ID A0A673X6S8_SALTR Unreviewed; 1039 AA.
AC A0A673X6S8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Arginine-glutamic acid dipeptide repeats protein-like {ECO:0000313|Ensembl:ENSSTUP00000019894.1};
GN Name=LOC115208057 {ECO:0000313|Ensembl:ENSSTUP00000019894.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000019894.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000019894.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A673X6S8; -.
DR Ensembl; ENSSTUT00000020901.1; ENSSTUP00000019894.1; ENSSTUG00000008828.1.
DR GeneTree; ENSGT00940000153615; -.
DR InParanoid; A0A673X6S8; -.
DR OMA; NEHNARE; -.
DR Proteomes; UP000472277; 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 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; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 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; PS51293; SANT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472277};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
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 REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..620
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 112574 MW; E49BD8DEADA90CB0 CRC64;
MDDLFSPRRS LNSTQGEIRV GSSHQAKLPE LQPRPVFGVQ TQTENEELVW MPGVNDCDLL
MYLRAARSMA AFAGMCDGGS TEDGCLAASR DDTTLNALNM LHASRYDAAK ALQRLVKKPV
PKLIEKCWSE DDVKRFIKGL RQYGKHFFRI RKELLPNKKT GELITFYYHW KKTPEAAGTR
PYRQHRRQPS SRKAKTRAAL ATVNTPSRAQ SLDVSSASED DLDSEDSEQG TCGHCATTTS
KDWQHGGRDN ILLCTTCRTF YNKHGRLPPG PKPADPPFMF KPVKEEEEGN GKHGMRTRRS
RAPLSSLRSG HKRRTGSPTS EDQQSSSHPS PAPSGASSTS NTSRSSCSDK TDSTKKPGKK
IKEEVPLPKS TKRSRESAAQ DPEEPERTAT KRTKTQQGEQ VECRSEGDGE AEAEGGEVEE
ECCSDSRSAQ DDGSSDTKDI DQDNRSSSPS IPSPHQGNEG NESDSDSSAQ QPQGAHQAAV
ETISAPAAVT QTAPTVPPVQ AAVSTTFLPP QGTSPSAEPG QVQAQAPPSS EPPQPAQAGQ
SAGYESGPPH SQPPPHSSHP ISGPSPLPPP LGQALHPPSP VFQGPLPPPG SLPPTLPLHG
APPQGPRPQR PPPHIPRDPP LSQAIPLTSG PQIKPPPTTP IPPSHKQQPP HLSSAPPFPQ
MPSNLPPPPA LKPLNSLPNQ HPPGAPPPPL QLMPQSLPMQ QGLSPQPPVL TQLQNLSGRG
SHSHSTLPSS GPSALHPVPS ASAPSNMGPV PGLQPSFSSM PLRPSPGNPI GMGGSHVQIK
EEPLDECEPE SPPPPPRSPS PEPSVVDIAS HASQSARFIK HLDRGYNSCS RTDLFFTPLA
SSKLAKKREE AVERSKRENE HNAREREREK DRERERERER ERQEEKNAVS YMLWSSLYSL
FVFFDINKWW PIQKGNPSVV ASANIAQVGF ALLFTCGLFK STSSTHASSM SGARMRWCLL
LPCWCLLLPC CYYSLCLLFS DPPPSLRLSD FCVCSSKGFD GAYCAHCSGT ELHEGAEPIV
SFLKLTCLTI SYLSNDIIT
//
