Reviewed,
UniProtKB/Swiss-Prot Q42670 (PLSC_COCNU)
Last modified
June 16, 2009.
Version 38.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 1-acyl-sn-glycerol-3-phosphate acyltransferase Short name=1-AGP acyltransferase Short name=1-AGPAT EC=2.3.1.51 Alternative name(s): Lysophosphatidic acid acyltransferase Short name=LPAAT |
| Organism | Cocos nucifera (Coconut) |
| Taxonomic identifier | 13894 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Arecaceae › Arecoideae › Cocoseae › Attaleinae › Cocos |
Protein attributes
| Sequence length | 308 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. This enzyme shows a preference for medium-chain-length fatty acyl-coenzyme a substrates. |
| Catalytic activity | Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. |
| Subcellular location | Membrane; Multi-pass membrane protein Potential. |
| Domain | The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity. |
| Sequence similarities | Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phospholipid biosynthesis |
| Cellular component | Membrane |
| Domain | Transmembrane |
| Molecular function | Acyltransferase Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 1-acylglycerol-3-phosphate O-acyltransferase 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 – 308 | 308 | 1-acyl-sn-glycerol-3-phosphate acyltransferase | PRO_0000208185 | |||||
Regions | |||||||||
| Transmembrane | 65 – 85 | 21 | Potential | ||||||
| Transmembrane | 124 – 144 | 21 | Potential | ||||||
| Transmembrane | 148 – 168 | 21 | Potential | ||||||
| Motif | 130 – 135 | 6 | HXXXXD motif | ||||||
Sequences
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References
| [1] | "Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates." Knutzon D.S., Lardizabal K.D., Nelsen J.S., Bleibaum J.L., Davies H.M., Metz J.G. Plant Physiol. 109:999-1006(1995) [PubMed: 8552723] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Endosperm. |
Cross-references
Sequence databases | |
|---|---|
| U29657 mRNA. Translation: AAC49119.1. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.51. 118852. |
Family and domain databases | |
| InterPro | IPR002123. Acyltransferase. IPR004552. AGP_acyltrans. [Graphical view] |
| Pfam | PF01553. Acyltransferase. 1 hit. [Graphical view] |
| SMART | SM00563. PlsC. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00530. AGP_acyltrn. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PLSC_COCNU | ||||||||
| Accession | Primary (citable) accession number: Q42670 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


