ID M4AV43_XIPMA Unreviewed; 1560 AA.
AC M4AV43;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000018338.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000018338.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000018338.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Ensembl; ENSXMAT00000018365.2; ENSXMAP00000018338.2; ENSXMAG00000018246.2.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000164196; -.
DR HOGENOM; CLU_000991_2_2_1; -.
DR Proteomes; UP000002852; 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 CDD; cd16875; ARID_KDM5C_5D; 1.
DR CDD; cd15604; PHD1_KDM5C_5D; 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); 1.
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; 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:SF43; LYSINE-SPECIFIC DEMETHYLASE 5C; 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; 1.
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; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 12..53
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 77..167
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 349..399
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 493..659
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 193..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1341..1375
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 215..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1560 AA; 177547 MW; EB1B0C5B0BD2F17A CRC64;
MEVEEFIPPP ECPVFEPSWE EFQDPLGYIA KIRPIAEKSG ICKIRPPPDW QPPFSVELEN
FHFTPRIQRL NELEAETRVK LNYLDRIARF WEIQGSSLKI PHIERRILDL YSLSKIVADE
GGFELICKER RWARIAQRLG YPPGKNIGSL LRSHYERIVY PFEMFQSGAS LTHCKPKHYD
GEDVDKEYKP HSIPLRQSVP PSKMNSYGRR ANRCQPDPEP TEEDIEKNPE LKKLQIYGAG
PKMMGLGLVA RDKGFKKKDD LPQTVTIKDA TLPASNDAHG DAPIKPEHLD PEEKQTDEGS
SNLQLPPLTV TVKTEVKKEE VKAEYGEDDG SKMTMRLRRN ITNPQCVDSF ICRMCGRGDD
DEKLLQCDSC DENYHTYCLL PPLTDPPKSK WRCPKCVAEE CKKPSEAFGF EQATREYTLQ
SFGEMADSFK ADYFNMPVHM VPTELVEREF WRLVSSIEED VTVEYGADIH SKEFGSGFPM
NNGKKELTKE EEEYARSGWN LNVMPVLEQS LLCHINGDIS GMKVPWLYVG MVFSTFCWHI
EDHWSYSINY LHWGEPKTWY GVPSAAAEQL EDVMKKLTPE LFEYQPDLLH QLVTIMNPNI
LMAHGVPVVR TNQCAGEFVI TFPRAYHSGF NQGYNFAEAV NFCTADWLPA GRHCIEHYRR
LRRYCVFSHE ELTCKMAACP EKLDLNLAAA THREMFIIVQ EERKLRKNLM ERGITEAERE
AFELLPDDER QCDKCKTTCF LSALACSNCP ERLVCLYHTQ DLCNCPTEKL YLRYRYTLDE
LLAMLHRLKV RSESFDSWAN RVKEALEQEE GHKIEILDLE KLKTEAAEKR FPDNELLRKL
NAVFKDIAFC HQKSAELLSN TKTGDDRMTL AELKSLVEKM QNLPCVIKHL KEVQVVLQTV
EDFRKQAQVL VNNKDWRKES PPPEQLQSLL EDGGKLPVVV PECNLLQGLK AQGHWLEEVR
HTLGTGGGEK HEVTLEVLRN LMEAGCNVAQ SVSVETAMAE LQELLTIAER WEEKAQICLE
QRQKHPLSTL EAIVNEAQLI PVKLPNIEAL RGCLTRAQAW VTDLEEIQNG EHYPCLDDLE
GLVAIGRDLP VLMEELRQLE LQVTSAHSWR DKATKTFLKK SSQHSLLEVL CPCVKRRERR
TEPEPLDETL DDSDSNTLGL SAQALRDPAA IVLAFKEGEH QEKEALLRLQ KLNLCKSGLS
SASCKENGRW DETMDTDTSY RSEDSVKETR NGSRSATAQS VCVCAGPPRA PQLRCYLCKD
WFHGGCVSFP SLLPPSSPQS NRLCWWDWDT RFLCPQCQRS RRPRLATILA LLVALQRLPV
RLPEGEALQC LTERAITWQG RAKEALEMPE LQRALQELQE LAEKEEQKEK DAEGNSVIVL
SDSEGGEGED GVIDLTEDSS PIKKTKELDA SQAECQNGIS KKSNVTGVES LLPLLPLLKG
RVVTLSPGAR EQLEKLQLEG DLLEVTLDQT YTIHRVLQAA SDPPRETLQT LIQIELEEQR
GARTSRGRPK DKRKRKGHRG SSADAAGHQP QDASQSKKTC PLKNSPTRPH SNVEIHPEIL
//
