ID G3SR00_LOXAF Unreviewed; 1558 AA.
AC G3SR00;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Arginine-glutamic acid dipeptide repeats {ECO:0000313|Ensembl:ENSLAFP00000002258.3};
GN Name=RERE {ECO:0000313|Ensembl:ENSLAFP00000002258.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002258.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000002258.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002258.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000002258.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002258.3};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR RefSeq; XP_010591442.1; XM_010593140.1.
DR STRING; 9785.ENSLAFP00000002258; -.
DR Ensembl; ENSLAFT00000002698.3; ENSLAFP00000002258.3; ENSLAFG00000002698.3.
DR eggNOG; KOG2133; Eukaryota.
DR GeneTree; ENSGT00940000153615; -.
DR HOGENOM; CLU_005292_1_0_1; -.
DR InParanoid; G3SR00; -.
DR OMA; VMYLRAA; -.
DR TreeFam; TF328554; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:UP000007646};
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 103..283
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 284..387
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 391..443
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1238
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 50..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1558 AA; 171678 MW; 7887DEF2C7DD704B CRC64;
MTADKDKDKD KEKDRDRDRD RERDKRDKAR ESENSRPRRS CTLEGGAKNY AESDHSEDED
NDNNSATTEE STKKNKKKPP KKKSRYERTD TGEITSYITE DDVVYKPGDC VYIESRRPNT
PYFICSIQDF KLVHNSQACC RSPTPALCDP PACSLPVASQ PPQHLSEAGR GPVGSKRDHL
LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA
LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ
PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD
TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK
ELLPNKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS
EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG
ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRAS
PINEDIRSSG RNSPSAASTS SNDSKSETVK KSAKKVKEEA SSPLKSTKRQ REKVASDTEE
VDRTNSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD
NESDSDSSAQ QQMLQAQPPA LQAPSGAAPT PSTAPPGATQ HSTSGPTPSV PAGPPQGSPS
ASQPPNQPQA STAPAPHTHI QQAPALHPQR LPSPHPPLQP LTGPAGQTTA QPHAQPSLHS
QGPPGPHSLQ AGPLLQHPGP PQPFGLPPQA TQGQAPLGAP QAAAHPHSTL QLPASQAALQ
SQQPPREQPL PPAPLAMPHI KPPPTTPIPQ LPAPQAHKHP PHLSGPSPFS MNANLPPPPA
LKPLSSLSTH HPPSAHPPPL QLMPQSQPLP SSPAQPPVLT QSQSLPPTAA AHPTSGLHQV
APQPSFAQHP FVPGGPPSIT PPACPSTSTP PAGPGTSAQP PCSAAVSSGG SMPGGTSCPL
PTVQIKEEAL EEAEEPESPP PPPRSPSPEP TVVDTPSHAS QSARFYKHLD RGYNSCARTD
LYFMPLAGSK LAKKREEAIE KAKREAEQKA REEREREKEK EKERERERER EREAERAAKA
SSSAHEGRLS DPQLSGPGHM RPSFEPPPTT IAAVPPYIGP DTPALRTLSE YARPHVMSPT
NRNHPFYMPL NPTDPLLAYH MPGLYNVDPT IRERELRERE IREREIRERE LRERMKPGFE
VKPPELDPLH PATNPMEHFA RHSALTIPPT AGPHPFASFH PGLNPLERER LALAGPQLRP
EMSYPDRLAA ERIHAERMAS LTSDPLARLQ MFNVTPHHHQ HSHIHSHLHL HQQDPLHQGS
AGPVHPLVDP LTAGPHLARF PYPPGTLPNP LLGQPPHEHE MLRHPVFGTP YPRDLPGAIP
PPMSAAHQLQ AMHAQSAELQ RLAMEQQWLH GHPHMHGGHL PSQEDYYSRL KKEGDKQL
//