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TRO_ARATH
ID   TRO_ARATH               Reviewed;         509 AA.
AC   Q9C8J7;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Protein TRAUCO {ECO:0000303|PubMed:20118203};
DE   AltName: Full=Protein ASH2 RELATIVE {ECO:0000303|PubMed:21423667};
DE            Short=AtASH2 {ECO:0000303|PubMed:23284292};
DE            Short=AtASH2R {ECO:0000303|PubMed:21423667};
GN   Name=TRO {ECO:0000303|PubMed:20118203};
GN   Synonyms=ASH2R {ECO:0000303|PubMed:21423667};
GN   OrderedLocusNames=At1g51450 {ECO:0000312|Araport:AT1G51450};
GN   ORFNames=F5D21.18 {ECO:0000312|EMBL:AAG52633.1};
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 {ECO:0000312|Proteomes:UP000006548};
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., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) 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   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=20118203; DOI=10.1093/jxb/erp396;
RA   Aquea F., Johnston A.J., Canon P., Grossniklaus U., Arce-Johnson P.;
RT   "TRAUCO, a Trithorax-group gene homologue, is required for early
RT   embryogenesis in Arabidopsis thaliana.";
RL   J. Exp. Bot. 61:1215-1224(2010).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH RBL,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=21423667; DOI=10.1371/journal.pgen.1001330;
RA   Jiang D., Kong N.C., Gu X., Li Z., He Y.;
RT   "Arabidopsis COMPASS-like complexes mediate histone H3 lysine-4
RT   trimethylation to control floral transition and plant development.";
RL   PLoS Genet. 7:E1001330-E1001330(2011).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=23284292; DOI=10.1371/journal.pgen.1003111;
RA   Ding Y., Ndamukong I., Xu Z., Lapko H., Fromm M., Avramova Z.;
RT   "ATX1-generated H3K4me3 is required for efficient elongation of
RT   transcription, not initiation, at ATX1-regulated genes.";
RL   PLoS Genet. 8:E1003111-E1003111(2012).
CC   -!- FUNCTION: Trithorax-group gene homolog required for early embryogenesis
CC       (PubMed:20118203, PubMed:21423667). Required for the expression of FLC
CC       and FLC homologs and represses flowering (PubMed:21423667). Required
CC       for proper leaf growth and development (PubMed:21423667). Part of
CC       COMPASS-like complexes responsible for H3K4 trimethylation, but not for
CC       di- or mono-methylation of histone H3 'Lys-4' (PubMed:21423667). Binds
CC       to target loci chromatin, increasing H3K4 trimethylation and causing
CC       activation of the gene (PubMed:21423667). Involved in the transition
CC       from transcription initiation to transcription elongation
CC       (PubMed:23284292). {ECO:0000269|PubMed:20118203,
CC       ECO:0000269|PubMed:21423667, ECO:0000269|PubMed:23284292}.
CC   -!- SUBUNIT: Part of a complex composed of TRO, RBL and WDR5A. Interacts
CC       with RBL, but not with WDR5A or WDR5B. This complex is formed during
CC       both vegetative and reproductive development.
CC       {ECO:0000269|PubMed:21423667}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20118203,
CC       ECO:0000269|PubMed:21423667}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in pollen and seeds.
CC       Expressed in the embryo and the suspensor cells. Detected in
CC       cotyledons, roots, leaf hydathodes, sepals, anthers and pollen grains
CC       (PubMed:20118203). Strongly expressed in root tips, shoot apices,
CC       vascular tissues, developing embryos and endosperms (PubMed:21423667).
CC       {ECO:0000269|PubMed:20118203, ECO:0000269|PubMed:21423667}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryo development.
CC       {ECO:0000269|PubMed:20118203}.
CC   -!- DISRUPTION PHENOTYPE: Embryo lethality when homozygous
CC       (PubMed:20118203, PubMed:21423667). Eearly flowering (PubMed:23284292).
