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Database: UniProt
Entry: A0A3Q2HAR2_HORSE
LinkDB: A0A3Q2HAR2_HORSE
Original site: A0A3Q2HAR2_HORSE 
ID   A0A3Q2HAR2_HORSE        Unreviewed;      1053 AA.
AC   A0A3Q2HAR2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE            EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN   Name=KDM4C {ECO:0000313|Ensembl:ENSECAP00000030682.2,
GN   ECO:0000313|VGNC:VGNC:19338};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000030682.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000030682.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030682.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000030682.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030682.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC         [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC         lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC         COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC         EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
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 JHDM3 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00009711}.
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DR   RefSeq; XP_005605058.1; XM_005605001.2.
DR   AlphaFoldDB; A0A3Q2HAR2; -.
DR   SMR; A0A3Q2HAR2; -.
DR   Ensembl; ENSECAT00000030189.3; ENSECAP00000030682.2; ENSECAG00000024063.4.
DR   GeneID; 100060699; -.
DR   VGNC; VGNC:19338; KDM4C.
DR   GeneTree; ENSGT00940000154930; -.
DR   Proteomes; UP000002281; Chromosome 23.
DR   Bgee; ENSECAG00000024063; Expressed in cerebellum and 23 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q2HAR2; baseline.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd15715; ePHD_JMJD2C; 1.
DR   CDD; cd15577; PHD_JMJD2C; 1.
DR   CDD; cd20465; Tudor_JMJD2C_rpt1; 1.
DR   CDD; cd20468; Tudor_JMJD2C_rpt2; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.10.330.70; -; 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; IPR034732; EPHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR003349; JmjN.
DR   InterPro; IPR040477; KDM4-like_Tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   PANTHER; PTHR10694:SF104; LYSINE-SPECIFIC DEMETHYLASE 4C; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF13831; PHD_2; 1.
DR   Pfam; PF18104; Tudor_2; 2.
DR   Pfam; PF13832; zf-HC5HC2H_2; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00333; TUDOR; 2.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          16..58
FT                   /note="JmjN"
FT                   /evidence="ECO:0000259|PROSITE:PS51183"
FT   DOMAIN          144..310
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          749..862
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51805"
FT   REGION          367..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  118948 MW;  952495E731F45BF2 CRC64;
     MEEAEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC
     YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSGKYCT PRYLDYEDLE
     RKYWKNLTFV APIYGADING SIYDEGVDEW NIARLNTVLD VVEEECGISI EGVNTPYLYF
     GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL
     RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
     YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP ESTPEVKAWL
     QRRRKVRKAS KSFQGTSSQS KRPKNEEDGE VLAAVEGAEG PTSDPHPDDL KASEKPEAAA
     KLGNTQAPSE EDASASRMQL DQNSSENIRL SGNSCSSTSI MEETKTENDQ ACVTIPPSNP
     SEADNSASSG HVTSEELDPP KLPWPKSPES CSSMAESNSV LTEGEESDVE SRGSGLEPGE
     VPAVPSGERN GFKVPTRIEG ETKTAKSWRH PLSKPPARSP MTLVKQQATS DEELLEVPSI
     EEEVEETESW AKPLVHLWQT KSPNFAAEQE YNAAVARMEP HCAICALLMP YYKPDSSNEE
     NDSRWETKLD EVVTSGGKTK PLIPEMCFIY SEENIEYSPP NAFLEEDGTS LLISCAKCCV
     RVHASCYGIP SHEICDGWLC ARCKRNAWSA ECCLCNLRGG ALKETKNNKW AHVMCAVAVP
     EVRFTNVPER TQIDVGRIPL QRLKLKCIFC RHRVKKVSGA CIQCSYGRCP ASFHVTCAHA
     AGVLMEPDDW PYVVNITCFR HKVNPNVKSK AGEKGISVGQ TVITKHRNTR YYSCRVMAVT
     SQTFYEVVFD DGSFSRDTFP EDIVSRDCVK LGPPAEGEVV QVKWPDGKLY GAKYLGSNVA
     HMYQVEFEDG SQIAMKREDI YTLDEELPKR VKARFSTASD MRFEDTFYGA DIIQGEKKRQ
     RVLSSRFKNE YVDDPVYRTF LKSSFQKKCQ KRQ
//
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