ID W5PQS3_SHEEP Unreviewed; 1694 AA.
AC W5PQS3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:ENSOARP00000012800.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000012800.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000012800.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000012800.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000012800.1}
RP IDENTIFICATION.
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 EMBL; AMGL01083793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; W5PQS3; -.
DR STRING; 9940.ENSOARP00000012800; -.
DR PaxDb; 9940-ENSOARP00000012800; -.
DR Ensembl; ENSOART00000012987.1; ENSOARP00000012800.1; ENSOARG00000011934.1.
DR eggNOG; KOG1246; Eukaryota.
DR HOGENOM; CLU_000991_2_0_1; -.
DR OMA; GFDQVCK; -.
DR Proteomes; UP000002356; Chromosome 3.
DR Bgee; ENSOARG00000011934; Expressed in major salivary gland and 54 other cell types or tissues.
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; cd15602; PHD1_KDM5A; 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); 3.
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; IPR047973; KDM5A_PHD1.
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 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:UP000002356};
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 20..61
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 85..175
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 294..344
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 438..604
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1163..1220
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1611..1665
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1326..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1409..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1409..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1694 AA; 192349 MW; 70D15D60B458C40C CRC64;
VPLTPLAGVY AAEFVPPPEC PVFEPSWEEF TDPLSFIGRI RPMAEKTGIC KIRPPKDWQP
PFACEVKSFR FTPRVQRLNE LEAMTRVRLD FLDQLAKFWE LQGSTLKIPV VERKILDLYA
LSKIVASKGG FEMVTKEKKW SKVGSRLGYL PGKGTGSLLK SHYERILYPY ELFQSGVSLM
GVQMPNLDLK EKVEPEVLSA DVQTSPEPGT RMNILPKRTR RVKSQSESGE VNRNTELKKL
RIFGAGPKVV GLAMGVKEKE DEVSRRRKVT NRSDAFNMQM RQRKGTLSVN FVDLYVCMFC
GRGNNEDKLL LCDGCDDSYH TFCLIPPLPD VPKGDWRCPK CVAEECNKPR EAFGFEQAVR
EYTLQSFGEM ADNFKSDYFN MPVHMVPTEL VEKEFWRLVS SIEEDVIVEY GADISSKDFG
SGFPVKDGRR KMLPEEEEYA LSGWNLNNMP VLEQSVLAHI NVDISGMKVP WLYVGMCFSS
FCWHIEDHWS YSINYLHWGE PKTWYGVPSH AAEQLEEVMR ELAPELFESQ PDLLHQLVTI
MNPNVLMEHG VPVYRTNQCA GEFVVTFPRA YHSGFNQGYN FAEAVNFCTA DWLPIGRQCV
SHYRRLRRHC VFSHEELIFK MAADPECLDV GLAAMVCKEL TLLTEEETRL RESVMQMGVL
MSEEEVFELV PDDERQCSAC RTTCFLSALT CSCNPERLVC LYHPTDLCPC PMQKKCLRYR
YPLEDLPSLL YGVKVRAQSY DTWVSRVTEA LSANFSHKKG DLIELRVMLE DAEDRKYPEN
DLFRKLKDAV KEAETCASVA QLLLSKKQKH RQSPDGGRTR TKLTVEELKA FVQQLFSLPC
VISQARQVKN LLDDVEEFHE RAQEAMMDET PDSSKLQMLI DMGSSLYVEL PELARLKQEL
QQARWLDEVR LTLSDPQQVT LDVMKKLIDS GVGLAPHHAV EKAMAELQEL LTVSERWEEK
AKVCLQARPR HSVASLESIV NEAKSIPAFL PNVLSLKEAL QKAREWTTKV EAIQSGSNYA
YLEQLESLSA KGRPIPVRLD ALPQVESQVA AARAWRERTG RTFLKKNSSH TLLQVLSPRT
DIGIYGSGKN RRKKVKELIE KEKEKDLDLE PLSDLEEGLE ETRDAATVVA VFKEREQKEL
EAMHSLRAAN LAKMSMVDRI EDVKFCICRK TASGFMLQCE LCKDWFHNSC VPLPKSSSQK
KGSSWQAKEV KFLCPLCMRS RRPRLETILS LLVSLQKLPV RLPEGEALQC LTERAMSWQD
RARQALATDE LSSALAKLSV LSQRMVEQAA REKTEKIISA ELQKAAANPD LQGHLPSFQQ
SAFNRVASSV SSSPRQTADY DDEETDSDED IRETYGYDMK DTASVKSSSS LEPNLFCDEE
IPIKSEEVVT HMWTAPSFCA EHAYSSASKS CSQGKGSSTP RKQPRKSPLV PRSLEPPVLE
LSPGAKAQLE ELMMVGDLLE VSLDETQHIW RILQATHPPS EDRFLHIMED DSMEEKPLKI
KGKDSSEKKR KRKLEKVEQL FGEGKQKSKE LKKMDKPKKK KLKLSAEKSK ELNKLAKKLA
KEEERKKKKE KAAAAKVELV KESTEKKREK KVLDIPSKYD WSGAEESDDE NAVCAAQNCQ
RPCKDKVDWV QCDGGCDEWF HQVCVGVSPE MAESEDYICT NCAKKQGPDS PGPVPPPSFI
MSYKLPVEDL KETS
//