CC       Slightly lower ATX1 occupancy at the 5'-end regions of the target genes
CC       (PubMed:23284292). Decreased TATA-binding protein (TBP) levels lower
CC       Ser5P Pol II levels near the transcription start sites (TSSs) of target
CC       genes and of Pol II at the genes 3'-ends thus affecting the transition
CC       from transcription initiation to transcription elongation
CC       (PubMed:23284292). Significantly reduced trimethylated 'Lys-4' of
CC       histone H3 (H3K4me3) levels at the 5'-ends of WRKY70 and LTP7 genes
CC       leading to reduced transcript accumulation (PubMed:23284292).
CC       {ECO:0000269|PubMed:20118203, ECO:0000269|PubMed:21423667,
CC       ECO:0000269|PubMed:23284292}.
CC   -!- MISCELLANEOUS: Named TRAUCO (TRO) in honor of the fertility mythology
CC       from the Chiloe island in southern Chile.
CC       {ECO:0000303|PubMed:20118203}.
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DR   EMBL; AC024261; AAG52633.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32669.1; -; Genomic_DNA.
DR   EMBL; BT023430; AAY56421.1; -; mRNA.
DR   EMBL; AK229176; BAF01046.1; -; mRNA.
DR   PIR; G96552; G96552.
DR   RefSeq; NP_175556.1; NM_104023.3.
DR   AlphaFoldDB; Q9C8J7; -.
DR   SMR; Q9C8J7; -.
DR   STRING; 3702.AT1G51450.1; -.
DR   iPTMnet; Q9C8J7; -.
DR   PaxDb; Q9C8J7; -.
DR   PRIDE; Q9C8J7; -.
DR   ProteomicsDB; 232375; -.
DR   EnsemblPlants; AT1G51450.1; AT1G51450.1; AT1G51450.
DR   GeneID; 841570; -.
DR   Gramene; AT1G51450.1; AT1G51450.1; AT1G51450.
DR   KEGG; ath:AT1G51450; -.
DR   Araport; AT1G51450; -.
DR   TAIR; locus:2033954; AT1G51450.
DR   eggNOG; KOG2626; Eukaryota.
DR   HOGENOM; CLU_041214_0_0_1; -.
DR   InParanoid; Q9C8J7; -.
DR   OMA; QRYICAP; -.
DR   OrthoDB; 444178at2759; -.
DR   PhylomeDB; Q9C8J7; -.
DR   PRO; PR:Q9C8J7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C8J7; baseline and differential.
DR   Genevisible; Q9C8J7; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IPI:TAIR.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:TAIR.
DR   GO; GO:0060776; P:simple leaf morphogenesis; IMP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR037353; ASH2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR10598; PTHR10598; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..509
FT                   /note="Protein TRAUCO"
FT                   /id="PRO_0000431784"
FT   DOMAIN          253..472
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  55507 MW;  97D912165102E724 CRC64;
     MESLQSNSKI EEAEQNPKIE EAQVSVSLPE EPTGVLLPSE LVDDSAPPES SDAVEESIET
     ASEAEVSISL LEGTTTGTAL LPSEENDLAP LESSGIIEEP IDTDLEKLDV VAMDVDQPGS
     DLKIESDSFS EEAPTTSSSD NPKSPKLDSV ANQNGSAMEE DEGDEEQDDP PHKKLKQLDC
     LTSVAVKEEE EPEQVLPSEA MVVEEAATLV ASAAKKSKSK KKNNNVWVTK STRKGKKKSK
     ANTPNPAAVE DKVLITPVPR FPDKGDDTPD LEICLSKVYK AEKVEISEDR LTAGSSKGYR
     MVRATRGVVE GAWYFEIKVL SLGETGHTRL GWSTDKGDLQ APVGYDGNSF GFRDIDGCKI
     HKALRETYAE EGYKEGDVIG FYINLPDGES FAPKPPHYVF YKGQRYICAP DAKEEPPKVV
     PGSEISFFKN GVCQGAAFTD IVGGRYYPAA SMYTLPDQSN CLVKFNFGPS FEFFPEDFGG
     RATPRPMWEV PYHGFNGRLE TNGSEDMKS
 
 
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