ID A0A1U7QHY5_MESAU Unreviewed; 1554 AA.
AC A0A1U7QHY5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Arginine-glutamic acid dipeptide repeats protein isoform X4 {ECO:0000313|RefSeq:XP_005079347.1};
GN Name=Rere {ECO:0000313|RefSeq:XP_005079347.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005079347.1};
RN [1] {ECO:0000313|RefSeq:XP_005079347.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_005079347.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_005079347.1; XM_005079290.3.
DR STRING; 10036.ENSMAUP00000013033; -.
DR eggNOG; KOG2133; Eukaryota.
DR OrthoDB; 3349425at2759; -.
DR Proteomes; UP000189706; Unplaced.
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 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:UP000189706};
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..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1230
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..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1554 AA; 171085 MW; 8BB3D306CAD31E58 CRC64;
MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENGRPRRS CTLEGGAKNY AESDHSEDED
NDNSATTEES TKKNKKKPPK KKSRYERTDT GEITSYITED DIVYRPGDCV YIESRRPNTP
YFICSIQDFK LVHSSQACCR 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 EEDGLSGKHS MRTRRSRGSM STLRSGRKKQ PASPDGRASP
INEDIRSSGR NSPSAASTSS NDSKAESVKK SAKKAKEESA SPLKSAKRQR EKVASDTEEP
DRTTSKKTKT QEISRPNSPS EGEGESSDSR SVNDEGSSDP KDIDQDNRST SPSIPSPQDN
ESDSDSSAQQ QTLQAQPPSL QAPSGAASAP SAPPGAPQLP APGPTPSATA VPPQGSPATS
QPPNQTQSAV APAAHTHIQQ APTLHPPRLP SPHAPLQPLT APPSQNTAQP HTQPSLHGQG
PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQGPLGPSPA AHPHTTVQLA ASQSALQPQQ
PPREQPLPPA PLAMPHIKPP PTTPIPQLPA PQAHKHPPHL SGPSPFSMNA NLPPPPALKP
LSSLSTHHPP SAHPPPLQLM PQSQPLPSSP AQPPGLTQSQ NLPPPAPAHP PTGLHQVPSQ
PPFPQHPFVP GGPPPVTPPT CPSTSTPPSG PSTSSQPPCP AGSSGGGVPG APSCPLPAVQ
IKEEAPDEAE EPESPPPPPR SPSPEPTIVD APSHASQSAR FYKHLDRGYN SCARTDLYFM
PLAGSKLAKK REEAIEKAKR EAEQKAREER EREKEKEKER EREREREREA ERAAKASSSA
HEGRLSDPQL SGPGHMRPSF EPPPTTIAAV PPYIGPDTPA LRTLSEYARP HVMSPTNRNH
PFYMPLNPTD PLLAYHMPGL YNVDPTIRER ELREREIRER EIRERELRER MKPGFEVKPP
ELDPLHPATN PMEHFARHSA LTIPPAAGPH PFASFHPGLN PLERERLALA GPQLRPEMSY
PDRLAAERIH AERMASLSSD PLARLQMFNV TPHHHQHSHI HSHLHLHQQD PLHQGSAGPV
HPLVDPLTAG PHLARFPYPP GTLPNPLLGQ PPHEHEMLRH PVFGTPYPRD LPGAIPPPMS
AAHQLQAMHA QSAELQRLAM EQQWLHGHPH MHGGHLPSQE DYYSRLKKEG DKQL
//