JMJD6_MOUSE
ID JMJD6_MOUSE Reviewed; 403 AA.
AC Q9ERI5; A2AA26; A8Y5I2; Q80TX1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6;
DE EC=1.14.11.-;
DE AltName: Full=Histone arginine demethylase JMJD6;
DE AltName: Full=JmjC domain-containing protein 6;
DE AltName: Full=Jumonji domain-containing protein 6;
DE AltName: Full=Lysyl-hydroxylase JMJD6;
DE AltName: Full=Peptide-lysine 5-dioxygenase JMJD6;
DE AltName: Full=Phosphatidylserine receptor;
DE Short=Protein PTDSR;
GN Name=Jmjd6; Synonyms=Kiaa0585, Ptdsr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Swiss Webster; TISSUE=Brain;
RX PubMed=10811223; DOI=10.1038/35011084;
RA Fadok V.A., Bratton D.L., Rose D.M., Pearson A., Ezekewitz R.A.,
RA Henson P.M.;
RT "A receptor for phosphatidylserine-specific clearance of apoptotic cells.";
RL Nature 405:85-90(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14645847; DOI=10.1126/science.1087621;
RA Li M.O., Sarkisian M.R., Mehal W.Z., Rakic P., Flavell R.A.;
RT "Phosphatidylserine receptor is required for clearance of apoptotic
RT cells.";
RL Science 302:1560-1563(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=14715629; DOI=10.1182/blood-2003-09-3245;
RA Kunisaki Y., Masuko S., Noda M., Inayoshi A., Sanui T., Harada M.,
RA Sasazuki T., Fukui Y.;
RT "Defective fetal liver erythropoiesis and T lymphopoiesis in mice lacking
RT the phosphatidylserine receptor.";
RL Blood 103:3362-3364(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14729065; DOI=10.1016/j.yexcr.2003.09.023;
RA Cui P., Qin B., Liu N., Pan G., Pei D.;
RT "Nuclear localization of the phosphatidylserine receptor protein via
RT multiple nuclear localization signals.";
RL Exp. Cell Res. 293:154-163(2004).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15345036; DOI=10.1186/jbiol10;
RA Boese J., Gruber A.D., Helming L., Schiebe S., Wegener I., Hafner M.,
RA Beales M., Koentgen F., Lengeling A.;
RT "The phosphatidylserine receptor has essential functions during
RT embryogenesis but not in apoptotic cell removal.";
RL J. Biol. 3:15.1-15.18(2004).
RN [9]
RP REVIEW ON FUNCTION.
RX PubMed=15453906; DOI=10.1186/jbiol14;
RA Williamson P., Schlegel R.A.;
RT "Hide and seek: the secret identity of the phosphatidylserine receptor.";
RL J. Biol. 3:14.1-14.4(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH U2AF2.
RX PubMed=21300889; DOI=10.1073/pnas.1008098108;
RA Boeckel J.N., Guarani V., Koyanagi M., Roexe T., Lengeling A.,
RA Schermuly R.T., Gellert P., Braun T., Zeiher A., Dimmeler S.;
RT "Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic
RT sprouting and regulates splicing of VEGF-receptor 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3276-3281(2011).
RN [11]
RP INTERACTION WITH LIAT1.
RX PubMed=25369936; DOI=10.1073/pnas.1419587111;
RA Brower C.S., Rosen C.E., Jones R.H., Wadas B.C., Piatkov K.I.,
RA Varshavsky A.;
RT "Liat1, an arginyltransferase-binding protein whose evolution among
RT primates involved changes in the numbers of its 10-residue repeats.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4936-E4945(2014).
CC -!- FUNCTION: Dioxygenase that can both act as a arginine demethylase and a
CC lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-
CC hydroxylation on specific lysine residues of target proteins such as
CC U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-
CC hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity
CC of U2AF2/U2AF65. Hydroxylates its own N-terminus, which is required for
CC homooligomerization. In addition to peptidyl-lysine 5-dioxygenase
CC activity, may act as an RNA hydroxylase, as suggested by its ability to
CC bind single strand RNA. Also acts as an arginine demethylase which
CC preferentially demethylates asymmetric dimethylation. Demethylates
CC histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me),
CC including mono-, symmetric di- and asymmetric dimethylated forms,
CC thereby playing a role in histone code. However, histone arginine
CC demethylation may not constitute the primary activity in vivo. In
CC collaboration with BRD4, interacts with the positive transcription
CC elongation factor b (P-TEFb) complex in its active form to regulate
CC polymerase II promoter-proximal pause release for transcriptional
CC activation of a large cohort of genes. On distal enhancers, so called
CC anti-pause enhancers, demethylates both histone H4R3me2 and the methyl
CC cap of 7SKsnRNA leading to the dismissal of the 7SKsnRNA:HEXIM1
CC inhibitor complex. After removal of repressive marks, the complex
CC BRD4:JMJD6 attract and retain the P-TEFb complex on chromatin, leading
CC to its activation, promoter-proximal polymerase II pause release, and
CC transcriptional activation. Demethylates other arginine methylated-
CC proteins such as ESR1. Has no histone lysine demethylase activity (By
CC similarity). Required for differentiation of multiple organs during
CC embryogenesis (PubMed:15345036). Acts as a key regulator of
CC hematopoietic differentiation: required for angiogenic sprouting by
CC regulating the pre-mRNA splicing activity of U2AF2/U2AF65
CC (PubMed:21300889). Seems to be necessary for the regulation of
CC macrophage cytokine responses (By similarity).
