ID   PLG7_SCHPO              Reviewed;         438 AA.
AC   Q9URV1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Putative phospholipase A2;
DE            EC=3.1.1.47;
DE   AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE   AltName: Full=2-acetyl-1-alkylglycerophosphocholine esterase;
GN   Name=plg7 {ECO:0000312|EMBL:CAB53727.1}; ORFNames=SPBC106.11c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAB53727.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC         alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC         Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC         Evidence={ECO:0000250|UniProtKB:P83006,
CC         ECO:0000250|UniProtKB:Q13093};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000255}.
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DR   EMBL; CU329671; CAB53727.1; -; Genomic_DNA.
DR   PIR; T39268; T39268.
DR   RefSeq; NP_595160.1; NM_001021069.2.
DR   AlphaFoldDB; Q9URV1; -.
DR   SMR; Q9URV1; -.
DR   BioGRID; 276349; 5.
DR   STRING; 4896.SPBC106.11c.1; -.
DR   ESTHER; schpo-PLG7; PAF-Acetylhydrolase.
DR   MaxQB; Q9URV1; -.
DR   PaxDb; Q9URV1; -.
DR   EnsemblFungi; SPBC106.11c.1; SPBC106.11c.1:pep; SPBC106.11c.
DR   GeneID; 2539799; -.
DR   KEGG; spo:SPBC106.11c; -.
DR   PomBase; SPBC106.11c; plg7.
DR   VEuPathDB; FungiDB:SPBC106.11c; -.
DR   eggNOG; KOG3847; Eukaryota.
DR   HOGENOM; CLU_655796_0_0_1; -.
DR   InParanoid; Q9URV1; -.
DR   OMA; GNWIGKF; -.
DR   PhylomeDB; Q9URV1; -.
DR   Reactome; R-SPO-418346; Platelet homeostasis.
DR   PRO; PR:Q9URV1; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IMP:PomBase.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR   GO; GO:0009395; P:phospholipid catabolic process; IMP:PomBase.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005065; PAF_acetylhydro-like.
DR   InterPro; IPR016715; PAF_acetylhydro_eucaryote.
DR   PANTHER; PTHR10272; PTHR10272; 1.
DR   Pfam; PF03403; PAF-AH_p_II; 1.
DR   PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..438
FT                   /note="Putative phospholipase A2"
FT                   /id="PRO_0000316918"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        291
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q13093"
FT   ACT_SITE        368
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q13093"
SQ   SEQUENCE   438 AA;  49847 MW;  24767654F94C10F9 CRC64;
     MGLGFSSKKQ LPAYCGPLPV GSLVLELSVP EEFRCEYKTI EHKLRTVKVR IFYPLDPTKD
     VEPRTDELWL PFHEGIPEVA KGFRWWLLRA FASGLTNLAL PVYKGELFHP PNNGKLPVFI
     FSHGLVGSRN VYSSLCGTIA SYGIVVLAME HRDNSAIIST VRDPLHPEEP PYVVQYREIS
     DFYADATVVL QNERLLFRQQ EIQIALQMIR NINDLGTPDE NLPFLCSVDS SFYNSVFQSM
     KGNLNTAQGE LIVAGHSFGA ATCAFISGSS TKSLYNDYMF HTEFKCSILY DIWMLPVRQL
     HLSTMRYPTL MIISYEFRRF VDNFQALESW LVNKDSENQN AGESADEKMS VVPLKKYSHV
     FVYDGTVHAN QSDLPILLPR MVLRVLKGKF EADPYEALRI NTRSSVQFLR ENHVENVQGD
     NDPSSLQTNI IPGWERIM