GTE3_ARATH
ID GTE3_ARATH Reviewed; 461 AA.
AC Q9S7T1; Q0WSA6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Transcription factor GTE3, chloroplastic;
DE AltName: Full=Bromodomain-containing protein GTE3;
DE AltName: Full=Protein GLOBAL TRANSCRIPTION FACTOR GROUP E3;
DE Flags: Precursor;
GN Name=GTE3; OrderedLocusNames=At1g73150; ORFNames=F3N23.35, T18K17.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
RN [6]
RP FUNCTION, INTERACTION WITH SIZ1, SUMOYLATION, AND ACETYLATED HISTONE
RP H3-BINDING.
RX PubMed=18502747; DOI=10.1074/jbc.m708176200;
RA Garcia-Dominguez M., March-Diaz R., Reyes J.C.;
RT "The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain
RT GTE proteins.";
RL J. Biol. Chem. 283:21469-21477(2008).
CC -!- FUNCTION: Probable transcription factor that binds to acetylated
CC histone H3. {ECO:0000269|PubMed:18502747}.
CC -!- SUBUNIT: Interacts with SIZ1 (via PHD domain).
CC {ECO:0000269|PubMed:18502747}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DOMAIN: The NET domain could serve as an interface to localize
CC different proteins or complexes to chromatin.
CC -!- PTM: Sumoylated by SIZ1. Sumoylation reduces capacity to bind to
CC acetylated histone H3. {ECO:0000269|PubMed:18502747}.
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DR EMBL; AC008017; AAD55662.1; -; Genomic_DNA.
DR EMBL; AC010556; AAG52122.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35419.1; -; Genomic_DNA.
DR EMBL; BT020256; AAV84477.1; -; mRNA.
DR EMBL; AK228031; BAE99992.1; -; mRNA.
DR PIR; D96757; D96757.
DR RefSeq; NP_177458.1; NM_105973.4.
DR AlphaFoldDB; Q9S7T1; -.
DR SMR; Q9S7T1; -.
DR BioGRID; 28865; 2.
DR STRING; 3702.AT1G73150.1; -.
DR iPTMnet; Q9S7T1; -.
DR PaxDb; Q9S7T1; -.
DR PRIDE; Q9S7T1; -.
DR ProteomicsDB; 230168; -.
DR EnsemblPlants; AT1G73150.1; AT1G73150.1; AT1G73150.
DR GeneID; 843646; -.
DR Gramene; AT1G73150.1; AT1G73150.1; AT1G73150.
DR KEGG; ath:AT1G73150; -.
DR Araport; AT1G73150; -.
DR TAIR; locus:2032692; AT1G73150.
DR eggNOG; KOG1474; Eukaryota.
DR HOGENOM; CLU_009580_1_0_1; -.
DR InParanoid; Q9S7T1; -.
DR OMA; KVTELGH; -.
DR OrthoDB; 904818at2759; -.
DR PhylomeDB; Q9S7T1; -.
DR PRO; PR:Q9S7T1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7T1; baseline and differential.
DR Genevisible; Q9S7T1; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd05506; Bromo_plant1; 1.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037377; GTE_bromo.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Chloroplast; Chromatin regulator; Plastid; Reference proteome;
KW Transcription; Transcription regulation; Transit peptide; Ubl conjugation.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..461
FT /note="Transcription factor GTE3, chloroplastic"
FT /id="PRO_0000397040"
FT DOMAIN 131..203
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 298..379
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 164
FT /note="G -> E (in Ref. 4; BAE99992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 50812 MW; 4E0786F78DCAC6B1 CRC64;
MASGPIAGGG VSKTKHKWSD SGNKSQKRSK PTVANSNSLG LEDNHQMMKI SLSSISKLEV
RNLKRKLQAE LEEVRSLIKR LEPQGNNFAP VPNKKLKTAN GGKKGGVHGA AADKGTVQIL
KSCNNLLTKL MKHKSGWIFN TPVDVVTLGL HDYHNIIKEP MDLGTVKTRL SKSLYKSPLE
FAEDVRLTFN NAMLYNPVGH DVYHMAEILL NLFEEKWVPL ETQYELLIRK QQPVRDIDFH
APVSTNTHNV EALPLPAPTP SLSPPPPPKV VENRTLERAE SMTNPVKPAV LPVVPEKLVE
EASANRDLTF DEKRQLSEDL QDLPYDKLEA VVQIIKKRTP ELSQQDDEIE LDIDSLDLET
LWELFRFVTE YKESLSKKKE EQGLDSERDA ESFHNSVHES NTLVTGLESS KVTELGHVAS
TVRQEVNVGG SSSSNSSSSG SGSGSSGSDS DSSGHESDTG N
