ID L9JAX2_TUPCH Unreviewed; 1507 AA.
AC L9JAX2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN ORFNames=TREES_T100003395 {ECO:0000313|EMBL:ELW47691.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW47691.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR EMBL; KB321094; ELW47691.1; -; Genomic_DNA.
DR STRING; 246437.L9JAX2; -.
DR eggNOG; KOG1246; Eukaryota.
DR InParanoid; L9JAX2; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16874; ARID_KDM5B; 1.
DR CDD; cd15607; PHD2_KDM5B; 1.
DR CDD; cd15687; PHD3_KDM5B; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047981; KDM5B_ARID.
DR InterPro; IPR047979; KDM5B_PHD3.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:ELW47691.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:ELW47691.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 17..58
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 82..172
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 415..581
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1138..1186
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1447..1501
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 186..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1507 AA; 171812 MW; 078F344920ED0704 CRC64;
MHMDSGFSLG VGLEGECPVF EPSWEEFADP FAFIHKIRPI AEQTGICKVR PPPDWQPPFA
CDVDKLHFTP RIQRLNELEA QTRVKLNFLD QIAKYWELQG STLKIPHVER KILDLFQLNK
LVAEEGGFAV VCKDRKWTKI ATKMGFAPGK AVGSHIRGHY ERILNPYNLF LSGDSLRCLQ
KPNLTTDTKD KEYKPHDIPQ RQSVQPSETC PPARRAKRMR AESSSINHYA FFFCKGNIQY
MTPFLFLFIF FKAMNIKIEP EETTEARTHN LRRRMGCPTP KCENEKEMKS NVKQESIEKK
DYIVESEKEK PKSRSKKTTN AECSKPQEAF GFEQAARDYT LRTFGEMADA FKSDYFNMPV
HMVPTELVEK EFWRLVSTIE EDVTVEYGAD IASKEFGSGF PVRDGKVKLS PEEEEYLDSG
WNLNNMPVME QSVLAHITAD ICGMKLPWLY VGMCFSSFCW HIEDHWSYSI NYLHWGEPKT
WYGVPGYAAE QLENVMKKLA PELFVSQPDL LHQLVTIMNP NTLMTHEVPV YRTNQCAGEF
VITFPRAYHS GFNQGFNFAE AVNFCTVDWL PLGRQCVEHY RLLHRYCVFS HDEMICKMAS
KADVLDVVVA STVQKDMAIM IEDEKALRET VRKLGVIDSE RMDFELLPDD ERQCIKCKTT
CFMSAISCSC KPGLLVCLHH VKELCSCPPY KYKLRYRYTL DDLYPMMNAL KLRAESYNEW
ALNVNEALEA KINKKKSLFN FKALIEESEM KKFPDNDLLR HLRLVTQDAE KCASVAQQLL
NGKRQTRYRS GGGKSPNQLT VNELRQFVTQ LYALPCLLSQ TPLLKDLLNR VEDFQQHSQK
LLSEEMPSAA ELQDLLDVSF EFDVELPQLA EMRIRLEQAR WLEEVQQACL DPSSLTLDDM
RRLIDLGVGL APYSAVEKAM ARLQELLTVS EHWDDKAKSF LKARPRHSLS SLATAVKEIE
EIPAYLPNGA ALKDSVQKAR DWLQDVEALQ AGGRVPVLDT LVELVTRGRS IPVHLNSLPR
LESLVAEVQA WKECAASTFL TENSPYSLLE VLCPRCDIGL LGLKRKQRKL KEPLPSGKKK
STKLESLSDL ERALTESKET ASAMATLGEA RLREMEALQS LRLANEGKLL SPAQEVEMKV
CLCQKAPATP MIQCELCRDA FHTSCVAVPS AAQGPRIWLC PHCRRSEKPP LEKILPLLAS
LQRIRVRLPE GDALRYMIER TVNWQHRAQQ LLSSGNLKFV QDRLGSGLLL SRWQASAGQV
SETNKVSQPP GTTSFSLPDD WDNRTSYLHS PFSTGRSCIP LHGISPEVNE LLMEAQLLQV
SLPEIQELYQ TLLAKPSPAQ QTDRSSPVRP SSEKIDCCRG KRDGTNNGLE RKLKRRPERE
GLSSERWDRV KKMRTPKKKK IKLSPPKDMN NFKLERERSY ELVRSAETHS LPSDTSYSEQ
EDSEDEDAIC PAVSCLQPEG DEVDWVQCDG SCNQWFHQVC VGVSPEMAEK EDYVCVRCTV
KDAPSRK
//
