LOCUS       NP_446337               1559 aa            linear   ROD 31-MAR-2024
DEFINITION  arginine-glutamic acid dipeptide repeats protein [Rattus
            norvegicus].
ACCESSION   NP_446337 XP_575962
VERSION     NP_446337.2
DBSOURCE    REFSEQ: accession NM_053885.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1559)
  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
REFERENCE   2  (residues 1 to 1559)
  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
REFERENCE   3  (residues 1 to 1559)
  AUTHORS   Jordan,V.K., Fregeau,B., Ge,X., Giordano,J., Wapner,R.J.,
            Balci,T.B., Carter,M.T., Bernat,J.A., Moccia,A.N., Srivastava,A.,
            Martin,D.M., Bielas,S.L., Pappas,J., Svoboda,M.D., Rio,M.,
            Boddaert,N., Cantagrel,V., Lewis,A.M., Scaglia,F., Kohler,J.N.,
            Bernstein,J.A., Dries,A.M., Rosenfeld,J.A., DeFilippo,C.,
            Thorson,W., Yang,Y., Sherr,E.H., Bi,W. and Scott,D.A.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Genotype-phenotype correlations in individuals with pathogenic RERE
            variants
  JOURNAL   Hum Mutat 39 (5), 666-675 (2018)
   PUBMED   29330883
REFERENCE   4  (residues 1 to 1559)
  AUTHORS   Kim,B.J. and Scott,D.A.
  TITLE     Mouse model reveals the role of RERE in cerebellar foliation and
            the migration and maturation of Purkinje cells
  JOURNAL   PLoS One 9 (1), e87518 (2014)
   PUBMED   24466353
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1559)
  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
REFERENCE   6  (residues 1 to 1559)
  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
REFERENCE   7  (residues 1 to 1559)
  AUTHORS   Khan,F.A., Margolis,R.L., Loev,S.L., Sharp,A.H., Li,S.H. and
            Ross,C.A.
  TITLE     cDNA cloning and characterization of an atrophin-1 (DRPLA disease
            gene)-related protein
  JOURNAL   Neurobiol Dis 3 (2), 121-128 (1996)
   PUBMED   9173919
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1, AW920332.1, CK470955.1, AI113241.1, CB728130.1,
            CA511326.1 and CB328253.1.
            
            On Oct 17, 2007 this sequence version replaced NP_446337.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA5760383,
                              SAMEA5760386 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1559
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..1559
                     /product="arginine-glutamic acid dipeptide repeats
                     protein"
                     /note="atrophin-1-related protein; arginine-glutamic acid
                     dipeptide (RE) repeats"
                     /calculated_mol_wt=171685
     Region          1..89
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62901.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Region          101..306
                     /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            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80TZ9; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Region          285..335
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Region          394..439
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(395,425..426,428..429,431..433,435..437)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          463..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62901.2)"
     Region          502..551
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          541..1125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62901.2)"
     Region          567..1558
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1098
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80TZ9; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1150
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q80TZ9; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Region          1154..1239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1252
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     Site            1259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P2R6; propagated from
                     UniProtKB/Swiss-Prot (Q62901.2)"
     CDS             1..1559
                     /gene="Rere"
                     /gene_synonym="Arp"
                     /coded_by="NM_053885.2:581..5260"
                     /db_xref="GeneID:116665"
                     /db_xref="RGD:629475"
ORIGIN      
        1 mtadkdkdkd kekdrdrdrd rerdkrdkar esenarprrs ctleggakny aesdhseded
       61 ndngattees arksrkkppk kksryertdt geitsyited dvvyrpgdcv yiesrrpntp
      121 yficsiqdfk lvhnsqaccr spapalcdpp acslpvasqp pqhlseagrg pvgskrdhll
      181 mnvkwyyrqs evpdsvyqhl vqdrhnends grelvitdpv iknrelfisd yvdtyhaaal
      241 rgkcnishfs difaarefka rvdsffyilg ynpetrrlns tqgeirvgps hqaklpdlqp
      301 fpspdgdtvt qheelvwmpg vsdcdllmyl raarsmaafa gmcdggsted gcvaasrddt
      361 tlnalntlhe ssydagkalq rlvkkpvpkl iekcwtedev krfvkglrqy gknffrirke
      421 llpnketgel itfyyywkkt peaassrahr rhrrqavfrr iktrtastpv ntpsrppsse
      481 fldlssased dfdsedseqe lkgyacrhcf tttskdwhhg grenillctd crihfkkyge
      541 lppiekpvdp ppfmfkpvke eddglsgkhs mrtrrsrgsm stlrsgrkkq paspdgrasp
      601 vnedvrssgr nspsaastss ndskaeavkk sakkvkeeaa splkntkrqr ekvasdtedt
      661 dratskktkt qeisrpnsps egegessdsr svndegssdp kdidqdnrst spsipspqdn
      721 esdsdssaqq qmlqtqppal qapsgaasap stappgttql ptpgptpsat tvppqgspat
      781 sqppnqtqst vapaahtliq qtptlhpprl psphpplqpm tappsqnsaq phpqpslhgq
      841 gppgphslqt gpllqhpgpp qpfgltpqss qgqgplgpsp aaahphstiq lpasqsalqp
      901 qqppreqplp paplamphik pppttpipql papqahkhpp hlsgpspfsm nanlppppal
      961 kplsslsthh ppsahppplq lmpqsqplps spaqppgltq sqslpppaas hpttgglhqv
     1021 psqspfpqhp fvpggpppit ppscpptstp pagpssssqp pcsaavssgg nvpgapscpl
     1081 pavqikeeal deaeepespp ppprspspep tvvdtpshas qsarfykhld rgynscartd
     1141 lyfmplagsk lakkreeaie kakreaeqka reererekek ekerererer ereaeraaqk
     1201 asssahegrl sdpqlsgpgh mrpsfepppt tiaavppyig pdtpalrtls eyarphvmsp
     1261 tnrnhpfymp lnptdpllay hmpglynvdp tirerelrer eirereirer elrermkpgf
     1321 evkppeldpl hpatnpmehf arhsaltipp aagphpfasf hpglnplere rlalagpqlr
     1381 pemsypdrla aerihaerma sltsdplarl qmfnvtphhh qhshihshlh lhqqdplhqg
     1441 sagpvhplvd pltagphlar fpyppgtlpn pllgqppheh emlrhpvfgt pyprdlpgai
     1501 pppmsaahql qamhaqsael qrlameqqwl hghphmhggh lpsqedyysr lkkegdkql
//
