JMJ26_ARATH
ID JMJ26_ARATH Reviewed; 875 AA.
AC C0SUU8; A0A178WJ43; O65384;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Lysine-specific demethylase JMJ26 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O64752};
DE AltName: Full=Jumonji domain-containing protein 26 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ26 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 26 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ26 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine monodemethylase JMJ26 {ECO:0000305};
GN Name=JMJ26 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At1g11950 {ECO:0000312|Araport:AT1G11950};
GN ORFNames=F12F1.18 {ECO:0000312|EMBL:AAC17616.1};
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 [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].
RA Fujita M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=18713399; DOI=10.1111/j.1744-7909.2008.00692.x;
RA Lu F., Li G., Cui X., Liu C., Wang X.-J., Cao X.;
RT "Comparative analysis of JmjC domain-containing proteins reveals the
RT potential histone demethylases in Arabidopsis and rice.";
RL J. Integr. Plant Biol. 50:886-896(2008).
CC -!- FUNCTION: May function as histone H3 lysine demethylase and be involved
CC in regulation of gene expression. {ECO:0000250|UniProtKB:O64752}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q8GUI6};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GUI6};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, roots, siliques,
CC leaves and stems. {ECO:0000269|PubMed:18713399}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17616.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002131; AAC17616.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28820.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60277.1; -; Genomic_DNA.
DR EMBL; AB493451; BAH30289.1; -; mRNA.
DR PIR; D86254; D86254.
DR RefSeq; NP_001322575.1; NM_001332013.1.
DR RefSeq; NP_172659.3; NM_101067.6.
DR SMR; C0SUU8; -.
DR STRING; 3702.AT1G11950.1; -.
DR PRIDE; C0SUU8; -.
DR ProteomicsDB; 177401; -.
DR EnsemblPlants; AT1G11950.1; AT1G11950.1; AT1G11950.
DR EnsemblPlants; AT1G11950.3; AT1G11950.3; AT1G11950.
DR GeneID; 837747; -.
DR Gramene; AT1G11950.1; AT1G11950.1; AT1G11950.
DR Gramene; AT1G11950.3; AT1G11950.3; AT1G11950.
DR Araport; AT1G11950; -.
DR TAIR; locus:2008875; AT1G11950.
DR eggNOG; KOG1356; Eukaryota.
DR HOGENOM; CLU_001811_2_1_1; -.
DR OMA; CNCTRCN; -.
DR OrthoDB; 1185631at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0SUU8; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:TAIR.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..875
FT /note="Lysine-specific demethylase JMJ26"
FT /id="PRO_0000456192"
FT DOMAIN 614..837
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 193..240
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 317..347
FT /note="B box-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOTIF 62..69
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 658
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 660
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 805
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 875 AA; 100146 MW; EBCE1AA00EF636A4 CRC64;
MEGEVATNGV ILKHNGVKDI SLETCWPEKK KPVEATSLSS GSSDIEEEIS VECPKRVANQ
RRKRSKADEI KTKSSRKRKC DDENKCEENE KKQRSSVKKR ATTWKEEEVV VDDEKKCEQQ
LQLVPSSKAT SRSRSKKSVS VDTWLVNNEI DVSALSSRSE SELSDSYLKT EYFNDCRSMT
RSLKANLGEL AICHQCSKGE RRYLFICTFC EVRLYCFPCI KKWYPHLSTD DILEKCPFCR
GTCNCCTCLH SSGLIETSKR KLDKYERFYH LRFLIVAMLP FLKKLCKAQD QEIETEAKVQ
DSMASQVDIS ESLCSNEERV FCNHCATSIV DLHRSCPKCS YELCLNCCQE IRGGWLSDRP
ECQLQFEYRG TRYIHGEAAE PSSSSVSEDE TKTPSIKWNA DENGSIRCAP KELGGCGDSV
LELKRILPVT WMSDLEQKAE TFLASYSIKP PMSYCRCSSD MSSMKRKAAS RDGSSDNYLY
SPDSLDVLKQ EELLHFQEHW SKGEPVIVRN ALNNTAGLSW EPMVMWRALC ENVDSAISSN
MSDVKAIDCL ANCEVKINTL CFFEGYSKGR TYENFWPEML KLKDWPPSDK FENLLPRHCD
EFISALPFQE YSDPRSGILN IATKLPEGLL KPDLGPKTYV AYGTSDELGR GDSVTKLHCD
MSDAVNILMH TAEVTLSEEQ RSAIADLKQK HKQQNEKELQ EQNGLEEEEV VSDEIVVYDE
TSGALWDIFK REDVPKLEEY LRKHCIEFRH TYCSRVTKVY HPIHDQSYFL TVEHKRKLKA
EFGIEPWTFV QKLGEAVFIP AGCPHQVRNL KSCTKVAVDF VSPENIDECL RLTDEFRQLP
KNHKAREDKL EIKKMVIYAV EQALKEVETL LLDRS
