ID   PLB1_CRYNB              Reviewed;         637 AA.
AC   P0CP75; Q55ID9; Q5K7X8; Q9P8L1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Phospholipase B;
DE            EC=3.1.1.5;
DE   AltName: Full=Lysophospholipase;
DE   Flags: Precursor;
GN   Name=PLB1; Synonyms=PLB; OrderedLocusNames=CNBM0810;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B-3501;
RA   Varma A., Kwon-Chung K.J.;
RT   "The phospholipase B gene from a serotype D isolate of Cryptococcus
RT   neoformans.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Exhibits phospholipase B (PLB), lysophospholipase (LPL) and
CC       lysophospholipase/transacylase (LPTA) activities. {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:0000250}.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF61964.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF238241; AAF61964.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AAEY01000062; EAL17514.1; -; Genomic_DNA.
DR   RefSeq; XP_772161.1; XM_767068.1.
DR   AlphaFoldDB; P0CP75; -.
DR   SMR; P0CP75; -.
DR   BindingDB; P0CP75; -.
DR   ChEMBL; CHEMBL4157; -.
DR   GlyCosmos; P0CP75; 17 sites, No reported glycans.
DR   GeneID; 4939441; -.
DR   KEGG; cnb:CNBM0810; -.
DR   VEuPathDB; FungiDB:CNBM0810; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   OrthoDB; 1826981at2759; -.
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   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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..637
FT                   /note="Phospholipase B"
FT                   /id="PRO_0000410196"
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"
SQ   SEQUENCE   637 AA;  68594 MW;  ADBEEF88100BA6B1 CRC64;
     MSIITTAFAL SLLATTAFAV PPETPRIELQ AERGLGDQSY APWQVDCPSN VTWIRNATTG
     LGTGERAYIE AREKLVQPAI EQMMAARGLE TPPRTPVIGV ALAGGGYRAM LTGLGGIMGM
     MNESTEASQS ETGGWLDGVS YWSGLSGGSW ATGSFMSNGG QLPTTLLENL WNIDSNLVFP
     DDGKLSFYTN LYTETNAKSD LGFPVQITDI WGLAIGSHVL PEPYQLSNTP NLTFSSLPSV
     VAALGNASLP MPIIVAADRK RREAGELVIA ENATVWEFTP YEFGSWAFGS QYKSPGAFTP
     IEYLGTSVDD GSPNGTCWKG FDQLSFVMGT SATLFNGAFL ELNGTDSGLL TNLITAFLAD
     LGEDQADISR IPNSFSNYNS GENPIYNLTY ITLVDAGETN QNIPLEPLLV PTRDVDAIVA
     FDSSYDSDYI WPNGTALRTT YERAKILAEH ENTRVLMPEV PSMNGFVNGG YNSRPTFFGC
     NDTTTPVIIY IPSYPWSFAA NTSTYQLSYE NNEANEMLLN GMRSLTLNHS VPTWPTCFAC
     ALTDRSFMYT SENRSTTCQE CFDTWCWAGD DNTTEPANYE PVINSVPPWL IANNLSIGMA
     DAPGSNESTA GTASSGAAKM GVGMGMVALT AGLGLML
//