ID   PLB1_CRYNH              Reviewed;         637 AA.
AC   Q9P8P2; J9VV08;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 2.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Phospholipase B;
DE            EC=3.1.1.5 {ECO:0000269|PubMed:10749672, ECO:0000305|PubMed:16524904};
DE   AltName: Full=Lysophospholipase;
DE   Flags: Precursor;
GN   Name=PLB1; ORFNames=CNAG_06085;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS   CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=11123698; DOI=10.1046/j.1365-2958.2001.02236.x;
RA   Cox G.M., McDade H.C., Chen S.C.A., Tucker S.C., Gottfredsson M.,
RA   Wright L.C., Sorrell T.C., Leidich S.D., Casadevall A., Ghannoum M.A.,
RA   Perfect J.R.;
RT   "Extracellular phospholipase activity is a virulence factor for
RT   Cryptococcus neoformans.";
RL   Mol. Microbiol. 39:166-175(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA   Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA   Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA   Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA   Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA   Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT   grubii reveals complex RNA expression and microevolution leading to
RT   virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   STRAIN=BL-1;
RX   PubMed=10749672; DOI=10.1042/0264-6021:3470431;
RA   Chen S.C.A., Wright L.C., Golding J.C., Sorrell T.C.;
RT   "Purification and characterization of secretory phospholipase B,
RT   lysophospholipase and lysophospholipase/transacylase from a virulent strain
RT   of the pathogenic fungus Cryptococcus neoformans.";
RL   Biochem. J. 347:431-439(2000).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16524904; DOI=10.1128/ec.5.3.488-498.2006;
RA   Siafakas A.R., Wright L.C., Sorrell T.C., Djordjevic J.T.;
RT   "Lipid rafts in Cryptococcus neoformans concentrate the virulence
RT   determinants phospholipase B1 and Cu/Zn superoxide dismutase.";
RL   Eukaryot. Cell 5:488-498(2006).
CC   -!- FUNCTION: Exhibits phospholipase B (PLB), lysophospholipase (LPL) and
CC       lysophospholipase/transacylase (LPTA) activities.
CC       {ECO:0000269|PubMed:10749672, ECO:0000269|PubMed:16524904}.
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:0000269|PubMed:10749672, ECO:0000305|PubMed:16524904};
CC   -!- ACTIVITY REGULATION: Inhibited by Fe(3+) ion.
CC       {ECO:0000269|PubMed:10749672}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active only at acidic pHs. {ECO:0000269|PubMed:10749672};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10749672,
CC       ECO:0000269|PubMed:16524904}. Cell membrane
CC       {ECO:0000269|PubMed:16524904}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Localizes to lipid rafts in the cell membrane prior
CC       to secretion. {ECO:0000269|PubMed:16524904}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10749672}.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:10749672 describes peptide sequences that do not match
CC       PLB1, but originate from a copurified, contaminating chitin
CC       deacetylase. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AFR98312.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF223383; AAF65220.1; -; Genomic_DNA.
DR   EMBL; CP003831; AFR98312.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_012052996.1; XM_012197606.1.
DR   AlphaFoldDB; Q9P8P2; -.
DR   SMR; Q9P8P2; -.
DR   GlyCosmos; Q9P8P2; 17 sites, No reported glycans.
DR   GeneID; 23889325; -.
DR   KEGG; cng:CNAG_06085; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OrthoDB; 1826981at2759; -.
DR   BRENDA; 3.1.1.5; 1723.
DR   PHI-base; PHI:228; -.
DR   PHI-base; PHI:2843; -.
DR   PHI-base; PHI:7231; -.
DR   PHI-base; PHI:7259; -.
DR   PHI-base; PHI:9057; -.
DR   PHI-base; PHI:9874; -.
DR   Proteomes; UP000010091; Chromosome 12.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; 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   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   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..637
FT                   /note="Phospholipase B"
FT                   /id="PRO_0000024636"
FT   DOMAIN          46..572
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        606
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        6
FT                   /note="A -> G (in Ref. 1; AAF65220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="K -> N (in Ref. 1; AAF65220)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   637 AA;  68818 MW;  7C052A69669B2276 CRC64;
     MSIATATFAF SLFATIAFAV PPETPRIELQ AERGLGDKSY APWQVDCPSN VTWIRNATTG
     LGSGERAYIE AREKLVQPVI EQMMAARGLE TPPRTPNIGV ALSGGGYRAM LTGLGGIMGM
     MNESTEASES ETGGWLDGVS YWAGLSGGSW ATGTFMSNGG QLPTNLLENL WNIDSNLVFP
     DDDKLSFYTE LYTETNAKSD LGFPIQITDV WGLAIGSHVL PERYQLSNTP NLTFSSLPSV
     VSALGNASLP MPIIIAADRK RREAGELVIA ENATVWEFTP YEFGSWAFGS QYKSPGAFTP
     IEYLGTSVDD GSPNGTCWKG FDQLSFVMGT SATLFNGAFL ELNGTDSGLL TNLITAFLAD
     LGEDQADISR IPNTFSNYNS GENPIYNLTY ITLVDAGETN QNIPLEPLLV PTRDVDAIVA
     FDSSYDTDYI WPNGTALRTT YERAKVLAEH ENTRVLMPEV PSMNGFVNGG YNSRPTFFGC
     NDTTTPLIIY VPSYPWSFAA NTSTYQLSYE NDEANEMLLN GMRSLTLNHS VPTWPTCFAC
     ALTDRSFMYT SENRSTTCQK CFDTWCWAGD DNTTEPATYE PVINSVPPWL VANNLSIGVA
     DAPASNESTA GTASSGAAKA DVSMGMVALA AGLGLML
//