ID   PLB1_CANGA              Reviewed;         659 AA.
AC   Q8TG07; Q6FNG9;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Lysophospholipase 1;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B 1;
DE   Flags: Precursor;
GN   Name=PLB1; OrderedLocusNames=CAGL0J11770g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Clancy C., Cheng S., Checkley M.A., Lewin A., Nguyen M.-H.;
RT   "Cloning and characterization of phospholipase gene (PLB1) of Candida
RT   glabrata.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids.
CC       Phospholipase B may well contribute to pathogenicity by abetting the
CC       fungus in damaging and traversing host cell membranes, processes which
CC       likely increase the rapidity of disseminated infection (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR   EMBL; AF498581; AAM16160.1; -; Genomic_DNA.
DR   EMBL; CR380956; CAG61176.1; -; Genomic_DNA.
DR   RefSeq; XP_448225.1; XM_448225.1.
DR   AlphaFoldDB; Q8TG07; -.
DR   SMR; Q8TG07; -.
DR   STRING; 284593.Q8TG07; -.
DR   GlyCosmos; Q8TG07; 17 sites, No reported glycans.
DR   EnsemblFungi; CAGL0J11770g-T; CAGL0J11770g-T-p1; CAGL0J11770g.
DR   GeneID; 2889465; -.
DR   KEGG; cgr:CAGL0J11770g; -.
DR   CGD; CAL0133252; PLB1.
DR   VEuPathDB; FungiDB:B1J91_J11770g; -.
DR   VEuPathDB; FungiDB:CAGL0J11770g; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; Q8TG07; -.
DR   OMA; FGHINMS; -.
DR   PHI-base; PHI:3600; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR   GO; GO:0042597; C:periplasmic space; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:EnsemblFungi.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd07203; cPLA2_Fungal_PLB; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF33; LYSOPHOSPHOLIPASE 1-RELATED; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..659
FT                   /note="Lysophospholipase 1"
FT                   /id="PRO_0000024633"
FT   DOMAIN          35..590
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        605
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        374
FT                   /note="D -> H (in Ref. 1; AAM16160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="T -> R (in Ref. 1; AAM16160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586..590
FT                   /note="NGTID -> KPTMQ (in Ref. 1; AAM16160)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   659 AA;  71644 MW;  DEE85E44AC2C951C CRC64;
     MQLQDLVVTV SLLAAFNGGV EAWSPTNSYV PANVTCPNDI NLLRNATGLS QSEIDWLKKR
     DVNTREALES FLKRVTSNFT SNSSASNLID QLFSTNSSNI PKIGIAASGG GYRAMLSGAG
     MVSAMDNRTD GANEHGLGGL LQAATYLAGL SGGNWLTTTL SWNNWTSVQD IVDSQDNDSA
     IWDISHSIVS PGGINIFKTG SRWDHISDAV EDKQKAGFNV SLADVWGRAL SYQFFPTLYR
     GGVAYLWSDL RESDVFKNAE MPMPISVADG RYPGTAVIDL NSTVFEYSPF ELGSWDPSLS
     AFTDVQYLGT KVSDGKPAEE GKCIAGFDNV GFLMGTSSTL FNQFLLRIND TSIPKFIRNL
     ATHFLKDLSE DYDDIAVYAP NPFRDADYVN NNRSKSLSES EYLFLVDGGE DGQNVPLVPL
     IQQERDLDIV FALDNSADTE ENWPDGASLM HTYRRQFGFQ GQGVTFPSVP GTDTFVNLGL
     NKKPTFFGCD ARNMTDLEYI PPLIVYIPNS RHSYNGNTST FKLSYSEKER LGVIRNGFEA
     ATMNNLTADS NFAGCIGCAI MRRKQQALNL TLPKECETCF TNYCWNGTID NTPAKGVTAS
     NDFDNASGSA AADMAEQDAS GAASASSSSR KKNAAVSVDV NAKTLFAIIT AMTAVFQLI
//