ID   PLB2_YEAST              Reviewed;         706 AA.
AC   Q03674; D6VZI1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Lysophospholipase 2;
DE            EC=3.1.1.5;
DE   AltName: Full=Phospholipase B 2;
DE   Flags: Precursor;
GN   Name=PLB2; OrderedLocusNames=YMR006C; ORFNames=YM8270.08C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DG338;
RX   PubMed=10231538; DOI=10.1021/bi9824590;
RA   Fyrst H., Oskouian B., Kuypers F.A., Saba J.D.;
RT   "The PLB2 gene of Saccharomyces cerevisiae confers resistance to
RT   lysophosphatidylcholine and encodes a phospholipase B/lysophospholipase.";
RL   Biochemistry 38:5864-5871(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10497163; DOI=10.1074/jbc.274.40.28121;
RA   Merkel O., Fido M., Mayr J.A., Prueger H., Raab F., Zandonella G.,
RA   Kohlwein S.D., Paltauf F.;
RT   "Characterization and function in vivo of two novel phospholipases
RT   B/lysophospholipases from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 274:28121-28127(1999).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=15588231; DOI=10.1042/bj20041272;
RA   Merkel O., Oskolkova O.V., Raab F., El-Toukhy R., Paltauf F.;
RT   "Regulation of activity in vitro and in vivo of three phospholipases B from
RT   Saccharomyces cerevisiae.";
RL   Biochem. J. 387:489-496(2005).
RN   [8]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR.
RX   PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA   Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA   de Koster C.G.;
RT   "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT   identification of proteins covalently attached via
RT   glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL   J. Biol. Chem. 280:20894-20901(2005).
CC   -!- FUNCTION: Sequentially removes both fatty acyl groups from
CC       diacylglycerophospholipids and therefore has both phospholipase A and
CC       lysophospholipase activities. However, it does not display transacylase
CC       activity. Substrate preference is phosphatidylserine >
CC       phosphatidylinositol > phosphatidylcholine > phosphatidylethanolamine
CC       (PubMed:10231538, PubMed:10497163). The substrate specificity is
CC       pH- and ion-dependent. In contrast with activities observed at optimum
CC       pH 3.5, the order of substrate preference at pH 5.5 is
CC       phosphatidylserine = phosphatidylethanolamine > phosphatidylcholine >
CC       phosphatidylinositol (PubMed:15588231). {ECO:0000269|PubMed:10231538,
CC       ECO:0000269|PubMed:10497163, ECO:0000269|PubMed:15588231}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = H(+) +
CC         hexadecanoate + sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:40891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73004, ChEBI:CHEBI:143890;
CC         Evidence={ECO:0000269|PubMed:10231538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40892;
CC         Evidence={ECO:0000305|PubMed:10231538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC         hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC         Evidence={ECO:0000269|PubMed:10231538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:10231538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) +
CC         hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64765, ChEBI:CHEBI:75020;
CC         Evidence={ECO:0000269|PubMed:10231538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44553;
CC         Evidence={ECO:0000305|PubMed:10231538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000269|PubMed:10231538};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC         Evidence={ECO:0000305|PubMed:10231538};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4. {ECO:0000269|PubMed:10231538};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:10231538};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC       anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC       CWP).
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC   -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR   EMBL; AF129165; AAD28616.1; -; Genomic_DNA.
DR   EMBL; Z48613; CAA88521.1; -; Genomic_DNA.
DR   EMBL; AY693181; AAT93200.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09905.1; -; Genomic_DNA.
DR   PIR; S53035; S53035.
DR   RefSeq; NP_013719.1; NM_001182502.1.
DR   AlphaFoldDB; Q03674; -.
DR   SMR; Q03674; -.
DR   BioGRID; 35176; 120.
DR   STRING; 4932.YMR006C; -.
DR   SwissLipids; SLP:000000121; -.
DR   GlyCosmos; Q03674; 25 sites, No reported glycans.
DR   GlyGen; Q03674; 29 sites, 1 O-linked glycan (4 sites).
