Reviewed,
UniProtKB/Swiss-Prot A1C9L6 (NTE1_ASPCL)
Last modified
June 16, 2009.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Lysophospholipase nte1 EC=3.1.1.5 Alternative name(s): Neuropathy target esterase homolog Intracellular phospholipase B | ||||
| Gene names |
| ||||
| Organism | Aspergillus clavatus [Complete proteome] | ||||
| Taxonomic identifier | 5057 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 1528 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis. Responsible for the rapid PC turnover in response to inositol, elevated temperatures, or when choline is present in the growth medium By similarity. |
| Catalytic activity | 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate. |
| Enzyme regulation | Inhibited by organophosphorus esters By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the NTE family. Contains 2 cyclic nucleotide-binding domains. Contains 1 patatin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation Lipid metabolism |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Repeat Transmembrane |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylcholine metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | lysophospholipase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1528 | 1528 | Lysophospholipase nte1 | PRO_0000295309 | |||||
Regions | |||||||||
| Topological domain | 1 – 72 | 72 | Cytoplasmic By similarity | ||||||
| Transmembrane | 73 – 93 | 21 | Potential | ||||||
| Topological domain | 94 – 115 | 22 | Lumenal By similarity | ||||||
| Transmembrane | 116 – 136 | 21 | Potential | ||||||
| Topological domain | 137 – 1528 | 1392 | Cytoplasmic By similarity | ||||||
| Domain | 1225 – 1389 | 165 | Patatin | ||||||
| Nucleotide binding | 686 – 805 | 120 | cNMP 1 | ||||||
| Nucleotide binding | 846 – 966 | 121 | cNMP 2 | ||||||
| Motif | 1256 – 1260 | 5 | GXSXG | ||||||
| Compositional bias | 21 – 33 | 13 | Poly-Ser | ||||||
| Compositional bias | 59 – 64 | 6 | Poly-Pro | ||||||
| Compositional bias | 298 – 307 | 10 | Poly-Ser | ||||||
Sites | |||||||||
| Active site | 1258 | 1 | By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. Nierman W.C.PLoS Genet. 4:E1000046-E1000046(2008) [PubMed: 18404212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1. |
Cross-references
Sequence databases | |
|---|---|
| DS027048 Genomic DNA. Translation: EAW13540.1. Different initiation. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.5. 18580. |
Family and domain databases | |
| InterPro | IPR000595. cNMP_bd. IPR018488. cNMP_bd_CS. IPR001423. Lysophospholipase_patatin_CS. IPR002641. Patatin. [Graphical view] |
| Pfam | PF00027. cNMP_binding. 2 hits. PF01734. Patatin. 1 hit. [Graphical view] |
| SMART | SM00100. cNMP. 1 hit. [Graphical view] |
| PROSITE | PS00888. CNMP_BINDING_1. False negative. PS00889. CNMP_BINDING_2. False negative. PS50042. CNMP_BINDING_3. 2 hits. PS01237. UPF0028. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NTE1_ASPCL | ||||||||
| Accession | Primary (citable) accession number: A1C9L6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


