JMJD4_DANRE
ID JMJD4_DANRE Reviewed; 422 AA.
AC Q08BY5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
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; ORFNames=zgc:153974;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q9H9V9}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9V9}.
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DR EMBL; BC124503; AAI24504.1; -; mRNA.
DR RefSeq; NP_001070096.1; NM_001076628.1.
DR AlphaFoldDB; Q08BY5; -.
DR SMR; Q08BY5; -.
DR STRING; 7955.ENSDARP00000096160; -.
DR PaxDb; Q08BY5; -.
DR Ensembl; ENSDART00000105387; ENSDARP00000096160; ENSDARG00000058995.
DR GeneID; 767690; -.
DR KEGG; dre:767690; -.
DR CTD; 65094; -.
DR ZFIN; ZDB-GENE-060929-636; jmjd4.
DR eggNOG; KOG2131; Eukaryota.
DR GeneTree; ENSGT00940000159380; -.
DR HOGENOM; CLU_016785_2_2_1; -.
DR InParanoid; Q08BY5; -.
DR OrthoDB; 609279at2759; -.
DR PhylomeDB; Q08BY5; -.
DR TreeFam; TF105936; -.
DR PRO; PR:Q08BY5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000058995; Expressed in mature ovarian follicle and 21 other tissues.
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 Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..422
FT /note="2-oxoglutarate and iron-dependent oxygenase JMJD4"
FT /id="PRO_0000291962"
FT DOMAIN 139..298
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
SQ SEQUENCE 422 AA; 49892 MW; EAB8EE17A2FF1E46 CRC64;
MDRETFHSCS SLVKLPRQIH QQHCSSHFIE YIEREIPYSK FFKNYLIPNQ PCMFSKKFTE
EWNCRKKWVT AEGKPNLQRL LHEFDETPVP VANCSVKEYN ANPKQIMPFK EFIQYWRESI
QNGHSSPKGC LYLKDWHMQR NFPEHNIYKT PIYFSSDWLN EYWDTIEVDD YRFVYMGPKG
SWTPFHADVF RSYSWSANIC GRKKWLLYPP GQEDFLRDCH GNLAYDVTAP ILQDKGLYAQ
FEEACQPLEI IQEAGEIIFV PSGWHHQVYN LEDTISINHN WLNGCNLDIM WQFLQDELSS
VQREIEEWRD TMDTWHQHCQ VIMKSCTGID YAEFASFLKT IANNRISFLN SSPRNADSCQ
DLLAESLCAL GPHHAAFDLQ RVLHIFEIML NNEDFKRLDP ATLSFKPEDL LQEIREAIRT
IV