ID U3I8K6_ANAPP Unreviewed; 390 AA.
AC U3I8K6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Jumonji domain containing 6, arginine demethylase and lysine hydroxylase {ECO:0000313|Ensembl:ENSAPLP00000003577.2};
GN Name=JMJD6 {ECO:0000313|Ensembl:ENSAPLP00000003577.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000003577.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000003577.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000003577.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; U3I8K6; -.
DR STRING; 8840.ENSAPLP00000003577; -.
DR Ensembl; ENSAPLT00000004179.2; ENSAPLP00000003577.2; ENSAPLG00000004061.2.
DR GeneTree; ENSGT00940000156867; -.
DR HOGENOM; CLU_016785_8_0_1; -.
DR OMA; NAWVAMR; -.
DR Proteomes; UP000016666; Chromosome 19.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0033746; F:histone H3R2 demethylase activity; IEA:Ensembl.
DR GO; GO:0033749; F:histone H4R3 demethylase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005506; F:iron ion binding; IEA:Ensembl.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; IEA:Ensembl.
DR GO; GO:0106140; F:P-TEFb complex binding; IEA:Ensembl.
DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0140537; F:transcription regulator activator activity; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0032463; P:negative regulation of protein homooligomerization; IEA:Ensembl.
DR GO; GO:0140694; P:non-membrane-bounded organelle assembly; IEA:Ensembl.
DR GO; GO:0035513; P:oxidative RNA demethylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0043654; P:recognition of apoptotic cell; IEA:Ensembl.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT DOMAIN 117..281
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 312..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 390 AA; 44802 MW; 034C6066B1A75526 CRC64;
MLKAVPTFCI LRVPLSVPQD NVERADALQL TVEEFVERYE KPYKPVVLLN AQVGWSAQEK
WTLERLKRKY RNQKFKCGED NDGYSVKMKM KYYIEYMETT RDDSPLYIFD SSYGEHPKRR
KLLEDYKVPK FFTDDLFQYA GEKRRPPYRW FVMGPPRSGT GIHIDPLGTS AWNALVQGHK
RWCLFPTSTP RELIKVTREE GGNQQDEAIT WFNVIYPRTQ LPTWPPEFKP LEILQKPGET
VFVPGGWWHV VLNLDTTIAI TQNFASCTNF PVVWHKTVRG RPKLSRKWYR ILKQEHPDLA
ALADSVDLQE STGIASDSSS DSSSSSSSSS SDSDSECDSG SETEGMMHRR KKRRTCSMMG
NGDTTSQDDC VSKERSSSRI RESCGGRSYP
//
