JMJ31_CAEEL
ID JMJ31_CAEEL Reviewed; 1061 AA.
AC Q95QK3;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Lysine-specific demethylase jmjd-3.1 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000269|PubMed:17713478};
DE AltName: Full=JmjC domain-containing protein 3.1 {ECO:0000305};
GN Name=jmjd-3.1 {ECO:0000312|WormBase:F18E9.5b};
GN ORFNames=F18E9.5 {ECO:0000312|WormBase:F18E9.5b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17713478; DOI=10.1038/nature06145;
RA Agger K., Cloos P.A., Christensen J., Pasini D., Rose S., Rappsilber J.,
RA Issaeva I., Canaani E., Salcini A.E., Helin K.;
RT "UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene
RT regulation and development.";
RL Nature 449:731-734(2007).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21803287; DOI=10.1016/j.cmet.2011.07.001;
RA Jin C., Li J., Green C.D., Yu X., Tang X., Han D., Xian B., Wang D.,
RA Huang X., Cao X., Yan Z., Hou L., Liu J., Shukeir N., Khaitovich P.,
RA Chen C.D., Zhang H., Jenuwein T., Han J.D.;
RT "Histone demethylase UTX-1 regulates C. elegans life span by targeting the
RT insulin/IGF-1 signaling pathway.";
RL Cell Metab. 14:161-172(2011).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=22570628; DOI=10.1371/journal.pgen.1002647;
RA Vandamme J., Lettier G., Sidoli S., Di Schiavi E., Noerregaard Jensen O.,
RA Salcini A.E.;
RT "The C. elegans H3K27 demethylase UTX-1 is essential for normal
RT development, independent of its enzymatic activity.";
RL PLoS Genet. 8:E1002647-E1002647(2012).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-3 AND WDR-5.1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 811-HIS--GLU-813; GLY-888; SER-903; CYS-998; CYS-1001; CYS-1025 AND
RP CYS-1028.
RX PubMed=25124442; DOI=10.1126/science.1255885;
RA Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
RA Jarriault S.;
RT "Sequential histone-modifying activities determine the robustness of
RT transdifferentiation.";
RL Science 345:826-829(2014).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=26212459; DOI=10.1016/j.molcel.2015.06.027;
RA Labbadia J., Morimoto R.I.;
RT "Repression of the heat shock response is a programmed event at the onset
RT of reproduction.";
RL Mol. Cell 59:639-650(2015).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27133168; DOI=10.1016/j.cell.2016.04.012;
RA Merkwirth C., Jovaisaite V., Durieux J., Matilainen O., Jordan S.D.,
RA Quiros P.M., Steffen K.K., Williams E.G., Mouchiroud L., Tronnes S.U.,
RA Murillo V., Wolff S.C., Shaw R.J., Auwerx J., Dillin A.;
RT "Two Conserved Histone Demethylases Regulate Mitochondrial Stress-Induced
RT Longevity.";
RL Cell 165:1209-1223(2016).
CC -!- FUNCTION: Histone demethylase that specifically demethylates
CC trimethylated 'Lys-27' of histone H3, a mark associated with
CC transcriptional repression, thereby playing a central role in the
CC histone code (PubMed:17713478, PubMed:25124442). Involved in the
CC transcriptional regulation of the heat shock response, unfolded protein
CC response and possibly other stress response target genes
CC (PubMed:26212459,PubMed:27133168). Required for gonad development and
CC organization (PubMed:17713478). Required for the robust
CC transdifferentiation of the Y rectal epithelial cell to the PDA motor
CC neuron during larval development (PubMed:25124442). Acts cell-
CC autonomously in Y-to-PDA transdifferentiation, which depends on the
CC demethylase activity and on recognition of the H3 tail
CC (PubMed:25124442). Cooperates with set-2 and unc-3 to ensure robust Y-
CC to-PDA transdifferentiation (PubMed:25124442). Promotes mitochondrial
CC stress-induced longevity (PubMed:27133168). Involved in lifespan
CC regulation (PubMed:21803287, PubMed:26212459).
CC {ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:21803287,
CC ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:26212459,
CC ECO:0000269|PubMed:27133168}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:O15054};
CC -!- SUBUNIT: Interacts with wdr-5.1 and unc-3.
CC {ECO:0000269|PubMed:25124442}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25124442}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in head and tail.
CC {ECO:0000269|PubMed:22570628}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the Y cell before
CC transdifferentiation in the embryo and during redifferentiation into
CC the PDA neuron in larval stages L2 and L3 but not in larval stage L1
CC (PubMed:25124442). Expression declines in the adult soma
CC (PubMed:26212459). {ECO:0000269|PubMed:25124442,
CC ECO:0000269|PubMed:26212459}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in abnormal gonad
CC migration with aberrant turns and positioning of the distal end as well
CC as in disorganized accumulation of oocytes in the proximal gonad arm
CC (PubMed:17713478). RNAi-mediated knockdown also results in disruption
CC of invariant Y-to-PDA transdifferentiation (PubMed:25124442). RNAi-
CC mediated knockdown suppresses mitochondrial stress response mediated
CC longevity (PubMed:27133168). RNAi-mediated knockdown reduces lifespan
CC of floxuridine-treated animals (PubMed:21803287).
CC {ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:21803287,
CC ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:27133168}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
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DR EMBL; BX284606; CCD68428.1; -; Genomic_DNA.
DR RefSeq; NP_509451.2; NM_077050.5.
DR AlphaFoldDB; Q95QK3; -.
DR SMR; Q95QK3; -.
DR DIP; DIP-61429N; -.
DR IntAct; Q95QK3; 2.
DR STRING; 6239.F18E9.5b; -.
