P0C957 · PLB1_ASPFU
- ProteinLysophospholipase 1
- Geneplb1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids633 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Catalyzes the release of fatty acids from lysophospholipids.
Catalytic activity
- a 1-acyl-sn-glycero-3-phosphocholine + H2O = sn-glycerol 3-phosphocholine + a fatty acid + H+
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 | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | lysophospholipase activity | |
Molecular Function | phospholipase A2 activity | |
Biological Process | glycerophospholipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLysophospholipase 1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionP0C957
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 498 | in strain: ATCC 90240 / AF-10 | ||||
Sequence: S → N | ||||||
Natural variant | 590-593 | in strain: ATCC 90240 / AF-10 | ||||
Sequence: DGSL → NGTV |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
Protein family/group databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKTTTVACAVAGLLFSCVSG | ||||||
Chain | PRO_0000245555 | 21-609 | Lysophospholipase 1 | |||
Sequence: APDPVHVEIQQRALPNAPDGYTPSTVGCPASRPTIRSAASLSPNETSWLETRRGKTTSAMKDFFNHVKIQDFDAAGYIDRHSSNSSDLPNIGIAVSGGGYRALMNGAGAIKAFDSRTPNSTSAGQLGGLLQSATYLSGLSGGSWLVGSIYINNFTTISALQTHQKGTVWQFQNSIFEGPDGGSIQILDSATYYRDISNAVSGKSDAGYPTSITDYWGRALSYQMINATNGGPSYTWSSIALTDAFQKAEMPMPLVVADGRYPGELLISSNATVYEFNPWEFGTFDPTVFGFAPLEYLGTKFNGGSVPSNESCVRGFDNVGFVMGTSSTLFNQFLLQINSTALPDWLKSVFTDILKDIGENDEDIAQYAPNPFYHFSNTTNPSAAELELDLVDGGEDLQNIPLHPLIQPERHVDVIFAVDSSADTTYSWPNGTALVATYERSLNSSGIANGTSFPAIPDQNTFVNKGLNTRPTFFGCNSSNTTGPSPLIVYLPNYPYTAYSNFSTFQPDYTEQERDSTILNGYDVVTMGNSTRDGNWSTCVGCAILSRSLERTNTNVPEICKQCFQRYCWDGSLNSTTPAGYEPVTILDS | ||||||
Glycosylation | 64 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 139 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 173 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 290 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 329 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 358 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 397 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 450 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 463 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 469 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 497 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 500 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 521 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 549 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 555 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 594 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 609 | GPI-like-anchor amidated serine | ||||
Sequence: S | ||||||
Propeptide | PRO_0000245556 | 610-633 | Removed in mature form | |||
Sequence: AASGIIPSISTVAMAVVFAAWTIF |
Post-translational modification
The GPI-like anchor contains a phosphoceramide lipid group.
Keywords
- PTM
PTM databases
Expression
Induction
Induced by lecithin.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-594 | PLA2c | ||||
Sequence: GCPASRPTIRSAASLSPNETSWLETRRGKTTSAMKDFFNHVKIQDFDAAGYIDRHSSNSSDLPNIGIAVSGGGYRALMNGAGAIKAFDSRTPNSTSAGQLGGLLQSATYLSGLSGGSWLVGSIYINNFTTISALQTHQKGTVWQFQNSIFEGPDGGSIQILDSATYYRDISNAVSGKSDAGYPTSITDYWGRALSYQMINATNGGPSYTWSSIALTDAFQKAEMPMPLVVADGRYPGELLISSNATVYEFNPWEFGTFDPTVFGFAPLEYLGTKFNGGSVPSNESCVRGFDNVGFVMGTSSTLFNQFLLQINSTALPDWLKSVFTDILKDIGENDEDIAQYAPNPFYHFSNTTNPSAAELELDLVDGGEDLQNIPLHPLIQPERHVDVIFAVDSSADTTYSWPNGTALVATYERSLNSSGIANGTSFPAIPDQNTFVNKGLNTRPTFFGCNSSNTTGPSPLIVYLPNYPYTAYSNFSTFQPDYTEQERDSTILNGYDVVTMGNSTRDGNWSTCVGCAILSRSLERTNTNVPEICKQCFQRYCWDGSLN |
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.
- Length633
- Mass (Da)68,144
- Last updated2009-05-05 v1
- Checksum277A47E29FD74796
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF223004 EMBL· GenBank· DDBJ | AAF64038.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AAHF01000005 EMBL· GenBank· DDBJ | EAL89914.1 EMBL· GenBank· DDBJ | Genomic DNA |