ID A0A096ML87_PAPAN Unreviewed; 1063 AA. AC A0A096ML87; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 12-OCT-2022, entry version 49. 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=KDM4A {ECO:0000313|Ensembl:ENSPANP00000000299}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000000299, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000000299, ECO:0000313|Proteomes:UP000028761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A., RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B., RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B., RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C., RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D., RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F., RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G., RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H., RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J., RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P., RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R., RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S., RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T., RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V., RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W., RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000000299} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. 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 -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family. CC {ECO:0000256|ARBA:ARBA00009711}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_003891797.1; XM_003891748.2. DR RefSeq; XP_009205076.1; XM_009206812.1. DR STRING; 9555.ENSPANP00000000299; -. DR Ensembl; ENSPANT00000004156.3; ENSPANP00000000299.1; ENSPANG00000013120.3. DR GeneID; 101010163; -. DR KEGG; panu:101010163; -. DR CTD; 9682; -. DR eggNOG; KOG0958; Eukaryota. DR GeneTree; ENSGT00940000159643; -. DR HOGENOM; CLU_001442_0_1_1; -. DR OMA; AQQPPYC; -. DR OrthoDB; 1186832at2759; -. DR Proteomes; UP000028761; Chromosome 1. DR Bgee; ENSPANG00000013120; Expressed in cornea and 66 other tissues. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl. DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IEA:Ensembl. DR GO; GO:0140684; F:histone H3-tri/dimethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC. DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl. DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0070544; P:histone H3-K36 demethylation; IEA:Ensembl. DR GO; GO:0033169; P:histone H3-K9 demethylation; IEA:Ensembl. DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IEA:Ensembl. DR CDD; cd04508; TUDOR; 2. DR Gene3D; 3.30.40.10; -; 2. DR InterPro; IPR034732; EPHD. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR003349; JmjN. DR InterPro; IPR040477; KDM4_Tudor_2. DR InterPro; IPR002999; Tudor. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF18104; Tudor_2; 2. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. DR SMART; SM00333; TUDOR; 2. DR SUPFAM; SSF57903; SSF57903; 1. 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 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:UP000028761}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 14..56 FT /note="JmjN" FT /evidence="ECO:0000259|PROSITE:PS51183" FT DOMAIN 142..308 FT /note="JmjC" FT /evidence="ECO:0000259|PROSITE:PS51184" FT DOMAIN 771..884 FT /note="PHD-type" FT /evidence="ECO:0000259|PROSITE:PS51805" FT REGION 358..384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 499..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 615..640 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 462..489 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 501..536 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1063 AA; 120606 MW; 9CDCE99EBBEB9128 CRC64; MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP KEWKPRASYD DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI ANSDKYCTPR YSEFEELERK YWKNLTFNPP IYGADVNGTL YEKHVDEWNI GRLRTILDLV EKESGITIEG VNTPYLYFGM WKTSFAWHTE DMDLYSINYL HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH KMTLISPLML KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG KQAVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDNTV IDHTLPTPEA AEFLKESELP PRAGNEEECP EEDMEGVEDG EEGDLKTSLA KHRIGTKRHR VCLEIPQEVS QSELFPKEEL SSEQYEMTEC PAALAPVRPT HSSVRQVEDG LTFPDYSDST EVKFEELKNV KLEEEDEEEE QEAAALDLSV NPASVGGRLV FSGSQKKSPS LGSGSSRDSI SSDSETSEPL SCRAQGQTGV LTVHSYAKGD GRVTVGEPCM RKKGSAARSI SERELAEVAD EYMFSLEENK KSKGRRQPLS KLPRHHPLVL QECVSDDETS EQLTPEEEAE ETEAWAKPLS QLWQNRPPNF EAEKEFNETM AQQAPHCAVC MIFQTYHQVE FGGFTQNCGN ASDLAPQKQR TKPLIPEMCF TSTGCSTDIN LSTPYLEEDG TSILVSCKKC SVRVHASCYG VPPAKASEDW MCSRCSANAL EEDCCLCSLR GGALQRANDD RWVHVSCAVA ILEARFVNIA ERSPVDVSKI PLPRFKLKCI FCKKRRKRTA GCCVQCSHGR CPTAFHVSCA QAAGVMMQPD DWPFVVFITC FRHKIPNLER AKGALQSITA GQKVISKHKN GRFYQCEVVR LTTETFYEVN FDDGSFSDNL YPEDIVSQDC LQLGPPAEGE VVQVRWTDGQ VYGAKFVASH PIQMYQVEFE DGSQLVVKRD DVYTLDEELP KRVKSRLSVA SDMRFNEIFT EKEVKQEKKR QRVINSRYRE DYIEPALYRA IME //