CC {ECO:0000250|UniProtKB:Q6NYC1, ECO:0000269|PubMed:15345036,
CC ECO:0000269|PubMed:21300889}.
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:0000250|UniProtKB:Q6NYC1};
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:0000250|UniProtKB:Q6NYC1};
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:0000250|UniProtKB:Q6NYC1};
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:0000250|UniProtKB:Q6NYC1};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q6NYC1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6NYC1};
CC -!- SUBUNIT: Homooligomerizes; requires lysyl-hydroxylase activity (By
CC similarity). Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65
CC (PubMed:21300889). Interacts with LIAT1 (PubMed:25369936). Interacts
CC with CDK9 and CCNT1; the interaction is direct with CDK9 and associates
CC the P-TEFb complex when active. Interacts (via JmjC and N-terminal
CC domains) with BRD4 (via NET domain); the interaction is stronger in
CC presence of ssRNA and recruits JMJD6 on distal enhancers (By
CC similarity). {ECO:0000250|UniProtKB:Q6NYC1,
CC ECO:0000269|PubMed:21300889, ECO:0000269|PubMed:25369936}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:14729065}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q6NYC1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6NYC1}. Note=Mainly found throughout the
CC nucleoplasm outside of regions containing heterochromatic DNA, with
CC some localization in nucleolus. During mitosis, excluded from the
CC nucleus and reappears in the telophase of the cell cycle.
CC {ECO:0000250|UniProtKB:Q6NYC1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERI5-2; Sequence=VSP_014024, VSP_014025;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, eye, spinal
CC chord, thymus, lung, liver, kidney and intestine.
CC {ECO:0000269|PubMed:14645847, ECO:0000269|PubMed:15345036}.
CC -!- DEVELOPMENTAL STAGE: Expressed early in development. Expressed from
CC embryonic stem cells and throughout embryogenesis.
CC {ECO:0000269|PubMed:14645847, ECO:0000269|PubMed:15345036}.
CC -!- DOMAIN: The nuclear localization signal motifs are necessary and
CC sufficient to target it into the nucleus.
CC {ECO:0000250|UniProtKB:Q6NYC1}.
CC -!- PTM: Hydroxylates its own N-terminus; hydroxylation is required for
CC homooligomerization. {ECO:0000250|UniProtKB:Q6NYC1}.
CC -!- DISRUPTION PHENOTYPE: Mice display perinatal lethality, growth
CC retardation, severe anemia and a delay in terminal differentiation of
CC the kidney, intestine, liver and lungs during embryogenesis. Moreover,
CC eye development can be severely disturbed, ranging from defects in
CC retinal differentiation to complete unilateral or bilateral absence of
CC eyes. According to PubMed:14645847, mice are defective in removing
CC apoptotic cells, especially in the lung and brain, in which dead cells
CC accumulate, causing abnormal development and leading to neonatal
CC lethality. According to PubMed:14715629, mice lacking Jmjd6 display a
CC reduced number of macrophages and apoptotic cells in fetal liver. In
CC contrast, according to PubMed:15345036, mice show a normal engulfment
CC of apoptotic cells. The contradictory results concerning apoptosis and
CC macrophage function may be explained by the fact that the protein plays
CC a key role in hematopoietic differentiation.
CC {ECO:0000269|PubMed:14645847, ECO:0000269|PubMed:14715629,
CC ECO:0000269|PubMed:15345036}.
CC -!- SIMILARITY: Belongs to the JMJD6 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to constitute the phosphatidylserine
CC receptor, a receptor that mediates recognition of phosphatidylserine, a
CC specific marker only present at the surface of apoptotic cells.
