JMJ21_ARATH
ID JMJ21_ARATH Reviewed; 943 AA.
AC Q9M9E8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lysine-specific demethylase JMJ21 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O64752};
DE AltName: Full=F-box protein JMJ21 {ECO:0000305};
DE AltName: Full=Jumonji domain-containing protein 21 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ21 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 21 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ21 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine monodemethylase JMJ21 {ECO:0000305};
GN Name=JMJ21 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At1g78280 {ECO:0000312|Araport:AT1G78280};
GN ORFNames=F3F9.18 {ECO:0000312|EMBL:AAF71807.1};
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] OF 701-943.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, and, to a lower extent,
CC in inflorescences, roots, siliques and stems.
CC {ECO:0000269|PubMed:18713399}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71807.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013430; AAF71807.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36090.1; -; Genomic_DNA.
DR EMBL; BX817819; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A96812; A96812.
DR RefSeq; NP_177951.6; NM_106477.7.
DR AlphaFoldDB; Q9M9E8; -.
DR SMR; Q9M9E8; -.
DR BioGRID; 29382; 1.
DR IntAct; Q9M9E8; 1.
DR STRING; 3702.AT1G78280.1; -.
DR iPTMnet; Q9M9E8; -.
DR PaxDb; Q9M9E8; -.
DR PRIDE; Q9M9E8; -.
DR ProteomicsDB; 222405; -.
DR EnsemblPlants; AT1G78280.1; AT1G78280.1; AT1G78280.
DR GeneID; 844163; -.
DR Gramene; AT1G78280.1; AT1G78280.1; AT1G78280.
DR KEGG; ath:AT1G78280; -.
DR Araport; AT1G78280; -.
DR TAIR; locus:2032090; AT1G78280.
DR eggNOG; KOG2130; Eukaryota.
DR HOGENOM; CLU_012984_0_0_1; -.
DR InParanoid; Q9M9E8; -.
DR OMA; QMRNIHQ; -.
DR OrthoDB; 609279at2759; -.
DR PhylomeDB; Q9M9E8; -.
DR PRO; PR:Q9M9E8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9E8; baseline and differential.
DR Genevisible; Q9M9E8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..943
FT /note="Lysine-specific demethylase JMJ21"
FT /id="PRO_0000283365"
FT DOMAIN 14..60
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 216..379
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 396..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 347
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 943 AA; 108505 MW; 2CA3E947EFCA380B CRC64;
MTTLGQRDRR PDALGSLSVL PDETICVLLE YLAPRDIAHL ACVSSVMYIL CNEEPLWMSL
CLRRAKGPLE YKGSWKKTTL HLEGVTQEND AYRKCFHFDG FMSLYLYKRF YRCNTSLDGF
SFDNGNVERR RNISLDEFSK EYDAKKPVLL SGLADSWPAS NTWTIDQLSE KYGEVPFRIS
QRSPNKISMK FKDYIAYMKT QRDEDPLYVF DDKFGEAAPE LLKDYSVPHL FQEDWFEILD
KESRPPYRWL IVGPERSGAS WHVDPALTSA WNTLLCGRKR WALYPPGKVP LGVTVHVNED
DGDVSIDTPS SLQWWLDYYP LLADEDKPIE CTLLPGETIY VPSGWWHCIL NLEPTVAVTQ
NFVNKENFGF VCLDMAPGYH HKGVCRAGLL ALDDENSEDL EEETHDEEDN TLSYSDLTRK
EKRTRMNGGG ETENREEDVN GVSKRYNMWK NGFSYDIDFL ASFLDKERDH YNFPWSMGNS
VGQREMRAWL SKLWVLKPEM RELIWKGACI ALNAEKWLRC LEEVCTFHNL PLVTEDEKLP
VGTGSNPVYL LSDYAIKLFV EGGLEQSMYG LGTELEFYDI LGRADSPLKT HIPEVLASGI
LFFEKGSYKV VPWDGKRIPD IISSSSFDFD ASMLNSEFPF GIWNKTLREH KNQGKPAPDS
FGSLSSHVWP YIITKRCKGK IFAQLRDDLT WNDAQNLAFF LGQQLRNLHL LPYPPVTRPE
LLNVNAVHEE LNIPAEWKVF VDALCQKKKD VTSRLENWGN PIPRALMTKI DEYIPDDFFV
DLLHVFKETN GGDEIKPCTW IHSDVMDDNI HMEPYADDSV DGQHNSWRPS HILDFSDLTI
GDPICDLIPI YLDVFRGDAD LLKKLLENYG LPLIRSRSSE NGTTKTADST RKKVLSPSYR
TMCYCILHEE NVLGSIFSIW DELRTAESWE QVEQTVWSLL NTY
