JMJD4_MOUSE
ID JMJD4_MOUSE Reviewed; 427 AA.
AC Q8BFT6; Q4QQM9; Q80ZI5; Q8BPV8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase JMJD4 {ECO:0000250|UniProtKB:Q9H9V9};
DE EC=1.14.11.-;
DE AltName: Full=JmjC domain-containing protein 4;
DE AltName: Full=Jumonji domain-containing protein 4;
DE AltName: Full=Lysyl-hydroxylase JMJD4 {ECO:0000250|UniProtKB:Q9H9V9};
GN Name=Jmjd4;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Embryo, Eye, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27147518; DOI=10.1002/mrd.22654;
RA Yoo H., Son D., Lee Y.J., Hong K.;
RT "Mouse JMJD4 is dispensable for embryogenesis.";
RL Mol. Reprod. Dev. 83:588-593(2016).
CC -!- FUNCTION: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl
CC hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational
CC termination efficiency of ETF1 (By similarity). Not essential for
CC embryonic stem cell (ESC) maintenance and the embryonic and postnatal
CC development (PubMed:27147518). {ECO:0000250|UniProtKB:Q9H9V9,
CC ECO:0000269|PubMed:27147518}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-
CC [protein] + CO2 + succinate; Xref=Rhea:RHEA:57156, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15084, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:141495;
CC Evidence={ECO:0000250|UniProtKB:Q9H9V9};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q9H9V9};
CC -!- SUBUNIT: Interacts with ETF1 (By similarity). Interacts with the ETF1-
CC GSPT1 complex (By similarity). {ECO:0000250|UniProtKB:Q9H9V9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9V9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BFT6-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8BFT6-3; Sequence=VSP_026326;
CC Name=4;
CC IsoId=Q8BFT6-4; Sequence=VSP_026327, VSP_026328;
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate and
CC are healthy, fertile and physiologically normal (PubMed:27147518).
CC Embryonic stem cells (ESCs) exhibit normal colony morphology and cell
CC proliferation rates and maintain normal expression of pluripotent genes
CC (PubMed:27147518). {ECO:0000269|PubMed:27147518}.
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DR EMBL; AK037954; BAC29907.1; -; mRNA.
DR EMBL; AK052144; BAC34856.1; -; mRNA.
DR EMBL; AK079104; BAC37541.1; -; mRNA.
DR EMBL; AK145394; BAE26409.1; -; mRNA.
DR EMBL; AL592522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX255278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049148; AAH49148.1; -; mRNA.
DR EMBL; BC116707; AAI16708.1; -; mRNA.
DR EMBL; BC118020; AAI18021.1; -; mRNA.
DR CCDS; CCDS24768.1; -. [Q8BFT6-1]
DR CCDS; CCDS56777.1; -. [Q8BFT6-3]
DR RefSeq; NP_001191997.1; NM_001205068.1. [Q8BFT6-3]
DR RefSeq; NP_848774.1; NM_178659.6. [Q8BFT6-1]
DR AlphaFoldDB; Q8BFT6; -.
DR STRING; 10090.ENSMUSP00000104407; -.
DR PhosphoSitePlus; Q8BFT6; -.
DR EPD; Q8BFT6; -.
DR PaxDb; Q8BFT6; -.
DR PRIDE; Q8BFT6; -.
DR ProteomicsDB; 269366; -. [Q8BFT6-1]
DR ProteomicsDB; 269367; -. [Q8BFT6-3]
DR ProteomicsDB; 269368; -. [Q8BFT6-4]
DR Antibodypedia; 20772; 295 antibodies from 30 providers.
DR DNASU; 194952; -.
DR Ensembl; ENSMUST00000045279; ENSMUSP00000043473; ENSMUSG00000036819. [Q8BFT6-3]
DR Ensembl; ENSMUST00000108777; ENSMUSP00000104407; ENSMUSG00000036819. [Q8BFT6-1]
DR Ensembl; ENSMUST00000147163; ENSMUSP00000123531; ENSMUSG00000036819. [Q8BFT6-4]
DR GeneID; 194952; -.
DR KEGG; mmu:194952; -.
DR UCSC; uc007jdu.2; mouse. [Q8BFT6-1]
DR UCSC; uc007jdw.2; mouse. [Q8BFT6-3]
DR CTD; 65094; -.
DR MGI; MGI:2144404; Jmjd4.
DR VEuPathDB; HostDB:ENSMUSG00000036819; -.
DR eggNOG; KOG2131; Eukaryota.
DR GeneTree; ENSGT00940000159380; -.
DR HOGENOM; CLU_016785_2_2_1; -.
DR InParanoid; Q8BFT6; -.
DR OMA; MFSRRFT; -.
DR OrthoDB; 609279at2759; -.
DR PhylomeDB; Q8BFT6; -.
DR TreeFam; TF105936; -.
DR BioGRID-ORCS; 194952; 0 hits in 76 CRISPR screens.
DR PRO; PR:Q8BFT6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BFT6; protein.
DR Bgee; ENSMUSG00000036819; Expressed in ear vesicle and 150 other tissues.
DR Genevisible; Q8BFT6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106156; F:peptidyl-lysine 4-dioxygenase activity; IEA:RHEA.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; ISS:UniProtKB.
DR GO; GO:0018126; P:protein hydroxylation; ISS:UniProtKB.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..427
FT /note="2-oxoglutarate and iron-dependent oxygenase JMJD4"
FT /id="PRO_0000291960"
FT DOMAIN 147..306
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 196
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 274
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT VAR_SEQ 190..202
FT /note="WSPFHADIFRSFS -> C (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026326"
FT VAR_SEQ 191..200
FT /note="SPFHADIFRS -> RGGSPPGLPW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026327"
FT VAR_SEQ 201..427
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026328"
SQ SEQUENCE 427 AA; 49152 MW; EFBDCBB941333AAE CRC64;
MDRETRTFAE RYYRDLRDPV PSGGGGPTPS GVTFIQTPNA FSYADFVKGF LLPNLPCVFS
SAFTEGWGSR RRWVTSEGKP DFEYLQQKYG DAVVPVANCG VREYNSNPKE HMSFRDYISY
WKDYIQGSYS SSRGCLYLKD WHLCRDSLVN DLEDIFTLPV YFSSDWLNEF WDVLNVDDYR
FVYAGPRGTW SPFHADIFRS FSWSVNICGK KKWLFFPPGE EEALRDCHGN LPYDVTSTEL
LDTHLYPKIQ HHSLPIEVIQ EPGEMVFVPS GWHHQVYNLD DTISINHNWV NGCNLPNMWH
FLQQELQAVQ HEVEEWKDSM PDWHHHCQVI MKSCTGINFE EFYHFLKVIA EKRLLVLEQG
LKGDSGDSRS LDLGLQQAAF DIGRLADVLA SVVVNPDFQR VDTSAFSPQP EELLQQLEDA
VAAAEAL