DR PaxDb; Q95QK3; -.
DR EnsemblMetazoa; F18E9.5b.1; F18E9.5b.1; WBGene00017571.
DR GeneID; 181111; -.
DR KEGG; cel:CELE_F18E9.5; -.
DR UCSC; F18E9.5a.2; c. elegans.
DR CTD; 181111; -.
DR WormBase; F18E9.5b; CE30958; WBGene00017571; jmjd-3.1.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00970000196490; -.
DR HOGENOM; CLU_296162_0_0_1; -.
DR InParanoid; Q95QK3; -.
DR OrthoDB; 268901at2759; -.
DR PhylomeDB; Q95QK3; -.
DR BRENDA; 1.14.11.68; 1045.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-3214842; HDMs demethylate histones.
DR PRO; PR:Q95QK3; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017571; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q95QK3; baseline and differential.
DR GO; GO:0044666; C:MLL3/4 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071557; P:histone H3-K27 demethylation; IDA:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..1061
FT /note="Lysine-specific demethylase jmjd-3.1"
FT /id="PRO_0000438800"
FT DOMAIN 760..923
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..417
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:25124442"
FT REGION 418..759
FT /note="Required for binding of unc-3 and for function in Y-
FT to-PDA transdifferentiation"
FT /evidence="ECO:0000269|PubMed:25124442"
FT COMPBIAS 261..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 811
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 813
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 891
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 998
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1001
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1025
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT BINDING 1028
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O14607"
FT MUTAGEN 811..813
FT /note="HME->TMG: Disruption of Y-to-PDA
FT transdifferentiation."
FT /evidence="ECO:0000269|PubMed:25124442"
FT MUTAGEN 888
FT /note="G->E: In fp11; loss of demethylase activity and
FT disruption of Y-to-PDA transdifferentiation."
FT /evidence="ECO:0000269|PubMed:25124442"
FT MUTAGEN 903
FT /note="S->F: In fp25; loss of demethylase activity and
FT disruption of Y-to-PDA transdifferentiation."
FT /evidence="ECO:0000269|PubMed:25124442"
FT MUTAGEN 998
FT /note="C->S: Disruption of Y-to-PDA transdifferentiation;
FT when associated with S-1001; S-1025 and S-1028."
FT /evidence="ECO:0000269|PubMed:25124442"
FT MUTAGEN 1001
FT /note="C->S: Disruption of Y-to-PDA transdifferentiation;
FT when associated with S-998; S-1025 and S-1028."
FT /evidence="ECO:0000269|PubMed:25124442"
FT MUTAGEN 1025
FT /note="C->S: Disruption of Y-to-PDA transdifferentiation;
FT when associated with S-998; S-1001 and S-1028."
FT /evidence="ECO:0000269|PubMed:25124442"
FT MUTAGEN 1028
FT /note="C->S: Disruption of Y-to-PDA transdifferentiation;
FT when associated with S-998; S-1001 and S-1025."
FT /evidence="ECO:0000269|PubMed:25124442"
SQ SEQUENCE 1061 AA; 120302 MW; FB9A9043CBFFBF0E CRC64;
MQGKNSHLTG ITGTTHFTIF GASPRSMSLV KNSQETPPFP GMNSTMRPVE FNSTKQPEAQ
TIDQEQDAPK SFDFKNQTLG VYSDTVLNPL KNDSFKDELV VDVQKNLPIE SLTVSPKSST
DQNCRSTNEA IRIAGFDNFA DQLQESNGVF EACPEAHSEQ GNESEDFKDL INSETECNIE
DVVLPTVHVS TDSEEIISGD VIMNDSNVVS KPKNLEKVET PDVLIGSGSN DKLSDMTEQI
GNNQHLEKLI SEKTEKSLSD NETTLKPVPV QHTNSVGSSI GTTSGDSEIS DDDQKSWSPK
NESLDYQPAS TSSEFTETTS VANQTESNAG SVDDYCPRTS IDIGLDSSAP SCSSDATREP
TPIKKRGRKK KEQSATEPPI PRTKRAYTKN PNTIRKRRMK KNQSDDEEDD GPPKRRTINY
QIEFRDASGA WTMAQQLIFV RDFMSKKNDK IVKLSKSRQD RVDKFILQFQ KTQDSHYMRA
AIQLNTIFPD QGNYRHCQDY LKDLTIRVVV PPKRREGKRK SEVPANPPAL LLTGPLYLNF
YCTSQEVLEA AGQLLEFHVN AVYKDERLQP PVADKTLLDL ERAMYHEQVK DLTDYHKYRI
PCPTLTVTTK EEVFSSDFER ILNSASITNI SGIAKALNIK TELFSLPEIA KCHPELSIDI
LNQVPQSADG NCDSKGIRCW DVTSYSSKMK LQDFERYMQK EESEAMQAFE TISNCTAKEL
ESTCQKLKAE RIAAQNAIEG CDETMPWIKF GTNIDLLSEN FKKQMNEIEK LPTFLLPNRE
GNLLNYAGVD VLGINTVQMY AKPIGSRTPA HMENSLMASI NWNRGPGTCV WFAVPYEYWG
QLEFMIGEHG HKYQDQDYWP SEKELLELGV PVIKFEQKAD EMVYVNTGCF HWVQSNSFCI
NVSWNVGQPN FTQLATSIVA HDHNMLIGNQ AHVPLVNLVW NAARQRLFVD DPEMYKAMRG
VMIRSLAHSK WYFDLIDHHD YIVGDASEWK LADRVQRCKY CTSEIFNIVR WYTTEDLSVD
SYPFCSHCHV ANEYKKDRFL KYTWFFSLET LVNIFDAYVP N
