Q08108 · PLB3_YEAST
- ProteinLysophospholipase 3
- GenePLB3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids686 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol. Does not cleave phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and phosphatidylinositol-bisphosphate (PubMed:10497163).
Mainly responsible for the degradation of phosphatidylinositol in vivo (PubMed:15588231).
Mainly responsible for the degradation of phosphatidylinositol in vivo (PubMed:15588231).
Catalytic activity
- a 1-acyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + a fatty acid + H+This reaction proceeds in the forward direction.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular region | |
Cellular Component | fungal-type vacuole | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | lysophospholipase activity | |
Molecular Function | phospholipase A2 activity | |
Biological Process | glycerophospholipid catabolic process | |
Biological Process | phosphatidylinositol metabolic process | |
Biological Process | phosphatidylserine catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLysophospholipase 3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ08108
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MIRPLCSKIIISYIFAISQFLLAANA | ||||||
Chain | PRO_0000024648 | 27-659 | Lysophospholipase 3 | |||
Sequence: WSPTDSYVPGTVSCPDDINLVREATSISQNESAWLEKRNKVTSVALKDFLTRATANFSDSSEVLSKLFNDGNSENLPKIAVAVSGGGYRSMLTGAGVLAAMDNRTEGAYEHGLGGLLQSTTYLSGASGGNWLVGTLALNNWTSVQDILNNMQNDDSIWDLSDSIVTPGGINIFKTAKRWDHISNAVESKQNADYNTSLADIWGRALAYNFFPSLNRGGIGLTWSSIRDFPVFQNAEMPFPISVADGRYPGTKVINLNATVFEFNPFEMGSWDPSLNSFANVKYLGTNVSNGVPLERGKCTAGFDNAGFIMGTSSTLFNQFLLRINSTHLPSFITRLARHFLKDLSQDFNDIAVYSPNPFKDTKFLDSDYTTSIVDSDSLFLVDGGEDDENVPVLPLIQKERDVDIIFAVDNSADMRLAWPDGSSLVHTYERQFVKQGQGMSFPYVPDTNTFVNLGLNKKPTFFGCDANNLTDLQYIPPLVVYLPNAEYSFNSNQSAFKLSYSESQRRSMIQNGFEIATRNNFTDDPEFMGCVGCAIIRRKQQALNITLPPECETCFKNYCWNGTLDTTPLPDVEKDVHHSFINVNSFNSSIGQEESLYAGSSASQSSSSSSSSSSSSEIPSATATLEKKAATN | ||||||
Glycosylation | 56 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 82 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 129 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 166 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 221 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 283 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 313 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 351 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 495 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 519 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 547 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 571 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 588 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 614 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 659 | GPI-anchor amidated asparagine | ||||
Sequence: N | ||||||
Propeptide | PRO_0000372444 | 660-686 | Removed in mature form | |||
Sequence: SGSHLSGISVKFSAMIMLTLLMFTGAV |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-592 | PLA2c | ||||
Sequence: SCPDDINLVREATSISQNESAWLEKRNKVTSVALKDFLTRATANFSDSSEVLSKLFNDGNSENLPKIAVAVSGGGYRSMLTGAGVLAAMDNRTEGAYEHGLGGLLQSTTYLSGASGGNWLVGTLALNNWTSVQDILNNMQNDDSIWDLSDSIVTPGGINIFKTAKRWDHISNAVESKQNADYNTSLADIWGRALAYNFFPSLNRGGIGLTWSSIRDFPVFQNAEMPFPISVADGRYPGTKVINLNATVFEFNPFEMGSWDPSLNSFANVKYLGTNVSNGVPLERGKCTAGFDNAGFIMGTSSTLFNQFLLRINSTHLPSFITRLARHFLKDLSQDFNDIAVYSPNPFKDTKFLDSDYTTSIVDSDSLFLVDGGEDDENVPVLPLIQKERDVDIIFAVDNSADMRLAWPDGSSLVHTYERQFVKQGQGMSFPYVPDTNTFVNLGLNKKPTFFGCDANNLTDLQYIPPLVVYLPNAEYSFNSNQSAFKLSYSESQRRSMIQNGFEIATRNNFTDDPEFMGCVGCAIIRRKQQALNITLPPECETCFKNYCWNGTLD |
Sequence similarities
Belongs to the lysophospholipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length686
- Mass (Da)75,077
- Last updated1997-11-01 v1
- Checksum95A2DBF41BF3E20F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z74753 EMBL· GenBank· DDBJ | CAA99010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006948 EMBL· GenBank· DDBJ | DAA10772.1 EMBL· GenBank· DDBJ | Genomic DNA |