LOCUS       NP_001078961            1558 aa            linear   ROD 10-DEC-2024
DEFINITION  arginine-glutamic acid dipeptide repeats protein [Mus musculus].
ACCESSION   NP_001078961 XP_204015 XP_912917
VERSION     NP_001078961.1
DBSOURCE    REFSEQ: accession NM_001085492.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1558)
  AUTHORS   Alam,S.S., Kumar,S., Beauchamp,M.C., Bareke,E., Boucher,A.,
            Nzirorera,N., Dong,Y., Padilla,R., Zhang,S.J., Majewski,J. and
            Jerome-Majewska,L.A.
  TITLE     Snrpb is required in murine neural crest cells for proper splicing
            and craniofacial morphogenesis
  JOURNAL   Dis Model Mech 15 (6) (2022)
   PUBMED   35593225
REFERENCE   2  (residues 1 to 1558)
  AUTHORS   Kim,B.J. and Scott,D.A.
  TITLE     RERE deficiency causes retinal and optic nerve atrophy through
            degeneration of retinal cells
  JOURNAL   Dev Dyn 250 (10), 1398-1409 (2021)
   PUBMED   33742727
  REMARK    GeneRIF: RERE deficiency causes retinal and optic nerve atrophy
            through degeneration of retinal cells.
REFERENCE   3  (residues 1 to 1558)
  AUTHORS   Kim,B.J., Zaveri,H.P., Kundert,P.N., Jordan,V.K., Scott,T.M.,
            Carmichael,J. and Scott,D.A.
  TITLE     RERE deficiency contributes to the development of orofacial clefts
            in humans and mice
  JOURNAL   Hum Mol Genet 30 (7), 595-602 (2021)
   PUBMED   33772547
  REMARK    GeneRIF: RERE deficiency contributes to the development of
            orofacial clefts in humans and mice.
REFERENCE   4  (residues 1 to 1558)
  AUTHORS   Kim,B.J., Zaveri,H.P., Jordan,V.K., Hernandez-Garcia,A.,
            Jacob,D.J., Zamora,D.L., Yu,W., Schwartz,R.J. and Scott,D.A.
  TITLE     RERE deficiency leads to decreased expression of GATA4 and the
            development of ventricular septal defects
  JOURNAL   Dis Model Mech 11 (9) (2018)
   PUBMED   30061196
  REMARK    GeneRIF: Rere and Gata4 interact genetically in the development of
            congenital heart defects.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1558)
  AUTHORS   Vilhais-Neto,G.C., Fournier,M., Plassat,J.L., Sardiu,M.E.,
            Saraf,A., Garnier,J.M., Maruhashi,M., Florens,L., Washburn,M.P. and
            Pourquie,O.
  TITLE     The WHHERE coactivator complex is required for retinoic
            acid-dependent regulation of embryonic symmetry
  JOURNAL   Nat Commun 8 (1), 728 (2017)
   PUBMED   28959017
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1558)
  AUTHORS   Hou,R. and Sibinga,N.E.
  TITLE     Atrophin proteins interact with the Fat1 cadherin and regulate
            migration and orientation in vascular smooth muscle cells
  JOURNAL   J Biol Chem 284 (11), 6955-6965 (2009)
   PUBMED   19131340
REFERENCE   7  (residues 1 to 1558)
  AUTHORS   Shen,Y., Lee,G., Choe,Y., Zoltewicz,J.S. and Peterson,A.S.
  TITLE     Functional architecture of atrophins
  JOURNAL   J Biol Chem 282 (7), 5037-5044 (2007)
   PUBMED   17150957
  REMARK    GeneRIF: Atrophin-1 and the short form of Atrophin-2 can act as
            potent and evolutionarily conserved transcriptional activators.
REFERENCE   8  (residues 1 to 1558)
  AUTHORS   Zoltewicz,J.S., Stewart,N.J., Leung,R. and Peterson,A.S.
  TITLE     Atrophin 2 recruits histone deacetylase and is required for the
            function of multiple signaling centers during mouse embryogenesis
  JOURNAL   Development 131 (1), 3-14 (2004)
   PUBMED   14645126
  REMARK    GeneRIF: act as transcriptional co-repressor during embryonic
            development.
REFERENCE   9  (residues 1 to 1558)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Aizawa,H., Yuasa,S.,
            Nakajima,D., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: II. The complete nucleotide sequences of 400 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (1), 35-48 (2003)
   PUBMED   12693553
REFERENCE   10 (residues 1 to 1558)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606903.8, AL691453.7, AL606988.16 and AL606982.21.