CC Phosphatidylserine receptor probably participates in apoptotic cell
CC phagocytosis. This protein was identified using phage display
CC expressing mAb 217, an antibody that specifically recognizes
CC phosphatidylserine receptor. However, its nuclear localization and the
CC fact that mAb 217 antibody still recognizes the phosphatidylserine
CC receptor in mice lacking Jmjd6, strongly suggest that it does not
CC constitute the receptor for phosphatidylserine and is not involved in
CC apoptotic cell removal. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65599.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF304118; AAG27719.1; -; mRNA.
DR EMBL; AK122317; BAC65599.1; ALT_INIT; mRNA.
DR EMBL; AL645542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056629; AAH56629.1; -; mRNA.
DR CCDS; CCDS25678.1; -. [Q9ERI5-1]
DR RefSeq; NP_203971.2; NM_033398.2. [Q9ERI5-1]
DR AlphaFoldDB; Q9ERI5; -.
DR SMR; Q9ERI5; -.
DR BioGRID; 223601; 7.
DR STRING; 10090.ENSMUSP00000047570; -.
DR iPTMnet; Q9ERI5; -.
DR PhosphoSitePlus; Q9ERI5; -.
DR EPD; Q9ERI5; -.
DR MaxQB; Q9ERI5; -.
DR PaxDb; Q9ERI5; -.
DR PRIDE; Q9ERI5; -.
DR ProteomicsDB; 269122; -. [Q9ERI5-1]
DR ProteomicsDB; 269123; -. [Q9ERI5-2]
DR Antibodypedia; 3874; 448 antibodies from 41 providers.
DR Ensembl; ENSMUST00000047616; ENSMUSP00000047570; ENSMUSG00000056962. [Q9ERI5-1]
DR GeneID; 107817; -.
DR KEGG; mmu:107817; -.
DR UCSC; uc007mmi.1; mouse. [Q9ERI5-1]
DR UCSC; uc007mmj.1; mouse. [Q9ERI5-2]
DR CTD; 23210; -.
DR MGI; MGI:1858910; Jmjd6.
DR VEuPathDB; HostDB:ENSMUSG00000056962; -.
DR eggNOG; KOG2130; Eukaryota.
DR GeneTree; ENSGT00940000156867; -.
DR InParanoid; Q9ERI5; -.
DR OMA; DLFKYCG; -.
DR PhylomeDB; Q9ERI5; -.
DR TreeFam; TF314988; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 107817; 21 hits in 82 CRISPR screens.
DR ChiTaRS; Jmjd6; mouse.
DR PRO; PR:Q9ERI5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9ERI5; protein.
DR Bgee; ENSMUSG00000056962; Expressed in ear vesicle and 263 other tissues.
DR ExpressionAtlas; Q9ERI5; baseline and differential.
DR Genevisible; Q9ERI5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0032451; F:demethylase activity; ISS:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; ISS:UniProtKB.
DR GO; GO:0033746; F:histone H3-methyl-arginine-2 demethylase activity; ISS:UniProtKB.
DR GO; GO:0033749; F:histone H3-methyl-arginine-3 demethylase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0035515; F:oxidative RNA demethylase activity; ISS:UniProtKB.
DR GO; GO:0106140; F:P-TEFb complex binding; ISO:MGI.
DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR GO; GO:0140537; F:transcription regulator activator activity; ISS:UniProtKB.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0070078; P:histone H3-R2 demethylation; IEA:Ensembl.
DR GO; GO:0070079; P:histone H4-R3 demethylation; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0042116; P:macrophage activation; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0035513; P:oxidative RNA demethylation; ISS:UniProtKB.
DR GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; ISS:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006482; P:protein demethylation; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:MGI.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Cytoplasm;
KW Developmental protein; Differentiation; Dioxygenase; Iron; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Oxidoreductase;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..403
FT /note="Bifunctional arginine demethylase and lysyl-
FT hydroxylase JMJD6"
FT /id="PRO_0000129370"
FT DOMAIN 141..305
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 336..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..10
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT MOTIF 91..95
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT MOTIF 141..145
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT MOTIF 167..170
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT MOTIF 373..378
FT /note="Nuclear localization signal 5"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT COMPBIAS 336..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 197
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 285
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT VAR_SEQ 270..298
FT /note="GWWHVVLNLDTTIAITQNFASSTNFPVVW -> IDELEETIPVRPSSDWSGL
FT VLYCHFGVES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_014024"
FT VAR_SEQ 299..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_014025"
FT CONFLICT 43
FT /note="P -> S (in Ref. 1; AAG27719 and 4; AAH56629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 46567 MW; D440E880B2F1BB37 CRC64;
MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESYPLNPA 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
