ID   PLB2_CANAX              Reviewed;         608 AA.
AC   O93795;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Lysophospholipase 2;
DE            EC=3.1.1.5;
DE   AltName: Full=CaPLB2;
DE   AltName: Full=Phospholipase B 2;
DE   Flags: Precursor;
GN   Name=PLB2;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10200936; DOI=10.1080/02681219980000091;
RA   Sugiyama Y., Nakashima S., Mirbod F., Kanoh H., Kitajima Y., Ghannoum M.A.,
RA   Nozawa Y.;
RT   "Molecular cloning of a second phospholipase B gene, caPLB2 from Candida
RT   albicans.";
RL   Med. Mycol. 37:61-67(1999).
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.
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; AB010809; BAA36162.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93795; -.
DR   SMR; O93795; -.
DR   VEuPathDB; FungiDB:C6_02000W_A; -.
DR   VEuPathDB; FungiDB:CAWG_05167; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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: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; Secreted;
KW   Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..608
FT                   /note="Lysophospholipase 2"
FT                   /id="PRO_0000024631"
FT   DOMAIN          30..564
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   608 AA;  67220 MW;  0ABEA2C878CD8610 CRC64;
     MLVWQSILLF LVGCVLSKSP TNLYTPGYVQ CPEGKLTRSS LDGINSNEKA YIDRRYANAK
     SELSRFLHNA KMVDFDVDGF LNSNPTIGLA FSGGGYRAML AGAGELLALD SRATNPSVLS
     GILQSSSYIV GLSGGSWLVG SLASNDLIPV DQLLREDKLW DIQNSLVAYY GVNIVRNTAM
     WGNINLQVQT KQLAGFTVSI TDVYGRALSH QLLTNFDNQG ASFLWSDVTE TTSFQNNEMP
     YPILAALGRE PNTVLMNFNS TVFELTPYEV GSWDPSLRSF VDTKYIGTRL DDGAPVSKRC
     VNGFDNAGFF MGTSSSLFNI VLQQLNNMPI PPFLKELISK FTLDPVEKLN IDIAQYNPNP
     FHKSNNSDTK IAQSRTLYLA DGGEDGQNVP LLPLIHRKVS AIFAFDQSAD KNNWPDGSAL
     IKTFERQFSS QGDGIAFPYV PDQNTFRNTN LTSKPTFFGC DAQNLTSLTE NIYDVPVVIY
     LANRPFTYFS NISTFKLKYS DTERQGMISN GYDVASRLNG KLDNEWAACV GCAIIRREQE
     RLGIEQTEQC KKCFENYCWD GTIYKGEPLG DNFSDEGLTT SAAYYNSNNV AGINDGGIAL
     VKRDDLSN