ARI3A_XENLA
ID ARI3A_XENLA Reviewed; 539 AA.
AC Q6GQD7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=AT-rich interactive domain-containing protein 3A;
DE Short=ARID domain-containing protein 3A;
DE AltName: Full=Bright homolog;
DE AltName: Full=Dead ringer-like protein 1;
GN Name=arid3a; Synonyms=dril1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=15680369; DOI=10.1016/j.ydbio.2004.11.017;
RA Callery E.M., Smith J.C., Thomsen G.H.;
RT "The ARID domain protein dril1 is necessary for TGF(beta) signaling in
RT Xenopus embryos.";
RL Dev. Biol. 278:542-559(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor required for smad1 and smad2-mediated
CC responses to TGFbeta during mesoderm induction.
CC {ECO:0000269|PubMed:15680369}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
CC Cytoplasm {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm.
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during early embryogenesis
CC and at highest levels between NF19 and NF28. Expressed in the
CC involuting mesoderm of the gastrula. Expressed in non-neural ectoderm
CC of the early neurula, and excluded from neural plate.
CC {ECO:0000269|PubMed:15680369}.
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DR EMBL; AY787401; AAW78333.1; -; mRNA.
DR EMBL; BC072808; AAH72808.1; -; mRNA.
DR RefSeq; NP_001085467.1; NM_001091998.1.
DR RefSeq; XP_018092210.1; XM_018236721.1.
DR RefSeq; XP_018092218.1; XM_018236729.1.
DR RefSeq; XP_018092229.1; XM_018236740.1.
DR RefSeq; XP_018092236.1; XM_018236747.1.
DR RefSeq; XP_018092242.1; XM_018236753.1.
DR RefSeq; XP_018092248.1; XM_018236759.1.
DR RefSeq; XP_018092257.1; XM_018236768.1.
DR RefSeq; XP_018092264.1; XM_018236775.1.
DR AlphaFoldDB; Q6GQD7; -.
DR SMR; Q6GQD7; -.
DR BioGRID; 102056; 1.
DR IntAct; Q6GQD7; 1.
DR DNASU; 443893; -.
DR GeneID; 443893; -.
DR KEGG; xla:443893; -.
DR CTD; 443893; -.
DR Xenbase; XB-GENE-945270; arid3a.S.
DR OMA; GHIHKIK; -.
DR OrthoDB; 858876at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 443893; Expressed in blastula and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR045147; ARI3A/B/C.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR023334; REKLES_domain.
DR PANTHER; PTHR15348; PTHR15348; 1.
DR Pfam; PF01388; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51486; REKLES; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..539
FT /note="AT-rich interactive domain-containing protein 3A"
FT /id="PRO_0000295160"
FT DOMAIN 209..301
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 404..499
FT /note="REKLES"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00819"
FT REGION 1..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..448
FT /note="Important for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 450..471
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 495..502
FT /note="Important for cytoplasmic localization"
FT /evidence="ECO:0000250"
FT REGION 497..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 58570 MW; A34C147C73CB8106 CRC64;
MKLQAVMETL QRQQRARLQQ ELEARQLQQD SSEGRTPPSA GYPGNGSDEA EPEALKIQRA
QAAALAAMRA AAAGLSQQPS PAASEEEDGE SMASDEEDEK ERDGESERYQ DMASEEEDLK
GKWDEDDFED EGEDEYEDME EGIGVNEAGR VGKGSTLPPK HSSQQAFPSQ RSQGAERAGL
PLSGHPQLQD HGDWTYEEQF KQLYELDGDP KRKEFLDDLF SFMQKRGTPV NRIPIMAKQV
LDLYMLYVLV TEKGGLVEVI NKKLWREITK GLNLPTSITS AAFTLRTQYM KYLYPYECEK
RGLSNPNELQ AAIDSNRREG RRQSFGGTLF TYSPSGAPSM LSSPKLQVSG LSLGGAALNG
STLSSMQKIK KEEDSPISLA MPPRIPVTLA GHSMVAAQVA AQAAALEQLR EKLESGEPPE
KKMALGSEEQ QRIIQRTIQH NLLAMTAQLP MNIRINSQAE GRQDSAVNLT TNGTNSISMS
VELNGIVYTG VLFAQPPTSA SGTSKGSSNR TGSIGGGSSN SQAAPPSTPS APNSNNPSP
