ID A0A3B3YK11_9TELE Unreviewed; 1168 AA.
AC A0A3B3YK11;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Arginine-glutamic acid dipeptide (RE) repeats b {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000027714.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000027714.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_014837630.1; XM_014982144.1.
DR AlphaFoldDB; A0A3B3YK11; -.
DR STRING; 48701.ENSPMEP00000027714; -.
DR Ensembl; ENSPMET00000017187.1; ENSPMEP00000027714.1; ENSPMEG00000012355.1.
DR GeneID; 106914927; -.
DR CTD; 799473; -.
DR OrthoDB; 3349425at2759; -.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion 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; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR002951; Atrophin-like.
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 InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR13859:SF39; ARGININE-GLUTAMIC ACID DIPEPTIDE REPEATS PROTEIN ISOFORM X1; 1.
DR PANTHER; PTHR13859; ATROPHIN-RELATED; 1.
DR Pfam; PF03154; Atrophin-1; 2.
DR Pfam; PF01448; ELM2; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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; PS51156; ELM2; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00094}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00094};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00094}.
FT DOMAIN 16..119
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 123..175
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 228..283
FT /note="GATA-type"
FT /evidence="ECO:0000259|PROSITE:PS50114"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 127446 MW; 5935F1C6B1461066 CRC64;
MDDLFSPRRS LNSTQGEIRV GPSHQAKLPE LQPRPAPSAQ TQTDNEELMW TPGVNDCDLL
MYLRAARSMA AFAGMCDGGS TEDGCLAASR DDTTLNALNM LHASHYDAAK ALQRLVKRPL
PKLIEKSWSE DDVKRFIKGL RQYGKNFFRI RKDFLPSKKT GELITFYYHW KKTPEAAGTR
AYRQQRRQPS SRKAKTRSAA ANVNPPSRNY SVEASSASED DVDSEDSEQE AKSCSHCGTT
TSKDWHQVGR DNSLLCTTCR TYENKHGCLP PASKSGNASF MFKPVKVEEE LNSKHGMRTR
QSRAPQLTSL RSGLRRFTGS PNTEDSQSGN QTGGISSSLR SCADHKNDST KKINKKIKEE
VTVPKTAKRV RESPALESDE PEKMTPKRPK TQDPRGGSRS EGEAEEESSS ESRSAQDDGS
DTKDIDQDNR SSSPSIPSPQ QGNESDSDSS AQPSGAPAEA GAATPTDVPV LQAVPSQDPP
IPPQPSQSLT SADPAQSPPS SSPDPPQGGA AQSPATASSG CRAMPVSGPR PQPAALGLDT
PLAPAPHFSP ALGPTQPNGS PPHTPPRSVP FFRDAQLPHP PQVKPPPTTP IPPSHKQLPH
QSAAPFPQMP SNLPPPPALK PLNSLPNQHP PGAPPPPLQL MPHPLPPHSA PSQLPVSSQV
QSHPGKSGAS SLPAAPAPLP LTSSAAGPVP TLQPSFPPHP PRPSPNSAAG GSQVQIKEEP
LDEVEEPESP PSPPRSPSPE PTVVNMASHA SQSARFIKHL DRGYNSCART DLFFTPLSSS
KLAKKREEAV ERMRREAELS ARQEREREKD RERERETDRN SRASSSSHDS RLSEVQMTAQ
IHGRPSFDQP PTTVAAVPPY IGPDTPAMRS LNDYARPHVM SPSNRNHPFY VSLSPGDPLL
AYHMPGLYST DPGLRERELR NFRERELRER MKPGFEVKPP DLETLHPSAN HLEHFARHGA
LALPHIPGPS HPFAPFHPGL SHLERERLAL AGPQMRPELS YAERLTAERL HAERMASVAT
DPAARLQMLN VTPHHHQHSH IHSHLHLHQQ DPLGQGSSPH PLVDPLAAGP RLARFPFPAG
PIPNPLLADL PHDHEMLRHP LFGAAYPREL QGPIPHMSAS HQLQAMHAQS AELQRMAMEQ
QWHHLHGGPL PSQEDYYSRL KKEGDKPS
//
