ID A6HKZ3_RAT Unreviewed; 403 AA. AC A6HKZ3; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 27-MAR-2024, entry version 5. DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 {ECO:0000256|ARBA:ARBA00039354}; DE AltName: Full=Histone arginine demethylase JMJD6 {ECO:0000256|ARBA:ARBA00041379}; DE AltName: Full=JmjC domain-containing protein 6 {ECO:0000256|ARBA:ARBA00042860}; DE AltName: Full=Jumonji domain-containing protein 6 {ECO:0000256|ARBA:ARBA00042719}; DE AltName: Full=Lysyl-hydroxylase JMJD6 {ECO:0000256|ARBA:ARBA00041767}; DE AltName: Full=Peptide-lysine 5-dioxygenase JMJD6 {ECO:0000256|ARBA:ARBA00042996}; DE AltName: Full=Phosphatidylserine receptor {ECO:0000256|ARBA:ARBA00042876}; GN Name=Jmjd6 {ECO:0000313|RGD:1305395}; GN ORFNames=rCG_35128 {ECO:0000313|EMBL:EDM06699.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:EDM06699.1, ECO:0000313|Proteomes:UP000234681}; RN [1] {ECO:0000313|EMBL:EDM06699.1, ECO:0000313|Proteomes:UP000234681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BN, Sprague-Dawley {ECO:0000313|Proteomes:UP000234681}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F., RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 2-oxoglutarate + N(omega),N(omega)'-dimethyl-L-arginyl- CC [protein] + 2 O2 = 2 CO2 + 2 formaldehyde + L-arginyl-[protein] + 2 CC succinate; Xref=Rhea:RHEA:58348, Rhea:RHEA-COMP:10532, Rhea:RHEA- CC COMP:11992, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29965, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:88221; Evidence={ECO:0000256|ARBA:ARBA00036511}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = (5S)-5-hydroxy-L- CC lysyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:58360, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:15144, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:141843; CC Evidence={ECO:0000256|ARBA:ARBA00035940}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(omega),N(omega)'-dimethyl-L-arginyl- CC [protein] + O2 = CO2 + formaldehyde + N(omega)-methyl-L-arginyl- CC [protein] + succinate; Xref=Rhea:RHEA:58472, Rhea:RHEA-COMP:11990, CC Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:65280, ChEBI:CHEBI:88221; CC Evidence={ECO:0000256|ARBA:ARBA00036252}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + a 5'-end methyltriphosphate-guanosine- CC ribonucleotide-snRNA + O2 = a 5'-end triphospho-guanosine- CC ribonucleotide-snRNA + CO2 + formaldehyde + H(+) + succinate; CC Xref=Rhea:RHEA:58784, Rhea:RHEA-COMP:15220, Rhea:RHEA-COMP:15221, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:138278, ChEBI:CHEBI:142789; CC Evidence={ECO:0000256|ARBA:ARBA00036280}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|ARBA:ARBA00001954}; CC -!- SIMILARITY: Belongs to the JMJD6 family. CC {ECO:0000256|ARBA:ARBA00038068}. 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 EMBL; CH473948; EDM06699.1; -; Genomic_DNA. DR RefSeq; NP_001012143.2; NM_001012143.2. DR SMR; A6HKZ3; -. DR GeneID; 360665; -. DR KEGG; rno:360665; -. DR CTD; 23210; -. DR RGD; 1305395; Jmjd6. DR Proteomes; UP000234681; Chromosome 10. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR Gene3D; 1.20.1280.270; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR InterPro; IPR003347; JmjC_dom. DR PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1. DR PANTHER; PTHR12480:SF32; BIFUNCTIONAL ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD6; 1. DR Pfam; PF02373; JmjC; 1. DR SMART; SM00558; JmjC; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. PE 3: Inferred from homology; FT DOMAIN 141..305 FT /note="JmjC" FT /evidence="ECO:0000259|PROSITE:PS51184" FT REGION 336..403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 336..360 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 403 AA; 46540 MW; 629EE773BD0DB737 CRC64; MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESYPLSPA AVPDNVERAD ALQLSVKEFV ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK CGEDNDGYSV KMKMKYYIEY MESTRDDSPL YIFDSSYGEH PKRRKLLEDY KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP RSGTGIHIDP LGTSAWNALV QGHKRWCLFP TNTPRELIKV TREEGGNQQD EAITWFNVIY PRTQLPTWPP EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK TVRGRPKLSR KWYRILKQEH PELAVLADAV DLQESTGIAS DSSSDSSSSS SSSSSDSDSE CESGSEGDGT THRRKKRRTC SMVGNGDTTS QDDCVSKERS SSR //