JMJ19_ARATH
ID JMJ19_ARATH Reviewed; 708 AA.
AC Q8L7T6; Q9ZV12;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable inactive lysine-specific demethylase JMJ19 {ECO:0000305};
DE AltName: Full=Jumonji domain-containing protein 19 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ19 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 19 {ECO:0000303|PubMed:18713399};
GN Name=JMJ19 {ECO:0000303|PubMed:18713399};
GN Synonyms=PKDM7A {ECO:0000303|PubMed:20202164};
GN OrderedLocusNames=At2g38950 {ECO:0000312|Araport:AT2G38950};
GN ORFNames=T7F6.12 {ECO:0000312|EMBL:AAC79608.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=20202164; DOI=10.1111/j.1365-313x.2010.04182.x;
RA Yang W., Jiang D., Jiang J., He Y.;
RT "A plant-specific histone H3 lysine 4 demethylase represses the floral
RT transition in Arabidopsis.";
RL Plant J. 62:663-673(2010).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- TISSUE SPECIFICITY: Expressed in inflorescences, roots, siliques,
CC leaves and stems. {ECO:0000269|PubMed:18713399}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20202164}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the 2 conserved His residues involved in iron binding
CC and essential for dioxygenase activity. Its enzyme activity is
CC therefore unsure. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79608.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005770; AAC79608.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09616.1; -; Genomic_DNA.
DR EMBL; AY127026; AAM83250.1; -; mRNA.
DR EMBL; BT001088; AAN46869.1; -; mRNA.
DR PIR; D84811; D84811.
DR RefSeq; NP_181429.2; NM_129453.4.
DR AlphaFoldDB; Q8L7T6; -.
DR SMR; Q8L7T6; -.
DR BioGRID; 3819; 3.
DR IntAct; Q8L7T6; 2.
DR STRING; 3702.AT2G38950.1; -.
DR PaxDb; Q8L7T6; -.
DR PRIDE; Q8L7T6; -.
DR ProteomicsDB; 232269; -.
DR EnsemblPlants; AT2G38950.1; AT2G38950.1; AT2G38950.
DR GeneID; 818480; -.
DR Gramene; AT2G38950.1; AT2G38950.1; AT2G38950.
DR KEGG; ath:AT2G38950; -.
DR Araport; AT2G38950; -.
DR TAIR; locus:2064910; AT2G38950.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_8_2_1; -.
DR InParanoid; Q8L7T6; -.
DR OMA; CRREFLA; -.
DR OrthoDB; 664180at2759; -.
DR PhylomeDB; Q8L7T6; -.
DR PRO; PR:Q8L7T6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L7T6; baseline and differential.
DR Genevisible; Q8L7T6; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR004198; Znf_C5HC2.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..708
FT /note="Probable inactive lysine-specific demethylase JMJ19"
FT /id="PRO_0000429997"
FT DOMAIN 108..149
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 293..454
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 544..581
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 35..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 646..653
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 558
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8GUI6"
SQ SEQUENCE 708 AA; 79304 MW; 79B821B44CA5D3DC CRC64;
MGIEGVSTYL KSGNMDTISA PPGFVSQTSF VLRNVPRDKE SPRSVSRQEQ TTGFGTDDKD
SCNMFLKSRP WIVHGHTIPS SEALRPKKTE VRRRRPLKVS ETKVLEEAPV FNPTEEEFRD
TLSYISSLRD RAEPYGICCV VPPPSWKPPC LLKEKQIWEA STFFPQVQLF GIQTENRKIK
KEVDADSNDA ASEGVQLCRV ERGPGYTLKS FKNFADTYKK SHFGMKDEVL GSENSSPSLK
PNELIVADIE KEYRQIVESP LIEIGVLYGN DLDTATFGSG FPLSAPSESS KYSSGWNLNS
TAKLPGSLLS LEDCESVCVP RLSVGMCLSS QFWKSEKERL YSLCYLHVGA PRVWYSVAGC
HRSKFKAAMK SFILEMSGEQ PKKSHNPVMM MSPYQLSVEG IPVTRCVQHP GQYVIIFPGS
YYSAFDCGFN CLEKANFAPL DWLPHGDIAV QVNQEMSKTS LISYDKLLFS AAREAVKCLK
EYGLSKKNTA CYTRWNDSCG TDGLFSNIIK SRIKLEKNRR EFLISSLESQ RMDKSYDAVN
KRECCVCLGD LYLSAVNCSC SANRYSCLNH MRKLCACPCD RKSFLYRYTM DELNLLVEAL
EGKKLSSMFR WAGIDQKFCA SPATTSSKPE EDKGKETDEV TPCNITRKDV AAGTKDQTRV
KARSLADILN VKDGNNDAKE TLESCSKKSN RPCDNDSSEA NAPKKQKQ
