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Database: UniProt
Entry: G3SR00_LOXAF
LinkDB: G3SR00_LOXAF
Original site: G3SR00_LOXAF 
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
//
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