DR   MaxQB; Q03674; -.
DR   PaxDb; 4932-YMR006C; -.
DR   PeptideAtlas; Q03674; -.
DR   EnsemblFungi; YMR006C_mRNA; YMR006C; YMR006C.
DR   GeneID; 855018; -.
DR   KEGG; sce:YMR006C; -.
DR   AGR; SGD:S000004608; -.
DR   SGD; S000004608; PLB2.
DR   VEuPathDB; FungiDB:YMR006C; -.
DR   eggNOG; KOG1325; Eukaryota.
DR   GeneTree; ENSGT01030000234606; -.
DR   HOGENOM; CLU_014602_0_0_1; -.
DR   InParanoid; Q03674; -.
DR   OMA; FARYCWN; -.
DR   OrthoDB; 1826981at2759; -.
DR   BioCyc; MetaCyc:YMR006C-MONOMER; -.
DR   BioCyc; YEAST:YMR006C-MONOMER; -.
DR   Reactome; R-SCE-111995; phospho-PLA2 pathway.
DR   Reactome; R-SCE-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-SCE-1482798; Acyl chain remodeling of CL.
DR   Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-SCE-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-SCE-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-SCE-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-SCE-1483115; Hydrolysis of LPC.
DR   Reactome; R-SCE-1483152; Hydrolysis of LPE.
DR   Reactome; R-SCE-1483166; Synthesis of PA.
DR   Reactome; R-SCE-2142753; Arachidonic acid metabolism.
DR   Reactome; R-SCE-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-SCE-432142; Platelet sensitization by LDL.
DR   Reactome; R-SCE-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 855018; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q03674; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03674; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IDA:SGD.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IDA:SGD.
DR   CDD; cd07203; cPLA2_Fungal_PLB; 1.
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 wall; Glycoprotein; GPI-anchor; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Lipoprotein; Membrane; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..680
FT                   /note="Lysophospholipase 2"
FT                   /id="PRO_0000024647"
FT   PROPEP          681..706
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000372443"
FT   DOMAIN          36..588
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT   REGION          627..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           680
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
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        390
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        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        524
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        543
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        630
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        634
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        642
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        648
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        652
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   706 AA;  75455 MW;  5E7BF22C77780DC2 CRC64;
     MQLRNILQAS SLISGLSLAA DSSSTTGDGY APSIIPCPSD DTSLVRNASG LSTAETDWLK
     KRDAYTKEAL HSFLSRATSN FSDTSLLSTL FSSNSSNVPK IGIACSGGGY RAMLGGAGMI
     AAMDNRTDGA NEHGLGGLLQ SSTYLSGLSG GNWLTGTLAW NNWTSVQEIV DHMSESDSIW
     NITKSIVNPG GSNLTYTIER WESIVQEVQA KSDAGFNISL SDLWARALSY NFFPSLPDAG
     SALTWSSLRD VDVFKNGEMP LPITVADGRY PGTTVINLNA TLFEFTPFEM GSWDPSLNAF
     TDVKYLGTNV TNGKPVNKDQ CVSGYDNAGF VIATSASLFN EFSLEASTST YYKMINSFAN
     KYVNNLSQDD DDIAIYAANP FKDTEFVDRN YTSSIVDADD LFLVDGGEDG QNLPLVPLIK
     KERDLDVVFA LDISDNTDES WPSGVCMTNT YERQYSKQGK GMAFPYVPDV NTFLNLGLTN
     KPTFFGCDAK NLTDLEYIPP LVVYIPNTKH SFNGNQSTLK MNYNVTERLG MIRNGFEAAT
     MGNFTDDSNF LGCIGCAIIR RKQESLNATL PPECTKCFAD YCWNGTLSTS ANPELSGNST
     YQSGAIASAI SEATDGIPIT ALLGSSTSGN TTSNSTTSTS SNVTSNSNSS SNTTLNSNSS
     SSSISSSTAR SSSSTANKAN AAAISYANTN TLMSLLGAIT ALFGLI
//