEGRLS DPQLSGPGHM RPSFEPPPTT IAAVPPYIGP DTPALRTLSE YARPHVMSPT
NRNHPFYMPL NPTDPLLAYH MPGLYNVDPT IRERELRERE IREREIRERE LRERMKPGFE
VKPPELDPLH PATNPMEHFA RHSALTIPPA AGPHPFASFH PGLNPLERER LALAGPQLRP
EMSYPDRLAA ERIHAERMAS LTSDPLARLQ MFNVTPHHHQ HSHIHSHLHL HQQDPLHQGS
AGPVHPLVDP LTAGPHLARF PYPPGTLPNP LLGQPPHEHE MLRHPVFGTP YPRDLPGAIP
PPMSAAHQLQ AMHAQSAELQ RLAMEQQWLH GHPHMHGGHL PSQEDYYSRL KKEGDKQL
