ID A0A667HTN5_LYNCA Unreviewed; 414 AA.
AC A0A667HTN5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
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|Ensembl:ENSLCNP00005023750.1};
OS Lynx canadensis (Canada lynx) (Felis canadensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX NCBI_TaxID=61383 {ECO:0000313|Ensembl:ENSLCNP00005023750.1, ECO:0000313|Proteomes:UP000472241};
RN [1] {ECO:0000313|Ensembl:ENSLCNP00005023750.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSLCNP00005023750.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 2-oxoglutarate + O2 = (5S)-5-hydroxy-L-
CC lysyl-[protein] + succinate + CO2; 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:ARBA00048645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 2-
CC oxoglutarate + 2 O2 = L-arginyl-[protein] + 2 formaldehyde + 2
CC succinate + 2 CO2; Xref=Rhea:RHEA:58348, Rhea:RHEA-COMP:10532,
CC Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:88221;
CC Evidence={ECO:0000256|ARBA:ARBA00047382};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2-
CC oxoglutarate + O2 = N(omega)-methyl-L-arginyl-[protein] +
CC formaldehyde + succinate + CO2; Xref=Rhea:RHEA:58472, Rhea:RHEA-
CC COMP:11990, Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:65280, ChEBI:CHEBI:88221;
CC Evidence={ECO:0000256|ARBA:ARBA00048563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end methyltriphosphate-guanosine-ribonucleotide-snRNA +
CC 2-oxoglutarate + O2 = a 5'-end triphospho-guanosine-ribonucleotide-
CC snRNA + formaldehyde + succinate + CO2 + H(+); Xref=Rhea:RHEA:58784,
CC Rhea:RHEA-COMP:15220, Rhea:RHEA-COMP:15221, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:138278,
CC ChEBI:CHEBI:142789; Evidence={ECO:0000256|ARBA:ARBA00047985};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBUNIT: Homooligomerizes; requires lysyl-hydroxylase activity.
CC Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65. Interacts with CDK9 and
CC CCNT1; the interaction is direct with CDK9 and associates the P-TEFb
CC complex when active. Interacts (via JmjC and N-terminal domains) with
CC BRD4 (via NET domain); the interaction is stronger in presence of ssRNA
CC and recruits JMJD6 on distal enhancers. Interacts with ARGLU1;
CC interaction may be involved in ARGLU1-mediated modulation of
CC alternative splicing. {ECO:0000256|ARBA:ARBA00049700}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JMJD6 family.
CC {ECO:0000256|ARBA:ARBA00038068}.
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DR RefSeq; XP_030151616.1; XM_030295756.1.
DR AlphaFoldDB; A0A667HTN5; -.
DR Ensembl; ENSLCNT00005026525.1; ENSLCNP00005023750.1; ENSLCNG00005015428.1.
DR GeneID; 115500956; -.
DR CTD; 23210; -.
DR Proteomes; UP000472241; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0033749; F:histone H4R3 demethylase activity; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106140; F:P-TEFb complex binding; IEA:TreeGrafter.
DR GO; GO:0006909; P:phagocytosis; IEA:TreeGrafter.
DR FunFam; 1.20.1280.270:FF:000001; Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6; 1.
DR FunFam; 2.60.120.650:FF:000010; bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 isoform X2; 1.
DR Gene3D; 1.20.1280.270; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR050910; JMJD6_ArgDemeth/LysHydrox.
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;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
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:UP000472241};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 141..305
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 336..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..356
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 47662 MW; 5AA912FBF993965F CRC64;
MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESFSLNPA AVADNVERAD ALQLSVEEFV
ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK CGEDNDGYSV KMKMKYYIEY
MESTRDDSPL YIFDSSYGEH PKRRKLLEDY KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP
RSGTGIHIDP LGTSAWNALV QGHKRWCLFP TSTPRELIKV TREEGGNQQD EAITWFSIIH
PRTQLPTWPP EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK
TVRGRPKLSR KWYRILKQEH PELAVLADSV DLQESTGIAS DSSSDSSSSS SSSSSDSDSE
CESGSEGDGT THRRKKRRTC SMMGNGDTTS QDDCVSKERS SSRIRDTCGG RAHP
//
