ID G1T899_RABIT Unreviewed; 1275 AA.
AC G1T899;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Arginine-glutamic acid dipeptide repeats {ECO:0000313|Ensembl:ENSOCUP00000012783.3};
GN Name=RERE {ECO:0000313|Ensembl:ENSOCUP00000012783.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000012783.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000012783.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000012783.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000012783.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000012783.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAGW02064345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02064346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02064347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02064348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02064349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1T899; -.
DR SMR; G1T899; -.
DR STRING; 9986.ENSOCUP00000012783; -.
DR PaxDb; 9986-ENSOCUP00000012783; -.
DR Ensembl; ENSOCUT00000014870.3; ENSOCUP00000012783.3; ENSOCUG00000014859.4.
DR eggNOG; KOG2133; Eukaryota.
DR GeneTree; ENSGT00940000153615; -.
DR HOGENOM; CLU_005292_1_0_1; -.
DR InParanoid; G1T899; -.
DR TreeFam; TF328554; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000014859; Expressed in uterus and 16 other cell types or tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IEA:Ensembl.
DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IEA:Ensembl.
DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IEA:Ensembl.
DR CDD; cd04709; BAH_MTA; 1.
DR CDD; cd11661; SANT_MTA3_like; 1.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 4.10.1240.50; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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 PANTHER; PTHR13859:SF12; ARGININE-GLUTAMIC ACID DIPEPTIDE REPEATS PROTEIN; 1.
DR PANTHER; PTHR13859; ATROPHIN-RELATED; 1.
DR Pfam; PF03154; Atrophin-1; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 102..282
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 283..386
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 390..442
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..88
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..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..931
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1051
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 138697 MW; D6DEA5D5A2E4468B CRC64;
MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY AESDHSEDED
NDNSATTEES TKKNKKKPPK KKSRYERTDT GEITSYITED DVVYRPGDCV YIESRRPNTP
YFICSIQDFK LVHNSQACCR SPTPALCDPP ACSLPVASQP PQHLSEAGRG PVGSKRDHLL
MNVKWYYRQS EVPDSVYQHL VQDRHNENDS GRELVITDPV IKNRELFISD YVDTYHAAAL
RGKCNISHFS DIFAAREFKA RVDSFFYILG YNPETRRLNS TQGEIRVGPS HQAKLPDLQP
FPSPDGDTVT QHEELVWMPG VNDCDLLMYL RAARSMAAFA GMFDGASTEE ACVFTFWENT
TLNALTPLHE SGYDAGKALQ RLVKKPVPKL IEKGWTEEEV KRFVKGLRQY GKNFFRIRKE
LLPNKETGEL ITFYYYWKKT PEAASSRAHR RHRRQAVFRR IKTRTASTPV STPSRPPSSE
FLDLSSASED DFDSEDSEQE LKGYACRHCF TTTSKDWHHG GRENILLCTD CRIHFKKYGE
LPPIEKPVDP PPFMFKPVKE EDDGLSGKHS MRTRRSRGSM STLRSGRKKQ PASPDGRASP
INEDIRSSGR TSPSAASTSS NDSKAETVKK SAKKVKEEAS SPLKSSKRQR EKVASDTEES
DRTSSKKTKT QEISRPNSPS EGEGESSDSR SVNDEGSSDP KDIDQDNRST SPSIPSPQDN
ESDSDSSAQQ QQLLQAQPPA LQAPGGAATA PPTAPAGPPQ LPTPGPTPSA PAAPAQGSPA
AVQPPSQAPA AVAPAAHSHV QQAPALHPPR LPSPHPPAGQ APAATHSQPA LHSQGPHGLQ
AGPLLQHPGP PQPFGLPPQA SQGQASLGAS PAAAHPHSTL PLPAAQAALQ PQQPPKEQPL
PPAPLAMPHI KPPPTTPIPQ LPAPQAHKHP PHLSGPSPFS MNANLPPPPA LKPLSSLSTH
HPPSAHPPPL QLMPQSQPLA SSPAQPPGLT QNQSLPPSAA SHPPASLHQV PPQPPFAQHP
FVPGGPPSIT PPACPSTSTP PAGPSTPAQP PCSAAVPSGG VPGGAACPLP AVQIKEEARE
DAEEPESPPP PPRSPSPEPT VVDTPSHASQ SARFYKHLDR GYNSCARTDL YFMPLAGSKL
AKKREEAIEK AKREAEQKAR EEREREKEKE KERERERERE REAERAAVSL GCQAPAGGHW
AAALAWAAWR VLESEDQVLV VPIPGFGDRG GASEPRSSGA LQVPADPHQC LESTCLGAAR
VGPLLSLYLK DLSPV
//
