ATXR7_ARATH
ID ATXR7_ARATH Reviewed; 1423 AA.
AC F4K1J4; A9QA58; Q56XT6; Q945S7; Q9FIH7;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Histone-lysine N-methyltransferase ATXR7 {ECO:0000305};
DE EC=2.1.1.354 {ECO:0000305|PubMed:19855050};
DE EC=2.1.1.357 {ECO:0000305|PubMed:19726574};
DE AltName: Full=Protein SET DOMAIN GROUP 25 {ECO:0000303|PubMed:19726574};
DE AltName: Full=Trithorax-related protein 7 {ECO:0000303|PubMed:19855050};
GN Name=ATXR7 {ECO:0000303|PubMed:19855050};
GN Synonyms=SDG25 {ECO:0000303|PubMed:19726574};
GN OrderedLocusNames=At5g42400 {ECO:0000312|Araport:AT5G42400};
GN ORFNames=MDH9.9 {ECO:0000312|EMBL:BAB10481.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19726574; DOI=10.1104/pp.109.143941;
RA Berr A., Xu L., Gao J., Cognat V., Steinmetz A., Dong A., Shen W.H.;
RT "SET DOMAIN GROUP25 encodes a histone methyltransferase and is involved in
RT FLOWERING LOCUS C activation and repression of flowering.";
RL Plant Physiol. 151:1476-1485(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-513.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1032-1290.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19855050; DOI=10.1105/tpc.109.070060;
RA Tamada Y., Yun J.Y., Woo S.C., Amasino R.M.;
RT "ARABIDOPSIS TRITHORAX-RELATED7 is required for methylation of lysine 4 of
RT histone H3 and for transcriptional activation of FLOWERING LOCUS C.";
RL Plant Cell 21:3257-3269(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21799800; DOI=10.1371/journal.pone.0022241;
RA Liu Y., Geyer R., van Zanten M., Carles A., Li Y., Horold A.,
RA van Nocker S., Soppe W.J.;
RT "Identification of the Arabidopsis REDUCED DORMANCY 2 gene uncovers a role
RT for the polymerase associated factor 1 complex in seed dormancy.";
RL PLoS ONE 6:E22241-E22241(2011).
CC -!- FUNCTION: Histone methyltransferase involved in regulation of flowering
CC time. Required for the expression of the flowering repressors FLC and
CC MADS-box genes of the MAF family (PubMed:19726574, PubMed:19855050).
CC Required for histone H3 dimethylation on 'Lys-36' H3K36me2 at the FLC
CC locus (PubMed:19726574). Required for histone H3 trimethylation on
CC 'Lys-4' (H3K4me3) at the FLC locus. Prevents trimethylation on 'Lys-27'
CC (H3K27me3) at the same locus (PubMed:19855050). Involved in the control
CC of seed dormancy and germination (PubMed:21799800).
CC {ECO:0000269|PubMed:19726574, ECO:0000269|PubMed:19855050,
CC ECO:0000269|PubMed:21799800}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000305|PubMed:19855050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+)
CC + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357;
CC Evidence={ECO:0000305|PubMed:19726574};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19726574}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot and root apices, vascular
CC tissues and mesophyll cells of rosette leaves.
CC {ECO:0000269|PubMed:19855050}.
CC -!- DISRUPTION PHENOTYPE: Early flowering (PubMed:19726574,
CC PubMed:19855050). Reduced seed dormancy and increased germination rate
CC of freshly harvested seeds (PubMed:21799800).
CC {ECO:0000269|PubMed:19726574, ECO:0000269|PubMed:19855050,
CC ECO:0000269|PubMed:21799800}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABV68922.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAB10481.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EU014691; ABV68922.1; ALT_SEQ; mRNA.
DR EMBL; AB016888; BAB10481.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK221587; BAD95095.1; -; mRNA.
DR EMBL; AF408061; AAL01112.1; -; mRNA.
DR RefSeq; NP_001318731.1; NM_001344444.1.
DR RefSeq; NP_001330664.1; NM_001344445.1.
DR RefSeq; NP_001330665.1; NM_001344446.1.
DR RefSeq; NP_001330666.1; NM_001344449.1.
DR RefSeq; NP_001330667.1; NM_001344450.1.
DR RefSeq; NP_001330668.1; NM_001344447.1.
DR RefSeq; NP_001330669.1; NM_001344448.1.
DR RefSeq; NP_001330670.1; NM_001344451.1.
DR AlphaFoldDB; F4K1J4; -.
DR SMR; F4K1J4; -.
DR STRING; 3702.AT5G42400.1; -.
DR PaxDb; F4K1J4; -.
