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Protein

Lysophospholipase 2

Gene

PLB2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol > phosphatidylcholine > phosphatidylethanolamine.1 Publication

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

GO - Molecular functioni

  • lysophospholipase activity Source: SGD

GO - Biological processi

  • glycerophospholipid metabolic process Source: SGD
  • phospholipid catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:YMR006C-MONOMER.
YEAST:YMR006C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipase 2 (EC:3.1.1.5)
Alternative name(s):
Phospholipase B 2
Gene namesi
Name:PLB2
Ordered Locus Names:YMR006C
ORF Names:YM8270.08C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIII

Organism-specific databases

CYGDiYMR006c.
EuPathDBiFungiDB:YMR006C.
SGDiS000004608. PLB2.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • extracellular region Source: SGD
  • fungal-type cell wall Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 680661Lysophospholipase 2PRO_0000024647Add
BLAST
Propeptidei681 – 70626Removed in mature formSequence AnalysisPRO_0000372443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi584 – 5841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi630 – 6301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi634 – 6341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi648 – 6481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
Lipidationi680 – 6801GPI-anchor amidated asparagineSequence Analysis

Post-translational modificationi

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ03674.
PaxDbiQ03674.
PeptideAtlasiQ03674.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
YHR080CP388001EBI-2079187,EBI-24597

Protein-protein interaction databases

BioGridi35176. 54 interactions.
STRINGi4932.YMR006C.

Structurei

3D structure databases

ProteinModelPortaliQ03674.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 588553PLA2cPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi369 – 3724Poly-Asp
Compositional biasi657 – 66711Poly-SerAdd
BLAST
Compositional biasi671 – 6744Poly-Ser

Sequence similaritiesi

Belongs to the lysophospholipase family.Curated
Contains 1 PLA2c domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG257248.
GeneTreeiENSGT00510000051940.
HOGENOMiHOG000189547.
InParanoidiQ03674.
KOiK13333.
OMAiITIADIW.
OrthoDBiEOG7N37NC.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
PROSITEiPS51210. PLA2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03674-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLRNILQAS SLISGLSLAA DSSSTTGDGY APSIIPCPSD DTSLVRNASG
60 70 80 90 100
LSTAETDWLK KRDAYTKEAL HSFLSRATSN FSDTSLLSTL FSSNSSNVPK
110 120 130 140 150
IGIACSGGGY RAMLGGAGMI AAMDNRTDGA NEHGLGGLLQ SSTYLSGLSG
160 170 180 190 200
GNWLTGTLAW NNWTSVQEIV DHMSESDSIW NITKSIVNPG GSNLTYTIER
210 220 230 240 250
WESIVQEVQA KSDAGFNISL SDLWARALSY NFFPSLPDAG SALTWSSLRD
260 270 280 290 300
VDVFKNGEMP LPITVADGRY PGTTVINLNA TLFEFTPFEM GSWDPSLNAF
310 320 330 340 350
TDVKYLGTNV TNGKPVNKDQ CVSGYDNAGF VIATSASLFN EFSLEASTST
360 370 380 390 400
YYKMINSFAN KYVNNLSQDD DDIAIYAANP FKDTEFVDRN YTSSIVDADD
410 420 430 440 450
LFLVDGGEDG QNLPLVPLIK KERDLDVVFA LDISDNTDES WPSGVCMTNT
460 470 480 490 500
YERQYSKQGK GMAFPYVPDV NTFLNLGLTN KPTFFGCDAK NLTDLEYIPP
510 520 530 540 550
LVVYIPNTKH SFNGNQSTLK MNYNVTERLG MIRNGFEAAT MGNFTDDSNF
560 570 580 590 600
LGCIGCAIIR RKQESLNATL PPECTKCFAD YCWNGTLSTS ANPELSGNST
610 620 630 640 650
YQSGAIASAI SEATDGIPIT ALLGSSTSGN TTSNSTTSTS SNVTSNSNSS
660 670 680 690 700
SNTTLNSNSS SSSISSSTAR SSSSTANKAN AAAISYANTN TLMSLLGAIT

ALFGLI
Length:706
Mass (Da):75,455
Last modified:November 1, 1997 - v1
Checksum:i5E7BF22C77780DC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129165 Genomic DNA. Translation: AAD28616.1.
Z48613 Genomic DNA. Translation: CAA88521.1.
AY693181 Genomic DNA. Translation: AAT93200.1.
BK006946 Genomic DNA. Translation: DAA09905.1.
PIRiS53035.
RefSeqiNP_013719.1. NM_001182502.1.

Genome annotation databases

EnsemblFungiiYMR006C; YMR006C; YMR006C.
GeneIDi855018.
KEGGisce:YMR006C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129165 Genomic DNA. Translation: AAD28616.1.
Z48613 Genomic DNA. Translation: CAA88521.1.
AY693181 Genomic DNA. Translation: AAT93200.1.
BK006946 Genomic DNA. Translation: DAA09905.1.
PIRiS53035.
RefSeqiNP_013719.1. NM_001182502.1.

3D structure databases

ProteinModelPortaliQ03674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35176. 54 interactions.
STRINGi4932.YMR006C.

Proteomic databases

MaxQBiQ03674.
PaxDbiQ03674.
PeptideAtlasiQ03674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR006C; YMR006C; YMR006C.
GeneIDi855018.
KEGGisce:YMR006C.

Organism-specific databases

CYGDiYMR006c.
EuPathDBiFungiDB:YMR006C.
SGDiS000004608. PLB2.

Phylogenomic databases

eggNOGiNOG257248.
GeneTreeiENSGT00510000051940.
HOGENOMiHOG000189547.
InParanoidiQ03674.
KOiK13333.
OMAiITIADIW.
OrthoDBiEOG7N37NC.

Enzyme and pathway databases

BioCyciMetaCyc:YMR006C-MONOMER.
YEAST:YMR006C-MONOMER.

Miscellaneous databases

NextBioi978201.
PROiQ03674.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF01735. PLA2_B. 1 hit.
[Graphical view]
SMARTiSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 1 hit.
PROSITEiPS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The PLB2 gene of Saccharomyces cerevisiae confers resistance to lysophosphatidylcholine and encodes a phospholipase B/lysophospholipase."
    Fyrst H., Oskouian B., Kuypers F.A., Saba J.D.
    Biochemistry 38:5864-5871(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: DG338.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Characterization and function in vivo of two novel phospholipases B/lysophospholipases from Saccharomyces cerevisiae."
    Merkel O., Fido M., Mayr J.A., Prueger H., Raab F., Zandonella G., Kohlwein S.D., Paltauf F.
    J. Biol. Chem. 274:28121-28127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages."
    Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M., de Koster C.G.
    J. Biol. Chem. 280:20894-20901(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GPI-ANCHOR.

Entry informationi

Entry nameiPLB2_YEAST
AccessioniPrimary (citable) accession number: Q03674
Secondary accession number(s): D6VZI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 623 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.