PLB3_YEAST
ID PLB3_YEAST Reviewed; 686 AA.
AC Q08108; D6W256;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Lysophospholipase 3;
DE EC=3.1.1.5 {ECO:0000269|PubMed:10497163};
DE AltName: Full=Phospholipase B 3;
DE Flags: Precursor;
GN Name=PLB3; OrderedLocusNames=YOL011W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
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 [4]
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).
CC -!- FUNCTION: Sequentially removes both fatty acyl groups from
CC diacylglycerophospholipids and therefore has both phospholipase A and
CC lysophospholipase activities. Substrate preference is
CC phosphatidylserine > phosphatidylinositol. Does not cleave
CC phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and
CC phosphatidylinositol-bisphosphate (PubMed:10497163). Mainly responsible
CC for the degradation of phosphatidylinositol in vivo (PubMed:15588231).
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 Evidence={ECO:0000269|PubMed:10497163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:10497163};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10497163};
CC Lipid-anchor, GPI-anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; Z74753; CAA99010.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10772.1; -; Genomic_DNA.
DR PIR; S66693; S66693.
DR RefSeq; NP_014632.1; NM_001183265.1.
DR AlphaFoldDB; Q08108; -.
DR SMR; Q08108; -.
DR BioGRID; 34393; 90.
DR DIP; DIP-4220N; -.
DR IntAct; Q08108; 1.
DR MINT; Q08108; -.
DR STRING; 4932.YOL011W; -.
DR MaxQB; Q08108; -.
DR PaxDb; Q08108; -.
DR PRIDE; Q08108; -.
DR EnsemblFungi; YOL011W_mRNA; YOL011W; YOL011W.
DR GeneID; 854151; -.
DR KEGG; sce:YOL011W; -.
DR SGD; S000005371; PLB3.
DR VEuPathDB; FungiDB:YOL011W; -.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; Q08108; -.
DR OMA; HTYERQF; -.
DR BioCyc; MetaCyc:YOL011W-MON; -.
DR BioCyc; YEAST:YOL011W-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:Q08108; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08108; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA: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; IMP: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:0046488; P:phosphatidylinositol metabolic process; IDA:SGD.
DR GO; GO:0006660; P:phosphatidylserine catabolic 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 membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..659
FT /note="Lysophospholipase 3"
FT /id="PRO_0000024648"
FT PROPEP 660..686
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372444"
FT DOMAIN 39..592
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT LIPID 659
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 686 AA; 75077 MW; 95A2DBF41BF3E20F CRC64;
MIRPLCSKII ISYIFAISQF LLAANAWSPT DSYVPGTVSC PDDINLVREA TSISQNESAW
LEKRNKVTSV ALKDFLTRAT ANFSDSSEVL SKLFNDGNSE NLPKIAVAVS GGGYRSMLTG
AGVLAAMDNR TEGAYEHGLG GLLQSTTYLS GASGGNWLVG TLALNNWTSV QDILNNMQND
DSIWDLSDSI VTPGGINIFK TAKRWDHISN AVESKQNADY NTSLADIWGR ALAYNFFPSL
NRGGIGLTWS SIRDFPVFQN AEMPFPISVA DGRYPGTKVI NLNATVFEFN PFEMGSWDPS
LNSFANVKYL GTNVSNGVPL ERGKCTAGFD NAGFIMGTSS TLFNQFLLRI NSTHLPSFIT
RLARHFLKDL SQDFNDIAVY SPNPFKDTKF LDSDYTTSIV DSDSLFLVDG GEDDENVPVL
PLIQKERDVD IIFAVDNSAD MRLAWPDGSS LVHTYERQFV KQGQGMSFPY VPDTNTFVNL
GLNKKPTFFG CDANNLTDLQ YIPPLVVYLP NAEYSFNSNQ SAFKLSYSES QRRSMIQNGF
EIATRNNFTD DPEFMGCVGC AIIRRKQQAL NITLPPECET CFKNYCWNGT LDTTPLPDVE
KDVHHSFINV NSFNSSIGQE ESLYAGSSAS QSSSSSSSSS SSSEIPSATA TLEKKAATNS
GSHLSGISVK FSAMIMLTLL MFTGAV
