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Protein

Lysophospholipase 1

Gene

PLB1

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.2 Publications

Catalytic activityi

2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate.

GO - Molecular functioni

  1. lysophospholipase activity Source: SGD

GO - Biological processi

  1. glycerophospholipid metabolic process Source: SGD
  2. phosphatidylcholine acyl-chain remodeling Source: SGD
  3. phospholipid catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:YMR008C-MONOMER.
YEAST:YMR008C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipase 1 (EC:3.1.1.5)
Alternative name(s):
Phospholipase B 1
Gene namesi
Name:PLB1
Ordered Locus Names:YMR008C
ORF Names:YM8270.10C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR008c.
SGDiS000004610. PLB1.

Subcellular locationi

Cell membrane 2 Publications; Lipid-anchorGPI-anchor 2 Publications

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. endoplasmic reticulum Source: SGD
  3. periplasmic space Source: SGD
  4. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 634612Lysophospholipase 1PRO_0000024646Add
BLAST
Propeptidei635 – 66430Removed in mature formSequence AnalysisPRO_0000372442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi26 – 261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi565 – 5651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
Lipidationi634 – 6341GPI-anchor amidated asparagineSequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP39105.
PaxDbiP39105.
PeptideAtlasiP39105.

Expressioni

Gene expression databases

GenevestigatoriP39105.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
YHR080CP388001EBI-13462,EBI-24597

Protein-protein interaction databases

BioGridi35177. 22 interactions.
DIPiDIP-2804N.
IntActiP39105. 2 interactions.
MINTiMINT-1717589.
STRINGi4932.YMR008C.

Structurei

3D structure databases

ProteinModelPortaliP39105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 586552PLA2cPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi587 – 62943Ala/Ser-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG271081.
GeneTreeiENSGT00510000051940.
HOGENOMiHOG000189547.
InParanoidiP39105.
KOiK13333.
OMAiYQFINAS.
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.

P39105-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLQSLLVSA AVLTSLTENV NAWSPNNSYV PANVTCDDDI NLVREASGLS
60 70 80 90 100
DNETEWLKKR DAYTKEALHS FLNRATSNFS DTSLLSTLFG SNSSNMPKIA
110 120 130 140 150
VACSGGGYRA MLSGAGMLAA MDNRTDGANE HGLGGLLQGA TYLAGLSGGN
160 170 180 190 200
WLTSTLAWNN WTSVQAIVDN TTESNSIWDI SHSILTPDGI NIFKTGSRWD
210 220 230 240 250
DISDDVQDKK DAGFNISLAD VWGRALAYNF WPSLHRGGVG YTWSTLREAD
260 270 280 290 300
VFKNGEMPFP ITVADGRYPG TTVINLNATL FEFNPFEMGS WDPTLNAFTD
310 320 330 340 350
VKYLGTNVTN GKPVNKGQCI AGFDNTGFIT ATSSTLFNQF LLRLNSTDLP
360 370 380 390 400
SFIANLATDF LEDLSDNSDD IAIYAPNPFK EANFLQKNAT SSIIESEYLF
410 420 430 440 450
LVDGGEDNQN IPLVPLLQKE RELDVIFALD NSADTDDYWP DGASLVNTYQ
460 470 480 490 500
RQFGSQGLNL SFPYVPDVNT FVNLGLNKKP TFFGCDARNL TDLEYIPPLI
510 520 530 540 550
VYIPNSRHSF NGNQSTFKMS YSDSERLGMI KNGFEAATMG NFTDDSDFLG
560 570 580 590 600
CVGCAIIRRK QQNLNATLPS ECSQCFTNYC WNGTIDSRSV SGVGNDDYSS
610 620 630 640 650
SASLSASAAA ASASASASAS ASASASGSST HKKNAGNALV NYSNLNTNTF
660
IGVLSVISAV FGLI
Length:664
Mass (Da):71,667
Last modified:February 1, 1996 - v2
Checksum:iE05A585E7AB73F34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → S in AAA61611. (PubMed:8051052)Curated
Sequence conflicti93 – 931S → P in AAT92807. (PubMed:17322287)Curated
Sequence conflicti494 – 4941E → D in AAA61611. (PubMed:8051052)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23089 Genomic DNA. Translation: AAA61611.1.
Z48613 Genomic DNA. Translation: CAA88523.1.
AY692788 Genomic DNA. Translation: AAT92807.1.
BK006946 Genomic DNA. Translation: DAA09906.1.
PIRiS53037.
RefSeqiNP_013721.1. NM_001182504.1.

Genome annotation databases

EnsemblFungiiYMR008C; YMR008C; YMR008C.
GeneIDi855020.
KEGGisce:YMR008C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23089 Genomic DNA. Translation: AAA61611.1.
Z48613 Genomic DNA. Translation: CAA88523.1.
AY692788 Genomic DNA. Translation: AAT92807.1.
BK006946 Genomic DNA. Translation: DAA09906.1.
PIRiS53037.
RefSeqiNP_013721.1. NM_001182504.1.

3D structure databases

ProteinModelPortaliP39105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35177. 22 interactions.
DIPiDIP-2804N.
IntActiP39105. 2 interactions.
MINTiMINT-1717589.
STRINGi4932.YMR008C.

Proteomic databases

MaxQBiP39105.
PaxDbiP39105.
PeptideAtlasiP39105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR008C; YMR008C; YMR008C.
GeneIDi855020.
KEGGisce:YMR008C.

Organism-specific databases

CYGDiYMR008c.
SGDiS000004610. PLB1.

Phylogenomic databases

eggNOGiNOG271081.
GeneTreeiENSGT00510000051940.
HOGENOMiHOG000189547.
InParanoidiP39105.
KOiK13333.
OMAiYQFINAS.
OrthoDBiEOG7N37NC.

Enzyme and pathway databases

BioCyciMetaCyc:YMR008C-MONOMER.
YEAST:YMR008C-MONOMER.

Miscellaneous databases

NextBioi978204.

Gene expression databases

GenevestigatoriP39105.

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 Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity."
    Lee K.S., Patton J.L., Fido M., Hines L.K., Kohlwein S.D., Paltauf F., Henry S.A., Levin D.E.
    J. Biol. Chem. 269:19725-19730(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 204508 / S288c.
  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. "Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins."
    Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.
    J. Bacteriol. 181:3886-3889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "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.

Entry informationi

Entry nameiPLB1_YEAST
AccessioniPrimary (citable) accession number: P39105
Secondary accession number(s): D6VZI2, Q6B2E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.