ID M3ZQT1_XIPMA Unreviewed; 1681 AA.
AC M3ZQT1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
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 Name=KDM5A {ECO:0000313|Ensembl:ENSXMAP00000004574.2};
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:ENSXMAP00000004574.2, 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:ENSXMAP00000004574.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000004574.2};
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 STRING; 8083.ENSXMAP00000004574; -.
DR Ensembl; ENSXMAT00000004579.2; ENSXMAP00000004574.2; ENSXMAG00000004521.2.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000157170; -.
DR HOGENOM; CLU_000991_2_0_1; -.
DR InParanoid; M3ZQT1; -.
DR OMA; GFDQVCK; -.
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; cd16873; ARID_KDM5A; 1.
DR CDD; cd15515; PHD1_KDM5A_like; 1.
DR CDD; cd15606; PHD2_KDM5A; 1.
DR CDD; cd15686; PHD3_KDM5A; 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; IPR047974; KDM5A_ARID.
DR InterPro; IPR047970; KDM5A_PHD2.
DR InterPro; IPR047972; KDM5A_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:SF17; LYSINE-SPECIFIC DEMETHYLASE 5A; 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; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
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; 3.
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 23..64
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 88..178
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 264..314
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 408..574
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1132..1192
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1573..1627
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1291..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1508..1549
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1681 AA; 191046 MW; F357ED18A0D4127A CRC64;
MTCFPRIHFD MAAFAEFVPP PECPVFEPSW EEFSDPLGFI NKIRPIAEKT GICKIRPPQD
WQPPFACDVR NFRFTPRVQR LNELEALTRV KLNFLDQIAK FWELQGSKIR FPHVERKILD
LYQLSKIVSS EGGFETVCKE KRWSKVATRM GFPPGKGTGS LLRSHYERFL YPYELFQSGA
TLTVSGARRS TDLLPSIGIR LFYSFLLILS PQRENKEPTS LKIFGTSPKM VGLEIVSAGK
LFYCFFKCNL QTSGGLIRFC TIDLYFCLVC GRGDEEDRLL LCDGCDDSYH TFCLIPPLQD
VPKGDWRCPK CVAEECSKPR EAFGFEQAVR EYTLQSFGEM ADHFKSDYFN MPVHMVPTEL
VEKEFWRLVS SIEEDVIVEY GADISSKDVG SGFPIKDGKR RLLGDEEEYA NSGWNLNNMP
VLEQSVLTHI NVDISGMKVP WLYVGMCFSS FCWHIEDHWS YSINFLHWGE PKTWYGVPAS
AAEKLEAVMK KLAPELFDSQ PDLLHQLVTI MNPNVLMDHG VPVYRTNQCA GEFVVTFPRA
YHSGFNQGYN FAEAVNFCTA DWLPLGRQCV AHYRRLHRYC VFSHEELLCK MVADPENLDV
ELAAAVFKEM DDMIEEETKL RQAVQEMGVL SSEQEVFELV PDDERQCYKC KTTCFLSALT
CSCSPDRLVC LHHAKDLCDC PLGSKCLRYR YGLEEFPSML YGVKTRAQSY DTWAKRVAEA
LAADQKNKKD LIELKVLLED AEDRKYPENV LFRRLREMVK EAETCSSVAQ LLLSRKQRHS
RLRSDSSRNR TKLTVDELKA FVEQLFRLPC IISQARQVKE LLETVEDFHE RAQVALSDEM
PDSSKLQELL DLGSGLDVEL PELPKLKQEL QQARWLDEVR GTLAEPHRVT LELMKRLIDS
GVGLAPHHAV EKAMAELQEV LTVSERWEDK ARACLQARPR HSMVTLENIV LEARNIPAYL
PNVLALEEAL QKAKDWTSKV EAIHSGSSYA YLEQLESLLA RGRSIPVRLD LLGQVESQVA
SARAWRERTA RTFLKKNSTY TLLQVLSPRV DIGVYSNSKS KRKRVKELME KERSGYDPDA
LSDLEENLEE ARDPSAVVAA FKAKEQKEVE AIHSLRAANL AKMAMADHIE EVKFCLCRKT
ASGFMLQCEL CKDWFHGACV PLPKTGTQKK VGVSWQSNSK DSKFLCPLCQ RSRRPRLETI
LSLLVSLQKL PVRLPEGEAL QCLTERAMSW QDRARQALAT EELSSALAKL SVLSQRMVEQ
AAREKTEKII NAELLKAAAN PDLQGHIQTF QQSGFSRAAS PRPSVDYDDE ETDSDEDIRE
TYGYDMKDPG EVKPYLFCDE EIPVKSEEVV SHMWPAATPS FCAEHAYSSA SKSCVQNLST
PRKQPRKTPL VPRSLEPPVL ELSLQAKAQL EDLMMLGDLL EVSLDETQHI WRILQATHPP
SEERFLQVME PDNSLLEKPL KIKFKDSEKK RKRKLERAEQ LQKSKELKRV GLELGLGSKP
KKKKLKLNLE KNREMKQLAK RLAKEEKERK RKEKAAAKAE AIKDVLEKRK EKKILDIPSK
YDWSGAEDSN DENAVCAAKN CQRPCKDKVD WVQCDGGCDE WFHQVCVGVS CEMAENEDYI
CVDCSEKAAG AVDTVALEDV AGESIVVLSP CGTAAAMAPW SAVSLLNPAA SHQQQEPRQD
S
//
