A2WT95 · PLA1_ORYSI
- ProteinPhospholipase A1-II 1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids393 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 225 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 225 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 284 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 321 | Charge relay system | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | phospholipase A1 activity | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePhospholipase A1-II 1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionA2WT95
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000409363 | 1-393 | Phospholipase A1-II 1 | |||
Sequence: MSSLRGLGNIARRWRELNGVSYWKGLLDPLDVDLRNNIINYGELSQAAYTGLNRERRSRYAGSCLFSRKDFLSRVDVSNPNLYVITKFIYAMCTVSLPDAFMIKSWSKAAWSKQSNWMGFVAVATDEGKEVLGRRDVVVAWRGTIRMVEWMDDLDISLVPASEIVRPGSADDPCVHGGWLSVYTSADPESQYNKQSARYQVLNEIKRLQDMYEHEETSITITGHSLGAALATINATDIVSNGYNKSCPVSAFVFGSPRVGNPDFQKAFDSAPDLRLLRIRNSPDVVPNWPKLGYSDAGTELMIDTGKSPYLKAPGNPLTWHDMECYMHGVAGTQGSNGGFKLEIDRDIALVNKHEDALKNEYAIPSSWWVVQNKGMVKGTDGRWHLADHEDDD |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 200-220 | |||||
Sequence: QVLNEIKRLQDMYEHEETSIT |
Sequence similarities
Belongs to the AB hydrolase superfamily. Lipase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length393
- Mass (Da)43,956
- Last updated2011-05-31 v2
- Checksum8855CF6335E57BB0
Sequence caution
Keywords
- Technical term