            
            On or before Jul 25, 2007 this sequence version replaced
            XP_912917.1, XP_204015.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN00849374,
                              SAMN00849375 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1558
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 81.34 cM"
     Protein         1..1558
                     /product="arginine-glutamic acid dipeptide repeats
                     protein"
                     /note="atrophin-2"
                     /calculated_mol_wt=171624
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Region          102..307
                     /region_name="BAH_MTA"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in MTA1 and similar proteins. The Metastasis-associated
                     protein MTA1 is part of the NURD (nucleosome remodeling
                     and deacetylating) complex and plays a role in cellular
                     transformation and metastasis. BAH...; cd04709"
                     /db_xref="CDD:240060"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Region          286..336
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Region          395..440
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(396,426..427,429..430,432..434,436..438)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          464..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Region          503..552
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          542..1125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Region          568..1557
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1098
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1150
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Region          1154..1238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1251
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     Site            1258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q80TZ9.3)"
     CDS             1..1558
                     /gene="Rere"
                     /gene_synonym="1110033A15Rik; ARG; ARP; ATN1L; Atr2; DNB1;
                     eye<m03Jus>; eyes3; mKIAA0458"
                     /coded_by="NM_001085492.1:305..4981"
                     /db_xref="CCDS:CCDS38979.1"
                     /db_xref="GeneID:68703"
                     /db_xref="MGI:MGI:2683486"
ORIGIN      
        1 mtadkdkdkd kekdrdrdrd rerdkrdkar esenarprrs ctleggakny aesdhseded
       61 ndnnsattee snkksrkkpp kkksryertd tgeitsyite ddvvyrpgdc vyiesrrpnt
      121 pyficsiqdf klvhssqacc rspapafcdp pacslpvapq ppqhlseagr gpggskrdhl
      181 lmnvkwyyrq sevpdsvyqh lvqdrhnend sgrelvitdp viknrelfis dyvdtyhaaa
      241 lrgkcnishf sdifaarefk arvdsffyil gynpetrrln stqgeirvgp shqaklpdlq
      301 pfpspdgdtv tqheelvwmp gvsdcdllmy lraarsmaaf agmcdggste dgcvaasrdd
      361 ttlnalntlh essydagkal qrlvkkpvpk liekcwtede vkrfvkglrq ygknffrirk
      421 ellpsketge litfyyywkk tpeaassrah rrhrrqavfr riktrtastp vntpsrppss
      481 efldlssase ddfdsedseq elkgyacrhc ftttskdwhh ggrenillct dcrihfkkyg
      541 elppiekpvd pppfmfkpvk eeddglsgkh smrtrrsrgs mstlrsgrkk qptspdgras
      601 pinedirssg rnspsaasts sndskaetvk ksakkvkeea asplkstkrq rekvasdted
      661 tdritskktk tqeisrpnsp segegessds rsvndegssd pkdidqdnrs tspsipspqd
      721 nesdsdssaq qqmlqaqppa lqapsgaasa pstappgtpq lptqgptpsa tavppqgspa
      781 tsqppnqtqs tvapaahthi qqaptlhppr lpsphpplqp mtappsqssa qphpqpslhs
      841 qgppgphslq tgpllqhpgp pqpfglpsqp sqgqgplgps paaahphsti qlpasqsalq
      901 pqqppreqpl ppaplamphi kpppttpipq lpapqahkhp phlsgpspfs lnanlppppa
      961 lkplsslsth hppsahpppl qlmpqsqplp sspaqppglt qsqslpppaa shpttglhqv
     1021 psqspfpqhp fvpggpppit ppscpptstp pagpssssqp pcsaavssgg svpgapscpl
     1081 pavqikeeal deaeepespp ppprspspep tvvdtpshas qsarfykhld rgynscartd
     1141 lyfmplagsk lakkreeaie kakreaeqka reererekek ekerererer ereaeraaka
     1201 sssahegrls dpqlsgpghm rpsfeppptt iaavppyigp dtpalrtlse yarphvmspt
     1261 nrnhpfympl nptdpllayh mpglynvdpt irerelrere irereirere lrermkpgfe
     1321 vkppeldplh patnpmehfa rhsaltippa agphpfasfh pglnplerer lalagpqlrp
     1381 emsypdrlaa erihaermas ltsdplarlq mfnvtphhhq hshihshlhl hqqdplhqgs
     1441 agpvhplvdp ltagphlarf pyppgtlpnp llgqpphehe mlrhpvfgtp yprdlpgaip
     1501 ppmsaahqlq amhaqsaelq rlameqqwlh ghphmhgghl psqedyysrl kkegdkql
//
