JMJ29_ARATH
ID JMJ29_ARATH Reviewed; 883 AA.
AC C0SV12; O48794;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Lysine-specific demethylase JMJ29 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O64752};
DE AltName: Full=Jumonji domain-containing protein 29 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ29 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 29 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ29 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine monodemethylase JMJ29 {ECO:0000305};
GN Name=JMJ29 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At1g62310 {ECO:0000312|Araport:AT1G62310};
GN ORFNames=F24O1.3 {ECO:0000312|EMBL:AAF70852.1};
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=AAF70852.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003113; AAF70852.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33952.1; -; Genomic_DNA.
DR EMBL; AB493515; BAH30353.1; -; mRNA.
DR PIR; T01440; T01440.
DR RefSeq; NP_176421.1; NM_104911.3.
DR SMR; C0SV12; -.
DR STRING; 3702.AT1G62310.1; -.
DR PRIDE; C0SV12; -.
DR ProteomicsDB; 191564; -.
DR EnsemblPlants; AT1G62310.1; AT1G62310.1; AT1G62310.
DR GeneID; 842529; -.
DR Gramene; AT1G62310.1; AT1G62310.1; AT1G62310.
DR KEGG; ath:AT1G62310; -.
DR Araport; AT1G62310; -.
DR TAIR; locus:2027109; AT1G62310.
DR eggNOG; KOG1356; Eukaryota.
DR HOGENOM; CLU_001811_2_1_1; -.
DR OMA; FLKQICH; -.
DR OrthoDB; 1185631at2759; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0SV12; 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:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
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:0051567; P:histone H3-K9 methylation; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000039; P:regulation of trichome morphogenesis; IMP:TAIR.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR018866; Znf-4CXXC_R1.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF10497; zf-4CXXC_R1; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..883
FT /note="Lysine-specific demethylase JMJ29"
FT /id="PRO_0000456195"
FT DOMAIN 632..863
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 209..256
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 333..392
FT /note="B box-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOTIF 755..762
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 676
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 678
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 831
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 883 AA; 101477 MW; 3EBBE7B9060EB2F5 CRC64;
MDSGVKLEHM NCFQLSYQYS WTTRKKRTLK PFMSKGSSPS SSSDSRKRKL SRAEDSDDSA
VKRNAKRRRK ICKVEEYYED DDCILSDWVQ RNTAKRIDKR NEEVEVMVKI ESGDDCTIGK
WFSDVSSKRK DKRQVEVDED EEWEEEVTLC SKIKATSSRS RTHSLSANSP ENVTDVISPC
RSRSPASNVS DSIQKNDCTS SRKQSGPICH QCLKGERITL LICSECEKTM FCLQCIRKWY
PNLSEDDVVE KCPLCRQNCN CSKCLHLNGL IETSKRELAK SERRHHLQYL ITLMLPFLNK
LSIFQKLEIE FEATVQGKLP SEVEITAAIS YTDERVYCDH CATSIVDLHR SCPKCSYELC
LKCCQEIREG SLSERPEMKF HYVDRGHRYM HGLDAAEPSL SSTFEDEEAN PSDAKWSLGE
NGSITCAPEK LGGCGERMLE LRRILPLTWM SDLEHKAETF LSSYNISPRM LNCRCSSLET
ELTRKSASRT TSSDNYLFCP ESLGVLKEEE LLHFQEHWAK GEPVIVRNAL DNTPGLSWEP
MVMWRALCEN VNSTSSSEMS QVKAIDCLAN CEVEINTRQF FEGYSKGRTY ENFWPEMLKL
KDWPPSDKFE DLLPRHCDEF ISALPFQEYS DPRTGILNIA TKLPEGFIKP DLGPKTYIAY
GIPDELGRGD SVTKLHCDMS DAVNILTHTA EVTLSQEQIS SVKALKQKHK LQNKVDKQST
EDCNEKEEEE EEELNMPEIS SNENEETGSA LWDIFRREDV PKLEEYLRKH CKEFRHTYCS
PVTKVYHPIH DQSCYLTLEH KRKLKAEYGI EPWTFVQKLG EAVFIPAGCP HQVRNLKSCT
KVAVDFVSPE NIHECLRLTE EFRQLPKNHK AREDKLEASL LSL
