ID A0A671TPU6_SPAAU Unreviewed; 921 AA.
AC A0A671TPU6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE SubName: Full=AT-rich interactive domain 4A {ECO:0000313|Ensembl:ENSSAUP00010003984.1};
GN Name=arid4a {ECO:0000313|Ensembl:ENSSAUP00010003984.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010003984.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010003984.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSAUP00010003984.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSSAUP00010003984.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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DR AlphaFoldDB; A0A671TPU6; -.
DR Ensembl; ENSSAUT00010004303.1; ENSSAUP00010003984.1; ENSSAUG00010001622.1.
DR GeneTree; ENSGT00940000156159; -.
DR Proteomes; UP000472265; Chromosome 16.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:TreeGrafter.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR CDD; cd18641; CBD_RBP1_like; 1.
DR CDD; cd20390; Tudor_ARID4_rpt2; 1.
DR CDD; cd20459; Tudor_ARID4A_rpt1; 1.
DR FunFam; 2.30.30.140:FF:000012; AT-rich interactive domain-containing protein 4A; 1.
DR FunFam; 1.10.150.60:FF:000003; AT-rich interactive domain-containing protein 4B; 1.
DR FunFam; 2.30.30.140:FF:000009; AT-rich interactive domain-containing protein 4B; 1.
DR Gene3D; 2.30.30.140; -; 3.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR InterPro; IPR051232; ARID/SWI1_ChromRemod.
DR InterPro; IPR012603; ARID4A/B_PWWP.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR047473; CBD_RBP1-like.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR047472; Tudor_ARID4A_rpt1.
DR PANTHER; PTHR13964:SF27; HAT-TRICK, ISOFORM D; 1.
DR PANTHER; PTHR13964; RBP-RELATED; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF08169; RBB1NT; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51011; ARID; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 297..389
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT REGION 129..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..536
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..593
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..698
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..829
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..912
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 103427 MW; 88EE5FBB81D9639F CRC64;
MLLVCVLQAA DEPAYLTVGT DVSAKYRGAF CEAKIKTVKR LVKVKVTLKG ESTSQVVQDD
QVKGPLRVGS TVEVKTNEGL SSEAVISKLT DASLYTVVFD DGDEKTLRRT SLCLKGERHF
AESETLDQLP LTNPEHFGTP VIGKKSNRGG RRSSQAVADE ENESSSSEDE EEDRRRLNDE
LLGKVCSIEN EEEPSSWYLA LVVSPSCNDE LLVKKDQCLV RAFSDSKFDD DEEGDEEEEK
KKKKHMKEEV NVHMTAGVTD AAGRVRYLPV CVCVCVCVCV CVCVCVCVCQ PDEEPDPEER
DHFLQQLYKF MEDRGTPINK PPVLGYKDLN LFKLFRLVYH LGGCHKIESG TVWKQVYMDL
GIPVLNSAAS YNVKTAYRKY LYGFEEYCRS ASITFRTIHH NNPRPPTVPT NQNQTGPELK
EPSTPPLKVG TVDDKMEEAE SDSESEKEDM KERQLSPRVR HKRLFKLYST TSPNSETLAK
KQPSNRRMDD SEKGSEEEDE EDEDEDEEEV ERSEDEEDED SLTGTKVRVK YGRGKTQKIY
EAHIKKTDVD NGEQFYLVHY YGWNVRYDEW VKADRIIWPV EKGTKKRQRK KVKKERDKDE
EKTPKPTGVK RGRPQIRTTP TGSAGRSVSK TPSNEGRSNG RRTETPSNMA NGDMLKAEEW
PRPAEAMQRE VSEERPTGVA SKEPEVLAGT TPTTVEAPGP APTEEAEPQI GPEALVCHEV
DLDDPDDKEK PSPTTSPEHL LLMMREQQPA PPPLPNLLHA SLPSPHLPQP QVRPFLPAAA
PSSAPCLEEL HPARITCVTF DPSGQKRVMD CNSSPTAKKQ KRNQKRPHTP GKVEKNGADE
LDSMSSTERI SFLQEKLQEI RKYYMTLKSE VASIDRRRKR LKKKEREVSN TTASTSSGSS
DTAMSPSSAS PTQNTVAVEC R
//
