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Database: UniProt
Entry: A0A3P9PLG1_POERE
LinkDB: A0A3P9PLG1_POERE
Original site: A0A3P9PLG1_POERE 
ID   A0A3P9PLG1_POERE        Unreviewed;      1516 AA.
AC   A0A3P9PLG1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Arginine-glutamic acid dipeptide repeats {ECO:0000313|Ensembl:ENSPREP00000022558.1};
GN   Name=RERE {ECO:0000313|Ensembl:ENSPREP00000022558.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000022558.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000022558.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000022558.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   STRING; 8081.ENSPREP00000022558; -.
DR   Ensembl; ENSPRET00000022795.1; ENSPREP00000022558.1; ENSPREG00000015213.1.
DR   GeneTree; ENSGT00940000153615; -.
DR   OMA; VMYLRAA; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000015213; Expressed in caudal fin and 1 other cell type or tissue.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd11661; SANT_MTA3_like; 1.
DR   CDD; cd00202; ZnF_GATA; 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; 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; ATROPHIN-RELATED; 1.
DR   PANTHER; PTHR13859:SF11; GRUNGE, ISOFORM J; 1.
DR   Pfam; PF03154; Atrophin-1; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00320; GATA; 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:UP000242638};
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          115..266
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   DOMAIN          228..339
FT                   /note="ELM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51156"
FT   DOMAIN          343..395
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..1079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1490..1516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..808
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..910
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..976
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1006
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1027
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1516 AA;  167660 MW;  063652B4779BF581 CRC64;
     MTADKEKERE KERDRDRDRD RDKREAGKSR RQDGDRGESE SSRPRRSCTL EGGAKNYAES
     EHSEDEDNDN GSTGGGSGTA EEAGKKGKKK MPKKKSRYER TENGEITSFI TEDDVVYRPG
     DCVYIESRRP NTPYFICSIQ DFNFLCLLLT PSLSLSVFQS KRDHLLMNVK WYYRQSEVPD
     SVYQHLVQDR NNENDSGREL VITDPVVRSR ELFISDYVDT YHAAALRGKC NISHFSDIFA
     AREFKAKLPE LQPFPSPGGQ AVTENEELVW MPGVNDCDLL MYLRAARSMA AFAGMCDGGS
     TEDGCLAASR DDTTLNALNT LHESSYDAGK ALQRLVKKPV PKLIEKCWSE DEVKRFIKGL
     RQFGKNFFRI RKELLPNKET GELITFYYYW KKTPEAASCR AHRRHRRQPV FRRIKTRTAS
     TPVNTPSRPP SSEFLDLSSA SEDDFDSEDS EQELKGYACR HCFTTTSKDW HHGGRENILL
     CTDCRIHFKK YGELPPIEKP VDPPPFMFKP VKEEEDGLGG KHSMRTRRNR GSMSTLRSGR
     KKQTVSPDGR ASPTNEDLRS SGRTSPSAAS TDSTDSKTDS MKKTSKKIKE EAPSPIKSAK
     RQREKGASDT EEPERASAKK SKTQELTRPD SPSECDGEGE GEGESSDGRS INEELSSDPK
     DIDQDNRSSS PSIPSPRDNE SDSDSSAQQQ QLLQSQHPPV IQCQPGSSVA SSAPVPPTTS
     ASSLPPQVAP TAASTSLPPQ PLPQTSPMSL IQAGASLHPQ RLPSPHSPLT QAPPPGPPPS
     LPSPHHGPIP PMPHPLQPGP PLLPHPHAMT PQGFPVAASQ VPPLPISGQS QQRSHSPPPQ
     PQPSSQSGGQ PPREQPLPPA PMPMPHIKPP PTTPIPQMPT PQSHKHPPHG SVPPFPQMPS
     NLPPPPALKP LSSLSNHHPP SAHPPPLQLM SGGQQLQPPP AQPPVLTQSQ SLPPSASHQP
     PPPPPLPPPA AASHPSGAPQ QPPFSSHPFS TVLPPSGPPP SSSNSMPGLQ PPSSSSAPSS
     SISMPLPASV SCAPPAQVVP PIHIKEEPPD ESEEPESPPP PQRSPSPEPT VVNTPSHASQ
     SARFYKYLDR GYNSCARTDF YFTPLASSKL AKKREEALEK AKREAEQKVR EEKEREREKE
     KERERERERE KEVERAAKAS SSAHESRMGE PQMAGPTHMR PPYDGPPTTI AAVPPYIGPD
     TPALRTLSEY ARPHVMSPTN RNHPFFVSLN PADQLLAYHM PSLYNADPAM RERELREREM
     REREIREREL RERMKPGFEV KPPEMDSLHP STNPMEHFAR HGALTLPPMA GPHPFASFHP
     GLNPLERERL ALPGPQLRPD MTYPERLAAE RLHAERMATV ANDPIARLQM FNVTPHHHQH
     SHIHSHLHLH QQDPLHQGSG AHPLAVDPLA AGPHLARFPY PPGAIPNPLL GQPPHEHEML
     RHPVFGAPYP RDLPGGLPPQ MSAAHQLQAM HAQSAELQRL AMEQQWLHGH HHMHGGPLPG
     QEDYYSRLKK ESDKQL
//
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