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Lysine-specific demethylase jmjd-3.1 (EC 1.14.11.-) (JmjC domain-containing protein 3.1)

 JMJ31_CAEEL             Reviewed;        1061 AA.
Q95QK3;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 2.
25-OCT-2017, entry version 107.
RecName: Full=Lysine-specific demethylase jmjd-3.1 {ECO:0000305};
EC=1.14.11.- {ECO:0000269|PubMed:17713478};
AltName: Full=JmjC domain-containing protein 3.1 {ECO:0000305};
Name=jmjd-3.1 {ECO:0000312|WormBase:F18E9.5b};
ORFNames=F18E9.5 {ECO:0000312|WormBase:F18E9.5b};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17713478; DOI=10.1038/nature06145;
Agger K., Cloos P.A., Christensen J., Pasini D., Rose S.,
Rappsilber J., Issaeva I., Canaani E., Salcini A.E., Helin K.;
"UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene
regulation and development.";
Nature 449:731-734(2007).
[3] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21803287; DOI=10.1016/j.cmet.2011.07.001;
Jin C., Li J., Green C.D., Yu X., Tang X., Han D., Xian B., Wang D.,
Huang X., Cao X., Yan Z., Hou L., Liu J., Shukeir N., Khaitovich P.,
Chen C.D., Zhang H., Jenuwein T., Han J.D.;
"Histone demethylase UTX-1 regulates C. elegans life span by targeting
the insulin/IGF-1 signaling pathway.";
Cell Metab. 14:161-172(2011).
[4] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=22570628; DOI=10.1371/journal.pgen.1002647;
Vandamme J., Lettier G., Sidoli S., Di Schiavi E.,
Noerregaard Jensen O., Salcini A.E.;
"The C. elegans H3K27 demethylase UTX-1 is essential for normal
development, independent of its enzymatic activity.";
PLoS Genet. 8:E1002647-E1002647(2012).
[5] {ECO:0000305}
FUNCTION, INTERACTION WITH UNC-3 AND WDR-5.1, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
811-HIS--GLU-813; GLY-888; SER-903; CYS-998; CYS-1001; CYS-1025 AND
CYS-1028.
PubMed=25124442; DOI=10.1126/science.1255885;
Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
Jarriault S.;
"Sequential histone-modifying activities determine the robustness of
transdifferentiation.";
Science 345:826-829(2014).
[6] {ECO:0000305}
FUNCTION.
PubMed=26212459; DOI=10.1016/j.molcel.2015.06.027;
Labbadia J., Morimoto R.I.;
"Repression of the heat shock response is a programmed event at the
onset of reproduction.";
Mol. Cell 59:639-650(2015).
[7] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27133168; DOI=10.1016/j.cell.2016.04.012;
Merkwirth C., Jovaisaite V., Durieux J., Matilainen O., Jordan S.D.,
Quiros P.M., Steffen K.K., Williams E.G., Mouchiroud L., Tronnes S.U.,
Murillo V., Wolff S.C., Shaw R.J., Auwerx J., Dillin A.;
"Two Conserved Histone Demethylases Regulate Mitochondrial Stress-
Induced Longevity.";
Cell 165:1209-1223(2016).
-!- FUNCTION: Histone demethylase that specifically demethylates
trimethylated 'Lys-27' of histone H3, a mark associated with
transcriptional repression, thereby playing a central role in the
histone code (PubMed:17713478, PubMed:25124442). Involved in the
transcriptional regulation of the heat shock response, unfolded
protein response and possibly other stress response target genes
(PubMed:26212459,PubMed:27133168). Required for gonad development
and organization (PubMed:17713478). Required for the robust
transdifferentiation of the Y rectal epithelial cell to the PDA
motor neuron during larval development (PubMed:25124442). Acts
cell-autonomously in Y-to-PDA transdifferentiation, which depends
on the demethylase activity and on recognition of the H3 tail
(PubMed:25124442). Cooperates with set-2 and unc-3 to ensure
robust Y-to-PDA transdifferentiation (PubMed:25124442). Promotes
mitochondrial stress-induced longevity (PubMed:27133168). Involved
in lifespan regulation (PubMed:21803287, PubMed:26212459).
{ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:21803287,
ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:26212459,
ECO:0000269|PubMed:27133168}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000250|UniProtKB:O15054};
-!- SUBUNIT: Interacts with wdr-5.1 and unc-3.
{ECO:0000269|PubMed:25124442}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25124442}.
-!- TISSUE SPECIFICITY: Mainly expressed in head and tail.
{ECO:0000269|PubMed:22570628}.
