PLB2_YEAST
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 03-AUG-2022, entry version 163.
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; 116.
DR STRING; 4932.YMR006C; -.
DR SwissLipids; SLP:000000121; -.
DR MaxQB; Q03674; -.
DR PaxDb; Q03674; -.
DR PRIDE; Q03674; -.
DR EnsemblFungi; YMR006C_mRNA; YMR006C; YMR006C.
DR GeneID; 855018; -.
DR KEGG; sce:YMR006C; -.
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 BioCyc; MetaCyc:YMR006C-MON; -.
DR BioCyc; YEAST:YMR006C-MON; -.
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 PRO; PR:Q03674; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03674; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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 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 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
