DEFM_MOUSE
ID DEFM_MOUSE Reviewed; 231 AA.
AC S4R2K0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Peptide deformylase, mitochondrial {ECO:0000305};
DE EC=3.5.1.88 {ECO:0000250|UniProtKB:Q9HBH1};
DE AltName: Full=Polypeptide deformylase;
DE Flags: Precursor;
GN Name=Pdf {ECO:0000312|MGI:MGI:1915273};
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 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).
CC -!- FUNCTION: Removes the formyl group from the N-terminal Met of newly
CC synthesized proteins. {ECO:0000250|UniProtKB:Q9HBH1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-
CC terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA-
CC COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88;
CC Evidence={ECO:0000250|UniProtKB:Q9HBH1};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q9HBH1};
CC Note=Binds 1 Co(2+) ion. {ECO:0000250|UniProtKB:Q9HBH1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9HBH1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9HBH1}.
CC -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC {ECO:0000305}.
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DR RefSeq; NP_080789.2; NM_026513.2.
DR AlphaFoldDB; S4R2K0; -.
DR SMR; S4R2K0; -.
DR STRING; 10090.ENSMUSP00000138676; -.
DR EPD; S4R2K0; -.
DR MaxQB; S4R2K0; -.
DR PeptideAtlas; S4R2K0; -.
DR PRIDE; S4R2K0; -.
DR ProteomicsDB; 320989; -.
DR Antibodypedia; 56384; 175 antibodies from 22 providers.
DR Ensembl; ENSMUST00000055316; ENSMUSP00000138676; ENSMUSG00000078931.
DR GeneID; 68023; -.
DR KEGG; mmu:68023; -.
DR UCSC; uc009ngx.2; mouse.
DR CTD; 64146; -.
DR MGI; MGI:1915273; Pdf.
DR VEuPathDB; HostDB:ENSMUSG00000078931; -.
DR eggNOG; KOG3137; Eukaryota.
DR GeneTree; ENSGT00390000018698; -.
DR HOGENOM; CLU_061901_5_1_1; -.
DR OMA; ILYPMRI; -.
DR OrthoDB; 1532656at2759; -.
DR PhylomeDB; S4R2K0; -.
DR BioGRID-ORCS; 68023; 1 hit in 40 CRISPR screens.
DR ChiTaRS; Pdf; mouse.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; S4R2K0; protein.
DR Bgee; ENSMUSG00000078931; Expressed in quadriceps femoris and 60 other tissues.
DR ExpressionAtlas; S4R2K0; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042586; F:peptide deformylase activity; ISO:MGI.
DR GO; GO:0043686; P:co-translational protein modification; IBA:GO_Central.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; ISO:MGI.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd00487; Pep_deformylase; 1.
DR Gene3D; 3.90.45.10; -; 1.
DR HAMAP; MF_00163; Pep_deformylase; 1.
DR InterPro; IPR023635; Peptide_deformylase.
DR InterPro; IPR036821; Peptide_deformylase_sf.
DR PANTHER; PTHR10458; PTHR10458; 1.
DR Pfam; PF01327; Pep_deformylase; 1.
DR PIRSF; PIRSF004749; Pep_def; 1.
DR PRINTS; PR01576; PDEFORMYLASE.
DR SUPFAM; SSF56420; SSF56420; 1.
PE 3: Inferred from homology;
KW Cobalt; Hydrolase; Metal-binding; Mitochondrion; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..231
FT /note="Peptide deformylase, mitochondrial"
FT /id="PRO_0000455155"
FT REGION 153..163
FT /note="Hydrophobic dimerization interface"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
FT ACT_SITE 203
FT /evidence="ECO:0000250|UniProtKB:P0A6K3"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
FT BINDING 160
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
FT BINDING 202
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
FT BINDING 206
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9HBH1"
SQ SEQUENCE 231 AA; 25779 MW; 800F2EA72336FA57 CRC64;
MLLLGRLPRP AWVPGSRAQR CSSLAALEGP ARTRSYWRYL RRLVCGAPQP PYAHVCQVGD
PVLRVVAAPV EPEQLAGPEL QRLVGRMVQV MRRRGCVGLS APQLGVPLQV LALEFPDKLL
RAFSPRLREL RQMEPFPLRV LVNPSLRVLD SRLVTFPEGC ESVAGFLACV PRFQAVQISG
LDPKGEPVVW SASGWTARII QHEMDHLQGC LFIDKMDSGT FTNLHWMEVN D