-!- DEVELOPMENTAL STAGE: Expressed in the Y cell before
transdifferentiation in the embryo and during redifferentiation
into the PDA neuron in larval stages L2 and L3 but not in larval
stage L1 (PubMed:25124442). Expression declines in the adult soma
(PubMed:26212459). {ECO:0000269|PubMed:25124442,
ECO:0000269|PubMed:26212459}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in abnormal
gonad migration with aberrant turns and positioning of the distal
end as well as in disorganized accumulation of oocytes in the
proximal gonad arm (PubMed:17713478). RNAi-mediated knockdown also
results in disruption of invariant Y-to-PDA transdifferentiation
(PubMed:25124442). RNAi-mediated knockdown suppresses
mitochondrial stress response mediated longevity
(PubMed:27133168). RNAi-mediated knockdown reduces lifespan of
floxuridine-treated animals (PubMed:21803287).
{ECO:0000269|PubMed:17713478, ECO:0000269|PubMed:21803287,
ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:27133168}.
-!- SIMILARITY: Belongs to the UTX family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BX284606; CCD68428.1; -; Genomic_DNA.
RefSeq; NP_509451.2; NM_077050.5.
UniGene; Cel.17165; -.
ProteinModelPortal; Q95QK3; -.
SMR; Q95QK3; -.
DIP; DIP-61429N; -.
IntAct; Q95QK3; 2.
STRING; 6239.F18E9.5b.2; -.
PaxDb; Q95QK3; -.
EnsemblMetazoa; F18E9.5b; F18E9.5b; WBGene00017571.
GeneID; 181111; -.
KEGG; cel:CELE_F18E9.5; -.
UCSC; F18E9.5a.2; c. elegans.
CTD; 181111; -.
WormBase; F18E9.5b; CE30958; WBGene00017571; jmjd-3.1.
eggNOG; KOG1246; Eukaryota.
eggNOG; ENOG410XR9J; LUCA.
GeneTree; ENSGT00410000025758; -.
InParanoid; Q95QK3; -.
KO; K11447; -.
OrthoDB; EOG091G0HAA; -.
PhylomeDB; Q95QK3; -.
Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
PRO; PR:Q95QK3; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00017571; -.
ExpressionAtlas; Q95QK3; baseline and differential.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); IDA:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0071557; P:histone H3-K27 demethylation; IDA:WormBase.
GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
InterPro; IPR003347; JmjC_dom.
Pfam; PF02373; JmjC; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
Chromatin regulator; Complete proteome; Dioxygenase; Iron;
Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Zinc.
CHAIN 1 1061 Lysine-specific demethylase jmjd-3.1.
/FTId=PRO_0000438800.
DOMAIN 760 923 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
REGION 369 417 Required for nuclear localization.
{ECO:0000269|PubMed:25124442}.
REGION 418 759 Required for binding of unc-3 and for
function in Y-to-PDA
transdifferentiation.
{ECO:0000269|PubMed:25124442}.
METAL 811 811 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 813 813 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 891 891 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 998 998 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1001 1001 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1025 1025 Zinc. {ECO:0000250|UniProtKB:O14607}.
METAL 1028 1028 Zinc. {ECO:0000250|UniProtKB:O14607}.
MUTAGEN 811 813 HME->TMG: Disruption of Y-to-PDA
transdifferentiation.
{ECO:0000269|PubMed:25124442}.
MUTAGEN 888 888 G->E: In fp11; loss of demethylase
activity and disruption of Y-to-PDA
transdifferentiation.
{ECO:0000269|PubMed:25124442}.
MUTAGEN 903 903 S->F: In fp25; loss of demethylase
activity and disruption of Y-to-PDA
transdifferentiation.
{ECO:0000269|PubMed:25124442}.
MUTAGEN 998 998 C->S: Disruption of Y-to-PDA
transdifferentiation; when associated
with S-1001; S-1025 and S-1028.
{ECO:0000269|PubMed:25124442}.
MUTAGEN 1001 1001 C->S: Disruption of Y-to-PDA
transdifferentiation; when associated
with S-998; S-1025 and S-1028.
{ECO:0000269|PubMed:25124442}.
MUTAGEN 1025 1025 C->S: Disruption of Y-to-PDA
transdifferentiation; when associated
with S-998; S-1001 and S-1028.
{ECO:0000269|PubMed:25124442}.
MUTAGEN 1028 1028 C->S: Disruption of Y-to-PDA
transdifferentiation; when associated
with S-998; S-1001 and S-1025.
{ECO:0000269|PubMed:25124442}.
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


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