Q42870 (PLSC_LIMDO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 51.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | ||
| Gene names |
| ||
| Organism | Limnanthes douglasii (Douglas's meadowfoam) | ||
| Taxonomic identifier | 28973 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Limnanthaceae › Limnanthes |
Protein attributes
| Sequence length | 281 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. This enzyme uses erucoyl-CoA as an acyl donor. |
| Catalytic activity | Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. |
| Pathway | |
| 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 Transmembrane helix |
| Molecular function | Acyltransferase Transferase |
| 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 – 281 | 281 | 1-acyl-sn-glycerol-3-phosphate acyltransferase | PRO_0000208187 | |||||
Regions | |||||||||
| Transmembrane | 40 – 60 | 21 | Helical; Potential | ||||||
| Transmembrane | 71 – 91 | 21 | Helical; Potential | ||||||
| Transmembrane | 110 – 130 | 21 | Helical; Potential | ||||||
| Motif | 109 – 114 | 6 | HXXXXD motif | ||||||
Experimental info | |||||||||
| Sequence conflict | 46 | 1 | I → V in CAA86877. Ref.2 | ||||||
| Sequence conflict | 188 | 1 | R → G in CAA86877. Ref.2 | ||||||
| Sequence conflict | 262 | 1 | V → I in CAA86877. Ref.2 | ||||||
| Sequence conflict | 281 | 1 | N → K in CAA86877. Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant." Hanke C., Wolter F.P., Coleman J., Peterek G., Frentzen M. Eur. J. Biochem. 232:806-810(1995) [PubMed: 7588719] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Identification of a cDNA that encodes a 1-acyl-sn-glycerol-3-phosphate acyltransferase from Limnanthes douglasii." Brown A.P., Brough C.L., Kroon J., Slabas A.R. Plant Mol. Biol. 29:267-278(1995) [PubMed: 7579178] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X83266 mRNA. Translation: CAA58239.1. Z46836 mRNA. Translation: CAA86877.1. |
| PIR | S60477. |
3D structure databases | |
| ProteinModelPortal | Q42870. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.3.1.51. 3028. |
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_LIMDO | ||||||||
| Accession | Primary (citable) accession number: Q42870 Secondary accession number(s): Q40120 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with