PLB1_YEAST
ID PLB1_YEAST Reviewed; 664 AA.
AC P39105; D6VZI2; Q6B2E2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Lysophospholipase 1 {ECO:0000303|PubMed:8051052};
DE EC=3.1.1.5 {ECO:0000269|PubMed:10497163, ECO:0000269|PubMed:8051052};
DE AltName: Full=Phospholipase B 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=PLB1 {ECO:0000303|PubMed:8051052};
GN OrderedLocusNames=YMR008C {ECO:0000312|SGD:S000004610};
GN ORFNames=YM8270.10C {ECO:0000312|SGD:S000004610};
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, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8051052; DOI=10.1016/s0021-9258(17)32081-1;
RA Lee K.S., Patton J.L., Fido M., Hines L.K., Kohlwein S.D., Paltauf F.,
RA Henry S.A., Levin D.E.;
RT "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for
RT lysophospholipase and phospholipase B activity.";
RL J. Biol. Chem. 269:19725-19730(1994).
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 CATALYTIC ACTIVITY.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT "Amino acid residues in the omega-minus region participate in cellular
RT localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL J. Bacteriol. 181:3886-3889(1999).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, 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 B and
CC lysophospholipase activities. It also displays transacylase activity.
CC Substrate preference is phosphatidylserine > phosphatidylinositol >>
CC phosphatidylcholine > phosphatidylethanolamine (PubMed:10497163,
CC PubMed:8051052). The substrate specificity is pH- and ion-dependent. In
CC contrast with activities observed at optimum pH 3.5, the order of
CC substrate preference at pH 5.5 is phosphatidylcholine =
CC phosphatidylethanolamine >> phosphatidylinositol. Degrades
CC predominantly phosphatidylcholine and to some extent
CC phosphatidylinositol in vivo (PubMed:15588231).
CC {ECO:0000269|PubMed:10497163, ECO:0000269|PubMed:15588231,
CC ECO:0000269|PubMed:8051052}.
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, ECO:0000269|PubMed:8051052};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = a
CC fatty acid + H(+) + sn-glycero-3-phospho-1D-myo-inositol;
CC Xref=Rhea:RHEA:32987, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58444, ChEBI:CHEBI:64771;
CC Evidence={ECO:0000269|PubMed:10497163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32988;
CC Evidence={ECO:0000305|PubMed:10497163};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = a fatty acid +
CC H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:32979,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:64379, ChEBI:CHEBI:64765;
CC Evidence={ECO:0000269|PubMed:10497163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980;
CC Evidence={ECO:0000305|PubMed:10497163};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + 2 H2O =
CC 2 a carboxylate + 2 H(+) + sn-glycero-3-phospho-1D-myo-inositol;
CC Xref=Rhea:RHEA:32983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:57880, ChEBI:CHEBI:58444;
CC Evidence={ECO:0000269|PubMed:10497163, ECO:0000269|PubMed:15588231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32984;
CC Evidence={ECO:0000305|PubMed:10497163, ECO:0000305|PubMed:15588231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + 2 H2O = 2 a
CC carboxylate + 2 H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:32975, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:57262, ChEBI:CHEBI:64765;
CC Evidence={ECO:0000269|PubMed:10497163, ECO:0000269|PubMed:15588231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32976;
CC Evidence={ECO:0000305|PubMed:10497163, ECO:0000305|PubMed:15588231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40879, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:8051052};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40880;
CC Evidence={ECO:0000305|PubMed:8051052};
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, ECO:0000269|PubMed:8051052};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:10231538, ECO:0000305|PubMed:8051052};
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, ECO:0000269|PubMed:8051052};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:10231538, ECO:0000305|PubMed:8051052};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10383953,
CC ECO:0000305|PubMed:10497163}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:10383953, ECO:0000305|PubMed:10497163}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
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DR EMBL; L23089; AAA61611.1; -; Genomic_DNA.
DR EMBL; Z48613; CAA88523.1; -; Genomic_DNA.
DR EMBL; AY692788; AAT92807.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09906.1; -; Genomic_DNA.
DR PIR; S53037; S53037.
DR RefSeq; NP_013721.1; NM_001182504.1.
DR AlphaFoldDB; P39105; -.
DR SMR; P39105; -.
DR BioGRID; 35177; 49.
DR DIP; DIP-2804N; -.
DR IntAct; P39105; 2.
DR MINT; P39105; -.
DR STRING; 4932.YMR008C; -.
DR SwissLipids; SLP:000000078; -.
DR MaxQB; P39105; -.
DR PaxDb; P39105; -.
DR PRIDE; P39105; -.
DR EnsemblFungi; YMR008C_mRNA; YMR008C; YMR008C.
DR GeneID; 855020; -.
DR KEGG; sce:YMR008C; -.
DR SGD; S000004610; PLB1.
DR VEuPathDB; FungiDB:YMR008C; -.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_014602_0_0_1; -.
DR InParanoid; P39105; -.
DR OMA; WDISHSI; -.
DR BioCyc; MetaCyc:YMR008C-MON; -.
DR BioCyc; YEAST:YMR008C-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:P39105; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P39105; 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:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042597; C:periplasmic space; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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:0006650; P:glycerophospholipid metabolic process; IMP:SGD.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IMP: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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..634
FT /note="Lysophospholipase 1"
FT /id="PRO_0000024646"
FT PROPEP 635..664
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372442"
FT DOMAIN 35..586
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT LIPID 634
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 32
FT /note="A -> S (in Ref. 1; AAA61611)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="S -> P (in Ref. 4; AAT92807)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="E -> D (in Ref. 1; AAA61611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 71667 MW; E05A585E7AB73F34 CRC64;
MKLQSLLVSA AVLTSLTENV NAWSPNNSYV PANVTCDDDI NLVREASGLS DNETEWLKKR
DAYTKEALHS FLNRATSNFS DTSLLSTLFG SNSSNMPKIA VACSGGGYRA MLSGAGMLAA
MDNRTDGANE HGLGGLLQGA TYLAGLSGGN WLTSTLAWNN WTSVQAIVDN TTESNSIWDI
SHSILTPDGI NIFKTGSRWD DISDDVQDKK DAGFNISLAD VWGRALAYNF WPSLHRGGVG
YTWSTLREAD VFKNGEMPFP ITVADGRYPG TTVINLNATL FEFNPFEMGS WDPTLNAFTD
VKYLGTNVTN GKPVNKGQCI AGFDNTGFIT ATSSTLFNQF LLRLNSTDLP SFIANLATDF
LEDLSDNSDD IAIYAPNPFK EANFLQKNAT SSIIESEYLF LVDGGEDNQN IPLVPLLQKE
RELDVIFALD NSADTDDYWP DGASLVNTYQ RQFGSQGLNL SFPYVPDVNT FVNLGLNKKP
TFFGCDARNL TDLEYIPPLI VYIPNSRHSF NGNQSTFKMS YSDSERLGMI KNGFEAATMG
NFTDDSDFLG CVGCAIIRRK QQNLNATLPS ECSQCFTNYC WNGTIDSRSV SGVGNDDYSS
SASLSASAAA ASASASASAS ASASASGSST HKKNAGNALV NYSNLNTNTF IGVLSVISAV
FGLI
