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GTE6_ARATH
ID   GTE6_ARATH              Reviewed;         369 AA.
AC   Q9FT54;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Transcription factor GTE6;
DE   AltName: Full=Bromodomain-containing protein GTE6;
DE   AltName: Full=Protein GENERAL TRANSCRIPTION FACTOR GROUP E6;
DE   AltName: Full=Protein GLOBAL TRANSCRIPTION FACTOR GROUP E6;
GN   Name=GTE6; OrderedLocusNames=At3g52280; ORFNames=T25B15.50;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   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   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16166385; DOI=10.1101/gad.352005;
RA   Chua Y.L., Channeliere S., Mott E., Gray J.C.;
RT   "The bromodomain protein GTE6 controls leaf development in Arabidopsis by
RT   histone acetylation at ASYMMETRIC LEAVES1.";
RL   Genes Dev. 19:2245-2254(2005).
CC   -!- FUNCTION: Regulates differences in leaf patterning between juvenile and
CC       mature leaves by controlling differences in the development of
CC       primordia produced during juvenile and mature phases. Acts by
CC       activating transcription of the myb-domain protein AS1, a gene involved
CC       in leaf-axis specification. Associates with the promoter and the start
CC       of the transcribed region of AS1 and up-regulates expression of AS1
CC       through acetylation of histones H3 and H4.
CC       {ECO:0000269|PubMed:16166385}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16166385}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9FT54-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in flowers. Weakly expressed
CC       in roots, leaves and siliques; and undetectable in 5-day-old seedlings.
CC       In the basal rosette leaves of 21-day-old plants, it is more abundant
CC       in leaves 6 and 7, which possess narrow elliptical laminae, than in
CC       leaves 1-4, which have round laminae, suggesting a possible correlation
CC       between its expression and the formation of elliptical leaf laminae in
CC       mature leaves. {ECO:0000269|PubMed:16166385}.
CC   -!- DOMAIN: The NET domain could serve as an interface to localize
CC       different proteins or complexes to chromatin.
CC   -!- DISRUPTION PHENOTYPE: Disrupted formation of elliptical leaf laminae in
CC       mature leaves. {ECO:0000269|PubMed:16166385}.
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DR   EMBL; AL132972; CAC07919.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78925.1; -; Genomic_DNA.
DR   PIR; T46098; T46098.
DR   RefSeq; NP_190796.1; NM_115088.2. [Q9FT54-1]
DR   AlphaFoldDB; Q9FT54; -.
DR   SMR; Q9FT54; -.
DR   STRING; 3702.AT3G52280.2; -.
DR   PRIDE; Q9FT54; -.
DR   ProteomicsDB; 247231; -. [Q9FT54-1]
DR   EnsemblPlants; AT3G52280.1; AT3G52280.1; AT3G52280. [Q9FT54-1]
DR   GeneID; 824393; -.
DR   Gramene; AT3G52280.1; AT3G52280.1; AT3G52280. [Q9FT54-1]
DR   KEGG; ath:AT3G52280; -.
DR   Araport; AT3G52280; -.
DR   eggNOG; KOG1474; Eukaryota.
DR   HOGENOM; CLU_063149_0_0_1; -.
DR   InParanoid; Q9FT54; -.
DR   OMA; MEPVMAS; -.
DR   PhylomeDB; Q9FT54; -.
DR   PRO; PR:Q9FT54; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9FT54; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; IPR017413; GTE1.
DR   InterPro; IPR027353; NET_dom.
DR   InterPro; IPR038336; NET_sf.
DR   Pfam; PF17035; BET; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   PIRSF; PIRSF038154; Transcription_factor_GTE6; 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   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Bromodomain; Chromatin regulator;
KW   Coiled coil; Developmental protein; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..369
FT                   /note="Transcription factor GTE6"
FT                   /id="PRO_0000211204"
FT   DOMAIN          106..181
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DOMAIN          250..331
FT                   /note="NET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT   REGION          329..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          201..263
FT                   /evidence="ECO:0000255"
FT   MOTIF           351..368
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        329..362
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  42393 MW;  006F48BAD3216C58 CRC64;
     MADSVPGHVA GGGLQGFSVD AECIKQRVDE VLQWVDSLEH KLKEVEEFYS SIGVSNSGSI
     GKDTEKGRHV VGIRKIQQEA ARREAVAAKR MQDLMRQFGT IFRQITQHKC AWPFMHPVNV
     EGLGLHDYFE VIDKPMDFST IKNQMEAKDG TGYKHVMQIY ADMRLVFENA MNYNEETSDV
     YSMAKKLLEK FEEKWAHFLP KVQEEEKIRE EEEKQAAKEA LLAKEASHIK TTRELGNEIC
     HANDELEKLM RKVVERCRKI TIEEKRNIGL ALLKLSPDDL QKVLGIVAQA NPSFQPRAEE
     VSIEMDILDE PTLWRLKFFV KDALDNAMKK KKEEETKTRE LSGAQKKEVS KKRNATTKLA
     ERKTKRSRI
 
 
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