ID JMJD4_DROME Reviewed; 425 AA.
AC Q9VJ97;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase JMJD4 homolog {ECO:0000250|UniProtKB:Q9H9V9};
DE EC=1.14.11.-;
DE AltName: Full=JmjC domain-containing protein 4 homolog;
DE AltName: Full=Jumonji domain-containing protein 4 homolog {ECO:0000312|FlyBase:FBgn0032671};
DE AltName: Full=Lysyl-hydroxylase JMJD4 homolog {ECO:0000250|UniProtKB:Q9H9V9};
GN Name=JMJD4 {ECO:0000312|FlyBase:FBgn0032671};
GN ORFNames=CG7200 {ECO:0000312|FlyBase:FBgn0032671};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q9H9V9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9V9}.
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DR EMBL; AE014134; AAF53656.1; -; Genomic_DNA.
DR EMBL; AY051684; AAK93108.1; -; mRNA.
DR RefSeq; NP_001286031.1; NM_001299102.1.
DR RefSeq; NP_609870.1; NM_136026.4.
DR AlphaFoldDB; Q9VJ97; -.
DR SMR; Q9VJ97; -.
DR BioGRID; 61085; 5.
DR IntAct; Q9VJ97; 1.
DR STRING; 7227.FBpp0310373; -.
DR PaxDb; 7227-FBpp0080615; -.
DR DNASU; 35089; -.
DR EnsemblMetazoa; FBtr0081062; FBpp0080615; FBgn0032671.
DR EnsemblMetazoa; FBtr0343823; FBpp0310373; FBgn0032671.
DR GeneID; 35089; -.
DR KEGG; dme:Dmel_CG7200; -.
DR UCSC; CG7200-RA; d. melanogaster.
DR AGR; FB:FBgn0032671; -.
DR CTD; 65094; -.
DR FlyBase; FBgn0032671; JMJD4.
DR VEuPathDB; VectorBase:FBgn0032671; -.
DR eggNOG; KOG2131; Eukaryota.
DR HOGENOM; CLU_016785_2_2_1; -.
DR InParanoid; Q9VJ97; -.
DR OMA; MFSRRFT; -.
DR OrthoDB; 120564at2759; -.
DR PhylomeDB; Q9VJ97; -.
DR Reactome; R-DME-9629569; Protein hydroxylation.
DR BioGRID-ORCS; 35089; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG7200; fly.
DR GenomeRNAi; 35089; -.
DR PRO; PR:Q9VJ97; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032671; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other cell types or tissues.
DR ExpressionAtlas; Q9VJ97; baseline and differential.
DR Genevisible; Q9VJ97; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
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:0045905; P:positive regulation of translational termination; ISS:UniProtKB.
DR GO; GO:0018126; P:protein hydroxylation; ISS:UniProtKB.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12480:SF6; 2-OXOGLUTARATE AND IRON-DEPENDENT OXYGENASE JMJD4; 1.
DR PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..425
FT /note="2-oxoglutarate and iron-dependent oxygenase JMJD4
FT homolog"
FT /id="PRO_0000291963"
FT DOMAIN 165..316
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 212
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 214
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
SQ SEQUENCE 425 AA; 49169 MW; AEE20D162CEFD758 CRC64;
MASEERDGDV LLQLHPEEVV ETDPQLPEEI ERCSGLDYND FFWRYMHKNI PVIIANVSND
WECQNWTVGQ SSPESRDLNS NPSASSINFD YLKTKISDGP VPVANCNSSY FNSHTKLELN
FHDYLAKWRS SIESQSSAAW TSAEVNSNVA PASGDNLYLK DWHLAAQMPG YNFYKVPKYF
ASDWLNEQLI QQGKDDYRFV YMGPKNSWTS YHADVFGSFS WSTNIVGLKK WLIMPPGEEL
KLNDRLGNLP FSIDEKMLDE HNVRYYTINQ RANEAVFVPS GWFHQVWNLT DTISVNHNWF
NGCNISMVWQ NLKNNLKAVC NEISDCQQMD NFEAHCQTML RASFGINYLD FIELLEFIAA
RRLAEGTVAT KFLLFDSYTM NDYHVQYDLE CLWKITRTLT EDPTIQCSPL QLEDRCQGLL
ARLEF
//
