PLB1_CANGA
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 25-MAY-2022, entry version 98.
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 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
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 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; 5478.XP_448225.1; -.
DR EnsemblFungi; CAG61176; CAG61176; CAGL0J11770g.
DR GeneID; 2889465; -.
DR KEGG; cgr:CAGL0J11770g; -.
DR CGD; CAL0133252; PLB1.
DR VEuPathDB; FungiDB:CAGL0J11770g; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; Q8TG07; -.
DR OMA; WDISHSI; -.
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 InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; SSF52151; 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
