PLB1_CRYNH
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 25-MAY-2022, entry version 74.
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 EnsemblFungi; AFR98312; AFR98312; CNAG_06085.
DR GeneID; 23889325; -.
DR HOGENOM; CLU_014602_0_0_1; -.
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 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 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 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
