TRX1_ORYSJ
ID TRX1_ORYSJ Reviewed; 1022 AA.
AC Q6K431; Q6K430;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histone-lysine N-methyltransferase TRX1 {ECO:0000305};
DE Short=OsTrx1 {ECO:0000303|PubMed:24420930};
DE EC=2.1.1.364 {ECO:0000269|PubMed:24420930};
DE AltName: Full=Protein SET DOMAIN GROUP 723 {ECO:0000305};
DE AltName: Full=SET family protein 33 {ECO:0000305};
DE Short=OsSET33 {ECO:0000303|PubMed:23762371};
GN Name=TRX1 {ECO:0000303|PubMed:24420930};
GN Synonyms=SDG723 {ECO:0000305}, SET {ECO:0000303|PubMed:23762371};
GN OrderedLocusNames=Os09g0134500 {ECO:0000312|EMBL:BAF24549.1},
GN LOC_Os09g04890 {ECO:0000305};
GN ORFNames=P0406E03.49-1 {ECO:0000312|EMBL:BAD22318.1},
GN P0406E03.49-2 {ECO:0000312|EMBL:BAD22319.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23762371; DOI=10.1371/journal.pone.0065426;
RA Lu Z., Huang X., Ouyang Y., Yao J.;
RT "Genome-wide identification, phylogenetic and co-expression analysis of
RT OsSET gene family in rice.";
RL PLoS ONE 8:E65426-E65426(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EHD3, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24420930; DOI=10.1104/pp.113.228049;
RA Choi S.C., Lee S., Kim S.R., Lee Y.S., Liu C., Cao X., An G.;
RT "Trithorax group protein Oryza sativa Trithorax1 controls flowering time in
RT rice via interaction with early heading date3.";
RL Plant Physiol. 164:1326-1337(2014).
CC -!- FUNCTION: Possesses histone H3 methyltransferase activity in vitro
CC (PubMed:24420930). Methylates 'Lys-4' of histone H3. H3 'Lys-4'
CC methylation represents a specific tag for epigenetic transcriptional
CC activation. Functions as a receptor for the lipid messenger
CC phosphatidylinositol 5-phosphate (PI5P), which regulates negatively its
CC transcriptional activation activity (By similarity). Involved in the
CC regulation of flowering time and floral induction under long day (LD)
CC conditions. Acts as an activator of flowering under LD conditions. May
CC function through binding to EHD3, a repressor of GHD7
CC (PubMed:24420930). {ECO:0000250|UniProtKB:Q9C5X4,
CC ECO:0000269|PubMed:24420930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000269|PubMed:24420930};
CC -!- SUBUNIT: Interacts with EHD3. {ECO:0000269|PubMed:24420930}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24420930}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6K431-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6K431-2; Sequence=VSP_058520, VSP_058521;
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades and panicles.
CC {ECO:0000269|PubMed:24420930}.
CC -!- DISRUPTION PHENOTYPE: Late-flowering phenotype under long day (LD)
CC conditions. {ECO:0000269|PubMed:24420930}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AP005583; BAD22318.1; -; Genomic_DNA.
DR EMBL; AP005583; BAD22319.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24549.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT06966.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT06967.1; -; Genomic_DNA.
DR EMBL; AK065095; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074022; BAG93767.1; -; mRNA.
DR RefSeq; XP_015612383.1; XM_015756897.1. [Q6K431-1]
DR AlphaFoldDB; Q6K431; -.
DR SMR; Q6K431; -.
DR STRING; 4530.OS09T0134500-02; -.
DR PaxDb; Q6K431; -.
DR PRIDE; Q6K431; -.
DR EnsemblPlants; Os09t0134500-01; Os09t0134500-01; Os09g0134500. [Q6K431-2]
DR EnsemblPlants; Os09t0134500-02; Os09t0134500-02; Os09g0134500. [Q6K431-1]
DR GeneID; 4346464; -.
DR Gramene; Os09t0134500-01; Os09t0134500-01; Os09g0134500. [Q6K431-2]
DR Gramene; Os09t0134500-02; Os09t0134500-02; Os09g0134500. [Q6K431-1]
DR KEGG; osa:4346464; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_005729_0_0_1; -.
