RERE_RAT
ID RERE_RAT Reviewed; 1559 AA.
AC Q62901;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Arginine-glutamic acid dipeptide repeats protein;
DE AltName: Full=Atrophin-1-related protein;
GN Name=Rere; Synonyms=Arp;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9173919; DOI=10.1006/nbdi.1996.0012;
RA Khan F.A., Margolis R.L., Loev S.L., Sharp A.H., Li S.-H., Ross C.A.;
RT "cDNA cloning and characterization of an atrophin-1 (DRPLA disease gene)-
RT related protein.";
RL Neurobiol. Dis. 3:121-128(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-593; SER-599;
RP SER-641; SER-655; SER-674 AND SER-678, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role as a transcriptional repressor during
CC development. May play a role in the control of cell survival (By
CC similarity). Interacts with FAT1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HDAC1 and ATN1. Interaction with ATN1 is
CC improved when the poly-Gln region of ATN1 is extended (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000250}. Note=Localized
CC in nuclear bodies of variable size. Colocalized with PML and BAX in
CC nuclear PODs (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9173919}.
CC -!- DOMAIN: The interaction with ATN1 is mediated by the coiled domain.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA98970.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U44091; AAA98970.1; ALT_FRAME; mRNA.
DR EMBL; AABR03040456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03040863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03040940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03041203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T42731; T42731.
DR RefSeq; NP_446337.2; NM_053885.2.
DR AlphaFoldDB; Q62901; -.
DR SMR; Q62901; -.
DR STRING; 10116.ENSRNOP00000024443; -.
DR iPTMnet; Q62901; -.
DR PhosphoSitePlus; Q62901; -.
DR PaxDb; Q62901; -.
DR PRIDE; Q62901; -.
DR Ensembl; ENSRNOT00000024443; ENSRNOP00000024443; ENSRNOG00000017940.
DR GeneID; 116665; -.
DR KEGG; rno:116665; -.
DR UCSC; RGD:629475; rat.
DR CTD; 473; -.
DR RGD; 629475; Rere.
DR eggNOG; KOG2133; Eukaryota.
DR GeneTree; ENSGT00940000153615; -.
DR HOGENOM; CLU_005292_1_0_1; -.
DR InParanoid; Q62901; -.
DR OMA; HAYPGYA; -.
DR PhylomeDB; Q62901; -.
DR TreeFam; TF328554; -.
DR PRO; PR:Q62901; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000017940; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q62901; RN.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; ISO:RGD.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; ISO:RGD.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; ISO:RGD.
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..1559
FT /note="Arginine-glutamic acid dipeptide repeats protein"
FT /id="PRO_0000083506"
FT DOMAIN 102..282
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 283..386
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 390..442
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 507..532
FT /note="GATA-type"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1148..1205
FT /evidence="ECO:0000255"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..940
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..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:22673903"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ9"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ9"
FT MOD_RES 1111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 1150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80TZ9"
FT MOD_RES 1252
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT CROSSLNK 559
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT CROSSLNK 636
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P2R6"
FT CONFLICT 342..343
FT /note="MC -> IVV (in Ref. 1; AAA98970)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="A -> G (in Ref. 1; AAA98970)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="T -> N (in Ref. 1; AAA98970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1559 AA; 171815 MW; 2BE2A7A93CAE0600 CRC64;
MTADKDKDKD KEKDRDRDRD RERDKRDKAR ESENARPRRS CTLEGGAKNY AESDHSEDED
NDNGATTEES ARKSRKKPPK KKSRYERTDT GEITSYITED DVVYRPGDCV YIESRRPNTP
YFICSIQDFK LVHNSQACCR SPAPALCDPP ACSLPVASQP PQHLSEAGRG PVGSKRDHLL
MNVKWYYRQS EVPDSVYQHL VQDRHNENDS GRELVITDPV IKNRELFISD YVDTYHAAAL
RGKCNISHFS DIFAAREFKA RVDSFFYILG YNPETRRLNS TQGEIRVGPS HQAKLPDLQP
FPSPDGDTVT QHEELVWMPG VSDCDLLMYL RAARSMAAFA GMCDGGSTED GCVAASRDDT
TLNALNTLHE SSYDAGKALQ RLVKKPVPKL IEKCWTEDEV KRFVKGLRQY GKNFFRIRKE
LLPNKETGEL ITFYYYWKKT PEAASSRAHR RHRRQAVFRR IKTRTASTPV NTPSRPPSSE
FLDLSSASED DFDSEDSEQE LKGYACRHCF TTTSKDWHHG GRENILLCTD CRIHFKKYGE
LPPIEKPVDP PPFMFKPVKE EDDGLSGKHS MRTRRSRGSM STLRSGRKKQ PASPDGRASP
VNEDVRSSGR NSPSAASTSS NDSKAEAVKK SAKKVKEEAA SPLKNTKRQR EKVASDTEDT
DRATSKKTKT QEISRPNSPS EGEGESSDSR SVNDEGSSDP KDIDQDNRST SPSIPSPQDN
ESDSDSSAQQ QMLQTQPPAL QAPSGAASAP STAPPGTTQL PTPGPTPSAT TVPPQGSPAT
SQPPNQTQST VAPAAHTLIQ QTPTLHPPRL PSPHPPLQPM TAPPSQNSAQ PHPQPSLHGQ
GPPGPHSLQT GPLLQHPGPP QPFGLTPQSS QGQGPLGPSP AAAHPHSTIQ LPASQSALQP
QQPPREQPLP PAPLAMPHIK PPPTTPIPQL PAPQAHKHPP HLSGPSPFSM NANLPPPPAL
KPLSSLSTHH PPSAHPPPLQ LMPQSQPLPS SPAQPPGLTQ SQSLPPPAAS HPTTGGLHQV
PSQSPFPQHP FVPGGPPPIT PPSCPPTSTP PAGPSSSSQP PCSAAVSSGG NVPGAPSCPL
PAVQIKEEAL DEAEEPESPP PPPRSPSPEP TVVDTPSHAS QSARFYKHLD RGYNSCARTD
LYFMPLAGSK LAKKREEAIE KAKREAEQKA REEREREKEK EKERERERER EREAERAAQK
ASSSAHEGRL SDPQLSGPGH MRPSFEPPPT TIAAVPPYIG PDTPALRTLS EYARPHVMSP
TNRNHPFYMP LNPTDPLLAY HMPGLYNVDP TIRERELRER EIREREIRER ELRERMKPGF
EVKPPELDPL HPATNPMEHF ARHSALTIPP AAGPHPFASF HPGLNPLERE RLALAGPQLR
PEMSYPDRLA AERIHAERMA SLTSDPLARL QMFNVTPHHH QHSHIHSHLH LHQQDPLHQG
SAGPVHPLVD PLTAGPHLAR FPYPPGTLPN PLLGQPPHEH EMLRHPVFGT PYPRDLPGAI
PPPMSAAHQL QAMHAQSAEL QRLAMEQQWL HGHPHMHGGH LPSQEDYYSR LKKEGDKQL
