PLB2_CANGA
ID PLB2_CANGA Reviewed; 695 AA.
AC Q8TG06; Q6FNH0;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Lysophospholipase 2;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:P39105};
DE AltName: Full=Phospholipase B 2 {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN Name=PLB2 {ECO:0000303|Ref.1}; OrderedLocusNames=CAGL0J11748g;
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., Chekley M.A., Lewin A., Nguyen M.-H.;
RT "Cloning and characterization of phospholipase B gene (PLB2) 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).
RN [3]
RP PROTEIN SEQUENCE OF 38-48; 191-201 AND 279-309, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=26546455; DOI=10.1093/femsyr/fov098;
RA Gomez-Molero E., de Boer A.D., Dekker H.L., Moreno-Martinez A.,
RA Kraneveld E.A., Ichsan I., Chauhan N., Weig M., de Soet J.J.,
RA de Koster C.G., Bader O., de Groot P.W.;
RT "Proteomic analysis of hyperadhesive Candida glabrata clinical isolates
RT reveals a core wall proteome and differential incorporation of adhesins.";
RL FEMS Yeast Res. 15:0-0(2015).
RN [4]
RP PROTEIN SEQUENCE OF 91-101; 191-201; 295-309 AND 510-517, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18806209; DOI=10.1128/ec.00284-08;
RA de Groot P.W., Kraneveld E.A., Yin Q.Y., Dekker H.L., Gross U.,
RA Crielaard W., de Koster C.G., Bader O., Klis F.M., Weig M.;
RT "The cell wall of the human pathogen Candida glabrata: differential
RT incorporation of novel adhesin-like wall proteins.";
RL Eukaryot. Cell 7:1951-1964(2008).
CC -!- FUNCTION: Catalyzes the release of fatty acids from lysophospholipids
CC (By similarity). Phospholipase B may well contribute to pathogenicity
CC by abetting the fungus in damaging and traversing host cell membranes,
CC processes which likely increase the rapidity of disseminated infection
CC (By similarity). {ECO:0000250|UniProtKB:P78854,
CC ECO:0000250|UniProtKB:Q9UWF6}.
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 Evidence={ECO:0000250|UniProtKB:P39105};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Secreted, cell wall
CC {ECO:0000269|PubMed:18806209, ECO:0000269|PubMed:26546455}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; AF498582; AAM19335.1; -; Genomic_DNA.
DR EMBL; CR380956; CAG61175.1; -; Genomic_DNA.
DR RefSeq; XP_448224.1; XM_448224.1.
DR AlphaFoldDB; Q8TG06; -.
DR SMR; Q8TG06; -.
DR STRING; 5478.XP_448224.1; -.
DR EnsemblFungi; CAG61175; CAG61175; CAGL0J11748g.
DR GeneID; 2889464; -.
DR KEGG; cgr:CAGL0J11748g; -.
DR CGD; CAL0133296; PLB2.
DR VEuPathDB; FungiDB:CAGL0J11748g; -.
DR eggNOG; KOG1325; Eukaryota.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; Q8TG06; -.
DR OMA; FYRYASQ; -.
DR PHI-base; PHI:3601; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
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:0006650; P:glycerophospholipid metabolic process; 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 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..695
FT /note="Lysophospholipase 2"
FT /id="PRO_0000024634"
FT DOMAIN 28..577
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 612..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 254
FT /note="S -> P (in Ref. 1; AAM19335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 74629 MW; 929CE2E53036276C CRC64;
MQLSVLIASV LAAGAAVDAA SYTPQNVSCP DNANFIRNAA DGLSPAEKEW LKKRDPITRD
ALQTFLRRAF ANVSTEITSA LFNDTENVPK LGIAVAGGGY RAMFVGAGAF AAMDNRTDGA
NEHGLGGLLQ AATYMAGLSG GNWLTGTLAY NNFTSVQQIL EEGDKADAIW NITNSFLNPY
DKDFSKTLAR WTAIGSQVQG KRDAGFNVTI TDLWSRALAY GWFPTLPNAG AGLTWSSLRD
NEIFMNGEMP MPISVADGRY PGTTVINLNA TVFEMTPFEI GSWDPSLNAF SDIKYLGTQV
TDGKPETERC INGFDDASFI MGTSSSLFNE FTMSNDSAVA YTYLNTLSST LVKGIDKENN
DIAMYAPNPF KGSKYVDSNY TTSIVDSDSL FLVDGGEDLQ GIPFVPLLKQ ERDLDIIFAI
DVDTETSDNY PAGGPMMKTY ERQFSKQGKG MAFPYVPDMT TFVNLGLGGK PSFYGCDANN
LTDLEYIPPL IVYIPNSYHS FESNVSTFKL NYNYSERVGM IRNAFEATTR NNLTEDADYV
TCVGCAIIRR KQQSLNLTLP DICDKCFTNY CWNGTIDNTP TKLLTPNNQD PAAISSAIAA
VTDDSPIGAL LNTGSGTKSN SSSKTNSTLV TSSRATSTGT LISNSSSNST VSSTAARSST
SSTAKKNAGS VLKLEFSKSA SVMVAIAAAA VASLI
