OPLA_MOUSE
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 03-AUG-2022, entry version 133.
DE RecName: Full=5-oxoprolinase;
DE EC=3.5.2.9;
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, Pancreas,
RC 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}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; Q8K010; -.
DR PeptideAtlas; Q8K010; -.
DR PRIDE; Q8K010; -.
DR ProteomicsDB; 294103; -.
DR Antibodypedia; 7618; 73 antibodies from 21 providers.
DR DNASU; 75475; -.
DR Ensembl; ENSMUST00000023222; ENSMUSP00000023222; ENSMUSG00000022562.
DR Ensembl; ENSMUST00000171340; ENSMUSP00000129100; ENSMUSG00000022562.
DR GeneID; 75475; -.
DR KEGG; mmu:75475; -.
DR UCSC; uc007wjo.1; mouse.
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; 62698at2759; -.
DR PhylomeDB; Q8K010; -.
DR TreeFam; TF300520; -.
DR Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR SABIO-RK; Q8K010; -.
DR BioGRID-ORCS; 75475; 3 hits in 73 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 210 other tissues.
DR ExpressionAtlas; Q8K010; baseline and differential.
DR Genevisible; Q8K010; MM.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; ISS:MGI.
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; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR003692; Hydantoinase_B.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR PANTHER; PTHR11365; PTHR11365; 1.
DR Pfam; PF05378; Hydant_A_N; 1.
DR Pfam; PF01968; Hydantoinase_A; 1.
DR Pfam; PF02538; Hydantoinase_B; 1.
PE 1: Evidence at protein level;
KW ATP-binding; 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
