JMJ31_ARATH
ID JMJ31_ARATH Reviewed; 549 AA.
AC F4K2M8; Q8GZ41;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Lysine-specific demethylase JMJ31 {ECO:0000303|PubMed:18713399};
DE EC=1.14.11.- {ECO:0000250|UniProtKB:O64752};
DE AltName: Full=Jumonji domain-containing protein 31 {ECO:0000303|PubMed:18713399};
DE Short=AtJMJ31 {ECO:0000303|PubMed:18713399};
DE Short=Protein JUMONJI 31 {ECO:0000303|PubMed:18713399};
DE AltName: Full=Lysine-specific histone demethylase JMJ31 {ECO:0000303|PubMed:18713399};
DE AltName: Full=[histone H3]-trimethyl-L-lysine monodemethylase JMJ31 {ECO:0000305};
GN Name=JMJ31 {ECO:0000303|PubMed:18713399};
GN OrderedLocusNames=At5g19840 {ECO:0000312|Araport:AT5G19840};
GN ORFNames=T29J13.260 {ECO:0000312|EMBL:AF296838};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 inflorescences, and,
CC to a lower extent, in 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=BAC41899.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF296838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92755.1; -; Genomic_DNA.
DR EMBL; AK117223; BAC41899.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001190341.1; NM_001203412.2.
DR SMR; F4K2M8; -.
DR STRING; 3702.AT5G19840.2; -.
DR PaxDb; F4K2M8; -.
DR PRIDE; F4K2M8; -.
DR ProteomicsDB; 201586; -.
DR EnsemblPlants; AT5G19840.2; AT5G19840.2; AT5G19840.
DR GeneID; 832104; -.
DR Gramene; AT5G19840.2; AT5G19840.2; AT5G19840.
DR KEGG; ath:AT5G19840; -.
DR Araport; AT5G19840; -.
DR TAIR; locus:2183249; AT5G19840.
DR eggNOG; ENOG502QT8Y; Eukaryota.
DR InParanoid; F4K2M8; -.
DR OrthoDB; 1385616at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K2M8; baseline and differential.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR027445; FIH-1.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12461:SF80; PTHR12461:SF80; 1.
DR Pfam; PF13621; Cupin_8; 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.
FT CHAIN 1..549
FT /note="Lysine-specific demethylase JMJ31"
FT /id="PRO_0000456196"
FT DOMAIN 125..296
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 549 AA; 61906 MW; 5C1E13B39E791C9C CRC64;
MPTGCEFPMI KTFENALTAA DFESTVELTN FPAVFRGCAS VWDAYSKWNP FNSGLDYLEE
RAGSVEVEAM LSRTAPVFNG DIRSHERVSL PFSDFIRFCK QHMRGKGNGS GVDAKSADLN
PMCEDYRPGQ IYLAQFPILN DEKEEKVLLK ILRQDIQTPT FLDAKSLSSI NFWMNSAEAR
SSTHYDPHHN LLCVVSGRKK VVLWPPSASP SLYPMPIYGE ASNHSSVGLE NPNLSDYPRA
EHSLKQSQEI TLNAGDAVFI PEGWFHQVDS DELTVAVNFW WQSNYMSNMP EHMDSYYLRR
ITRSLLVSKP SSTDLRHLSE HIDQSRIEMA EGGNDNIGNE SIKKGLSTLH EKASLHDLDP
SASQALHDLI SLVHDHVNAV DTSKGLQHTS PSCSEGGEKS KFLVNAMSCL EDDRVAHLLW
NLEASRLRDV LLAMALELSY LKLLVKMEIF VLVLHKIFET LEALILHMLS PIAAEVLTQK
FDEIDQQTGE EDRTQFFREF YSAFDDEAAA MDIILSRKEA FAFQVCSLAS LCRLRTYHKL
KGEKFSASY