DR InParanoid; Q6K431; -.
DR OMA; PYIVSGF; -.
DR OrthoDB; 181572at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0048578; P:positive regulation of long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd15662; ePHD_ATX1_2_like; 1.
DR CDD; cd15494; PHD_ATX1_2_like; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR041956; ATX1/2_ePHD.
DR InterPro; IPR042010; ATX1/2_PHD.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003889; FYrich_C.
DR InterPro; IPR003888; FYrich_N.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF05965; FYRC; 1.
DR Pfam; PF05964; FYRN; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00542; FYRC; 1.
DR SMART; SM00541; FYRN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51543; FYRC; 1.
DR PROSITE; PS51542; FYRN; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Flowering; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1022
FT /note="Histone-lysine N-methyltransferase TRX1"
FT /id="PRO_0000437438"
FT DOMAIN 264..327
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 402..461
FT /note="FYR N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00875"
FT DOMAIN 465..548
FT /note="FYR C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00876"
FT DOMAIN 861..979
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 985..1001
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 553..609
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 564..615
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 31..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 943
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 978
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 989
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 991
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 996
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT VAR_SEQ 869..873
FT /note="RIHGF -> INLYQ (in isoform 2)"
FT /id="VSP_058520"
FT VAR_SEQ 874..1022
FT /note="Missing (in isoform 2)"
FT /id="VSP_058521"
SQ SEQUENCE 1022 AA; 115660 MW; 121B74C4998D773A CRC64;
MVIAVEGGFV HEEEEVDHPI RYLPLGRVYS SSAPCPLPKK PRSAEDGKPP VIVYYRRRRK
KPRVEGPPPS PATAPPMLHP REDDEDEEVT RRKGSLKYEL LSLGQAPPAL GGDGEEPARR
RCLRRSGGAE RRGYFSEPKR RQRQGVHKEA ASSAGRRWLE LEIEAADPLA FVGLGCKVFW
PLDEDWYKGS ITGYNEATKK HSVKYDDGES EDLNLADERI KFSISSEEMK CRNLKFGISN
LNKRGYDELL ALAVSLHDYQ GLDPGDLVWA KLTGHAMWPA VVVDESNVPA NRALKPGRLD
QSILVQFFGT HDFARIKLKQ AVPFLNGLLS SLHLKCKQAR FYRSLEEAKE FLCTQLLPEN
MLQLQKSMEK GSSDANSNKD VHSCDNLSED KTAESGGDYD EMTPIELGNL RVSKLGRIVT
DSDYFHNKKH IWPEGYTAFR KFRSVKDPHV VILYKMEVLR NSDIKARPLF RVTSEDGTQI
DGSTPNTCWK EIYCRLKEKQ RNVASGLDRD VCQGSGSYMF GFSNPQIRQL IQELPNARSC
LKYFENAGDT FRGYRAVHVN WKDLDYCSVC DMDEEYEDNL FLQCDKCRMM VHARCYGELE
PLNGVLWLCN LCRPEAPRVS PRCCLCPVTG GAMKPTTDGR WAHLACAIWI PETCLKDVKR
MEPIDGLSRI NKDRWKLLCS ICGVAYGACI QCSHPTCRVA YHPLCARAAD LCVELEDDDK
IHLMLLDEDE DPCIRLLSYC KKHRQPSTER PSLESNLAKP AVVVQTDAVP PSGCARTEPY
NIHGRRGQKQ PQVMATASVK RLYVENMPYI VSGFCQNRVG HDAISEPIQS VGFLDVAHQE
AVGNVSSMIE KYKSMKATFR RRLAFGKSRI HGFGVFAKVS HKAGDMMIEY IGELVRPPIS
DIRERRIYNS LVGAGTYMFR IDDERVIDAT RAGSIAHLIN HSCEPNCYSR VISVLGDEHI
IIFAKRDINP WEELTYDYRF VSSDQRLPCY CGFPKCRGVV NDVEAEGQSA KIRVNRSELF
QQ