DR PRIDE; F4K1J4; -.
DR GeneID; 834246; -.
DR KEGG; ath:AT5G42400; -.
DR Araport; AT5G42400; -.
DR TAIR; locus:2162346; AT5G42400.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_003563_0_0_1; -.
DR InParanoid; F4K1J4; -.
DR OrthoDB; 875190at2759; -.
DR PRO; PR:F4K1J4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K1J4; baseline and differential.
DR Genevisible; F4K1J4; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0010452; P:histone H3-K36 methylation; IDA:TAIR.
DR GO; GO:0051568; P:histone H3-K4 methylation; IGI:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.1490.40; -; 2.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF55277; SSF55277; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50829; GYF; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Flowering; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..1423
FT /note="Histone-lysine N-methyltransferase ATXR7"
FT /id="PRO_0000432765"
FT DOMAIN 263..312
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT DOMAIN 1266..1383
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 923..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1382
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT CONFLICT 1046
FT /note="A -> V (in Ref. 5; AAL01112)"
FT /evidence="ECO:0000305"
FT CONFLICT 1124
FT /note="Q -> K (in Ref. 5; AAL01112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1423 AA; 158663 MW; E0FC98122AF0697D CRC64;
MVAVDSTFPS HGSSYSSRRK KVSALEPNYF GSMCMGVYSD DVSISAREVA QDYSCDSCGD
LATVSSACCN FDELCGLDSA LEMGCRSNED CRAGQEASGS GIASGLDKSV PGYTMYASGW
MYGNQQGQMC GPYTQQQLYD GLSTNFLPED LLVYPIINGY TANSVPLKYF KQFPDHVATG
FAYLQNGIIS VAPSVTSFPP SSSNATVHQD EIQTEHATSA THLISHQTMP PQTSSNGSVL
DQLTLNHEES NMLASFLSLG NEHACWFLVD GEGRNHGPHS ILELFSWQQH GYVSDAALIR
DGENKLRPIT LASLIGVWRV KCGDANCDEP VTGVNFISEV SEELSVHLQS GIMKIARRAL
LDEIISSVIS DFLKAKKSDE HLKSYPPTSA VESISSRVIN AEKSVVSNTE SAGCKNTMNE
GGHSSIAAES SKYTKSVGSI ENFQTSCSAV CRTLHHHCMQ IMWNAVFYDT VATHSSCWRK
NKIWFRSSDI STVNYCKGSH TKYSDKPESF ESFTCRVDSS SSKTAYSDEF DLATNGARVR
GLSSDTYGTE SVIASISEHV ENELFLSLKT HLTDYTSILI KDGANNTTSS ARDGKMHEGS
FREQYNLEGS SKKKNGLNVV PAKLRFSNDF SDSQRLLQEG ESSEQITSED IIANIFSTAL
ETSDIPVNDE LDALAIHEPP PPGCESNINM PCLRYKYQPV RSKESIPEIK AYVSMALCRQ
KLHNDVMRDW KSLFLKCYLN EFLASLKGSH QVSRKETLAL KKRKTVTRNK KLVQSNISNQ
TAEKLRKPCV GASEKVLVKR SKKLSDSHSM KEVLKVDTPS IDLSVRKPSQ QKMRNTDRRD
HCIIKDATKL HKEKVGKDAF SKVICDKSQD LEMEDEFDDA LLITRLRRIS RNKTKELREC
RNAAKSCEEI SVTAEESEET VDCKDHEESL SNKPSQKVKK AHTSKLKRKN LSDARDEGTK
SCNGAVKSFT EISGKEGDTE SLGLAISDKV SHQNLSKRRK SKIALFLFPG FENTSRKCFT
KLLSPEDAAK NGQDMSNPTG NPPRLAEGKK FVEKSACSIS QKGRKSSQSS ILKRKHQLDE
KISNVPSRRR LSLSSTDSED AVIKEDYDVR NEEKLPCHTS DKLQKGPNKL IRRRKPLAKH
TTERSPIKDL SVDDGRPKPI ALKPLEKLSS KPSKKKLFLS IPKSDGCART SINGWHWHAW
SLKASAEERA RVRGSSCVHM QHFGSKSSLT QNVLSARTNR AKLRNLLAAA DGADVLKMSQ
LKARKKHLRF QQSKIHDWGL VALEPIEAED FVIEYVGELI RSSISEIRER QYEKMGIGSS
YLFRLDDGYV LDATKRGGIA RFINHSCEPN CYTKIISVEG KKKIFIYAKR HIDAGEEISY
NYKFPLEDDK IPCNCGAPNV YCFCEQVPWI AKLKRRTWFS RRN
