ID   OPLA_MOUSE              Reviewed;        1288 AA.
AC   Q8K010; Q8R3K2;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=5-oxoprolinase;
DE            EC=3.5.2.9 {ECO:0000250|UniProtKB:Q75WB5};
DE   AltName: Full=5-oxo-L-prolinase;
DE            Short=5-OPase;
DE   AltName: Full=Pyroglutamase;
GN   Name=Oplah;
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   TISSUE=Kidney;
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=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and 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).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate
CC       coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
CC       {ECO:0000250|UniProtKB:Q75WB5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC         phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC         Evidence={ECO:0000250|UniProtKB:Q75WB5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q75WB5}.
CC   -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}.
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DR   EMBL; BC025120; AAH25120.1; -; mRNA.
DR   EMBL; BC034522; AAH34522.1; -; mRNA.
DR   CCDS; CCDS27565.1; -.
DR   RefSeq; NP_694762.1; NM_153122.2.
DR   RefSeq; XP_006521572.1; XM_006521509.2.
DR   AlphaFoldDB; Q8K010; -.
DR   SMR; Q8K010; -.
DR   BioGRID; 217507; 1.
DR   IntAct; Q8K010; 2.
DR   STRING; 10090.ENSMUSP00000129100; -.
DR   iPTMnet; Q8K010; -.
DR   PhosphoSitePlus; Q8K010; -.
DR   SwissPalm; Q8K010; -.
DR   EPD; Q8K010; -.
DR   jPOST; Q8K010; -.
DR   MaxQB; Q8K010; -.
DR   PaxDb; 10090-ENSMUSP00000129100; -.
DR   PeptideAtlas; Q8K010; -.
DR   ProteomicsDB; 294103; -.
DR   Antibodypedia; 7618; 83 antibodies from 21 providers.
DR   DNASU; 75475; -.
DR   Ensembl; ENSMUST00000023222.13; ENSMUSP00000023222.7; ENSMUSG00000022562.16.
DR   Ensembl; ENSMUST00000171340.9; ENSMUSP00000129100.2; ENSMUSG00000022562.16.
DR   GeneID; 75475; -.
DR   KEGG; mmu:75475; -.
DR   UCSC; uc007wjo.1; mouse.
DR   AGR; MGI:1922725; -.
DR   CTD; 26873; -.
DR   MGI; MGI:1922725; Oplah.
DR   VEuPathDB; HostDB:ENSMUSG00000022562; -.
DR   eggNOG; KOG1939; Eukaryota.
DR   GeneTree; ENSGT00390000013463; -.
DR   HOGENOM; CLU_002157_0_1_1; -.
DR   InParanoid; Q8K010; -.
DR   OMA; TDCNVML; -.
DR   OrthoDB; 674at2759; -.
DR   PhylomeDB; Q8K010; -.
DR   TreeFam; TF300520; -.
DR   Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR   SABIO-RK; Q8K010; -.
DR   BioGRID-ORCS; 75475; 4 hits in 78 CRISPR screens.
DR   ChiTaRS; Oplah; mouse.
DR   PRO; PR:Q8K010; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8K010; Protein.
DR   Bgee; ENSMUSG00000022562; Expressed in right kidney and 212 other cell types or tissues.
DR   ExpressionAtlas; Q8K010; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:MGI.
DR   InterPro; IPR049517; ACX-like_C.
DR   InterPro; IPR008040; Hydant_A_N.
DR   InterPro; IPR002821; Hydantoinase_A.
DR   InterPro; IPR003692; Hydantoinase_B.
DR   InterPro; IPR045079; Oxoprolinase_fam.
DR   PANTHER; PTHR11365:SF2; 5-OXOPROLINASE; 1.
DR   PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1.
DR   Pfam; PF19278; Hydant_A_C; 1.
DR   Pfam; PF05378; Hydant_A_N; 1.
DR   Pfam; PF01968; Hydantoinase_A; 1.
DR   Pfam; PF02538; Hydantoinase_B; 1.
DR   Genevisible; Q8K010; MM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1288
FT                   /note="5-oxoprolinase"
FT                   /id="PRO_0000208578"
FT   REGION          1248..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1270
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97608"
FT   CONFLICT        902
FT                   /note="Q -> R (in Ref. 1; AAH25120)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1288 AA;  137611 MW;  DD6DDF24DF5AC390 CRC64;
     MGSPEERFHF AIDRGGTFTD VFAQCPGGHV RVLKLLSEDP ANYADAPTEG IRRILEQERG
     VLLPRGRPLD TSHIASIRMG TTVATNALLE RQGERVALLV TRGFRDLLHI GTQARPDLFD
     LAVPMPEVLY EEVVEVDERV LLYRGEPGAG SPVKGCTGDL LEIQQPVDLA ALRGKLEGLL
     TRGIHSLAVV LMHSYTWAQH EQQVGTLARE LGFTHVSLSS EVMPMVRIVP RGHTACADAY
     LTPTIQRYVQ GFRRGFQGQL KNVQVLFMRS DGGLAPMDAF SGSRAVLSGP AGGVVGYSTT
     TYQLEGGQPV IGFDMGGTST DVSRYAGEFE HVFEASTAGV TLQAPQLDIN TVAAGGGSRL
     FFRSGLFVVG PESAGAHPGP ACYRKGGPVT VTDANLVLGR LLPASFPCIF GPGEDQPLSP
     EASRKALEAV AMEVNSFLAS GPCPASQLSL EEVAMGFVRV ANEAMCRPIR ALTQARGHDP
     SAHVLACFGG AGGQHACAIA RALGMDTVHI HRHSGLLSAL GLALADVVHE AQEPCSLSYT
     PETFAQLDQR LSRLEEQCVD ALQAQGFSRS QISTESFLHL RYQGTDCALM VSANQHPATT
     CSPRAGDFGA AFVERYMREF GFIIPERSVV VDDVRVRGTG RSGLQLEETS KIQSGPPHVE
     KVTQCYFEGG YQETPVYLLG ELGYGHQLQG PCLIIDNNST ILVEPGCQAE VIETGDIRIS
     VGAEAPSMID TKLDPIQLSI FSHRFMSIAE QMGRILQRTA ISTNIKERLD FSCALFGPDG
     GLVSNAPHIP VHLGAMQETV QFQIQHLGAD LHPGDVLLSN HPSAGGSHLP DLTVITPVFW
     PGQSRPVFYV ASRGHHADIG GITPGSMPPH STTLQQEGAV FLSFKLVQGG VFQEEAVTEA
     LQAPGKISGC SGTRNLHDNL SDLRAQVAAN QKGIQLVGEL IGQYGLDVVQ AYMGHIQANA
     ELAVRDMLRA FGTSRQARGL PLEVSAKDHM DDGSPICLHV QINLNQGSAV FDFSGSGSEV
     FGNLNAPRAI TLSALIYCLR CLVGRDIPLN QGCLAPVQVI IPKGSILDPS PEAAVVGGNV
     LTSQRVVDVI LGAFGACAAS QGCMNNVTLG NARMGYYETV AGGAGAGPGW HGRSGVHSHM
     TNTRITDPEI LESRYPVILR RFELRPGSGG RGRFRGGDGV VRELVFREEA LLSVLTERRA
     FQPYGLHGGE PGTRGLNLLI RKDGRTVNLG GKTSVTVYPG DAFCLHTPGG GGYGDPEDPA
     PPPGSPPLYP AFPERGSVYE YRRAQEAV
//