JMJD7_MOUSE
ID JMJD7_MOUSE Reviewed; 316 AA.
AC P0C872; A2AP62; Q4QQM1; Q80VV8; Q91W88;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7 {ECO:0000250|UniProtKB:P0C870};
DE EC=1.14.11.63 {ECO:0000250|UniProtKB:P0C870};
DE EC=3.4.-.- {ECO:0000269|PubMed:28847961};
DE AltName: Full=JmjC domain-containing protein 7 {ECO:0000250|UniProtKB:P0C870};
DE AltName: Full=Jumonji domain-containing protein 7 {ECO:0000250|UniProtKB:P0C870};
DE AltName: Full=L-lysine (3S)-hydroxylase Jmjd7 {ECO:0000250|UniProtKB:P0C870};
GN Name=Jmjd7 {ECO:0000303|PubMed:28847961, ECO:0000312|MGI:MGI:3845785};
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].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION.
RX PubMed=28847961; DOI=10.1073/pnas.1706831114;
RA Liu H., Wang C., Lee S., Deng Y., Wither M., Oh S., Ning F., Dege C.,
RA Zhang Q., Liu X., Johnson A.M., Zang J., Chen Z., Janknecht R., Hansen K.,
RA Marrack P., Li C.Y., Kappler J.W., Hagman J., Zhang G.;
RT "Clipping of arginine-methylated histone tails by JMJD5 and JMJD7.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7717-E7726(2017).
CC -!- FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-
CC oxoglutarate-dependent monooxygenase (PubMed:28847961) (By similarity).
CC Endopeptidase that cleaves histones N-terminal tails at the carboxyl
CC side of methylated arginine or lysine residues, to generate 'tailless
CC nucleosomes', which may trigger transcription elongation
CC (PubMed:28847961). Preferentially recognizes and cleaves monomethylated
CC and dimethylated arginine residues of histones H2, H3 and H4. After
CC initial cleavage, continues to digest histones tails via its
CC aminopeptidase activity (PubMed:28847961). Additionally, may play a
CC role in protein biosynthesis by modifying the translation machinery.
CC Acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing
CC (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-
CC 21' of DRG2 translation factors (TRAFAC), promoting their interaction
CC with ribonucleic acids (RNA) (By similarity).
CC {ECO:0000250|UniProtKB:P0C870, ECO:0000269|PubMed:28847961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-
CC lysyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:57152, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15133, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:141492; EC=1.14.11.63;
CC Evidence={ECO:0000250|UniProtKB:P0C870};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P0C870};
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with DRG1 and DRG2.
CC {ECO:0000250|UniProtKB:P0C870}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C870}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C870}.
CC -!- CAUTION: This sequence was first thought to be an alternatively spliced
CC isoform of Pla2g4b. It is derived from Jmjd7 which is located upstream
CC of Pla2g4b. Most tissues also express read-through transcripts from
CC Jmjd7 into the downstream Pla2g4b gene, some of which may encode fusion
CC proteins combining the N-terminus of this protein with PLA2G4B protein.
CC {ECO:0000305}.
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DR EMBL; BC016255; AAH16255.1; -; mRNA.
DR CCDS; CCDS50676.1; -.
DR RefSeq; NP_001108109.1; NM_001114637.1.
DR PDB; 4QSZ; X-ray; 2.86 A; A/B=2-312.
DR PDB; 4QU2; X-ray; 2.70 A; A/B=1-316.
DR PDBsum; 4QSZ; -.
DR PDBsum; 4QU2; -.
DR AlphaFoldDB; P0C872; -.
DR SMR; P0C872; -.
DR STRING; 10090.ENSMUSP00000041220; -.
DR PhosphoSitePlus; P0C872; -.
DR EPD; P0C872; -.
DR MaxQB; P0C872; -.
DR PRIDE; P0C872; -.
DR ProteomicsDB; 301698; -.
DR Antibodypedia; 35028; 101 antibodies from 27 providers.
DR Ensembl; ENSMUST00000044675; ENSMUSP00000041220; ENSMUSG00000098789.
DR GeneID; 433466; -.
DR KEGG; mmu:433466; -.
DR UCSC; uc008luy.2; mouse.
DR CTD; 100137047; -.
DR MGI; MGI:3845785; Jmjd7.
DR VEuPathDB; HostDB:ENSMUSG00000098789; -.
DR eggNOG; KOG2508; Eukaryota.
DR GeneTree; ENSGT00900000141196; -.
DR HOGENOM; CLU_016785_6_0_1; -.
DR InParanoid; P0C872; -.
DR OMA; YWHDMEF; -.
DR OrthoDB; 1385616at2759; -.
DR PhylomeDB; P0C872; -.
DR BRENDA; 1.14.11.63; 3474.
DR BioGRID-ORCS; 433466; 1 hit in 70 CRISPR screens.
DR PRO; PR:P0C872; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P0C872; protein.
DR Bgee; ENSMUSG00000098789; Expressed in lens of camera-type eye and 71 other tissues.
DR ExpressionAtlas; P0C872; baseline and differential.
DR Genevisible; P0C872; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0004497; F:monooxygenase activity; ISO:MGI.
DR GO; GO:0106155; F:peptidyl-lysine 3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0018126; P:protein hydroxylation; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Disulfide bond; Hydrolase; Iron;
KW Metal-binding; Monooxygenase; Nucleus; Oxidoreductase; Protease;
KW Reference proteome.
FT CHAIN 1..316
FT /note="Bifunctional peptidase and (3S)-lysyl hydroxylase
FT Jmjd7"
FT /id="PRO_0000349375"
FT DOMAIN 128..307
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DISULFID 47
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P0C870"
FT HELIX 1..23
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:4QU2"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4QU2"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4QU2"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:4QU2"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:4QU2"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:4QU2"
SQ SEQUENCE 316 AA; 35917 MW; 710E3887F066353E CRC64;
MAEAALEAVR RALQEFPAAA RDLNVPRVVP YLDEPPSPLC FYRDWVCPNR PCIIRNALQH
WPALQKWSLS YLRATVGSTE VSVAVTPDGY ADAVRGDRFV MPAERRLPIS HVLDVLEGRA
QHPGVLYVQK QCSNLPTELP QLLSDIESHV PWASESLGKM PDAVNFWLGD ASAVTSLHKD
HYENLYCVVS GEKHFLLHPP SDRPFIPYNL YTPATYQLTE EGTFRVVDEE AMEKVPWIPL
DPLAPDLTQY PSYSQAQALH CTVRAGEMLY LPALWFHHVQ QSHGCIAVNF WYDMEYDLKY
SYFQLMDTLT RATGLD
