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Reviewed, UniProtKB/Swiss-Prot Q93841 (PLC1_CAEEL)

Last modified November 3, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1
      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
Name: acl-1
ORF Names: F59F4.4
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone By similarity.

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

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 processPhospholipid biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function1-acylglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1
PRO_0000208202

Regions

Transmembrane3 – 2321 Potential
Transmembrane29 – 4921 Potential
Transmembrane89 – 10921 Potential
Motif94 – 996HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q93841-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 0361FE6C9710593E

FASTA26229,638
        10         20         30         40         50         60 
MTFLAILFVI AVLLLLAQLP VIGFYIRAVY FGMCLIIGGF LGGLASIPFG KSPNNHFRMF 

        70         80         90        100        110        120 
KIFQAMTWPM GVRFELRNSE ILHDKKPYII IANHQSALDV LGMSFAWPVD CVVMLKSSLK 

       130        140        150        160        170        180 
YLPGFNLCAY LCDSVYINRF SKEKALKTVD TTLHEIVTKK RKVWIYPEGT RNAEPELLPF 

       190        200        210        220        230        240 
KKGAFILAKQ AKIPIVPCVF SSHKFFYSHA EKRLTSGNCI IDILPEVDSS KFDSIDDLSA 

       250        260 
HCRKIMQAHR EKLDAEAANL NI 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.

Cross-references

Sequence databases

Z81095, Z81089 Genomic DNA. Translation: CAB03160.1.
Z81089, Z81095 Genomic DNA. Translation: CAB03139.1.
PIRT22599.
RefSeqNP_510606.1.
UniGeneCel.823

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ93841.

Genome annotation databases

EnsemblF59F4.4; F59F4.4; F59F4.4; Caenorhabditis elegans. [Genome view]
GeneID181671.
KEGGcel:F59F4.4.
NMPDRfig|6239.3.peg.25503.
UCSCF59F4.4. c. elegans.

Organism-specific databases

CTD181671.
WormBaseWBGene00010339. acl-1.
WormPepF59F4.4. CE11552. [WorfDB]

Phylogenomic databases

OMAPRDYRNA.

Enzyme and pathway databases

BRENDA2.3.1.51. 672.

Gene expression databases

ArrayExpressQ93841.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR004552. AGP_acyltrans.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Other Resources

NextBio914894.

Entry information

Entry namePLC1_CAEEL
AccessionPrimary (citable) accession number: Q93841
Secondary accession number(s): Q93783
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 3, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents