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Q11087 (PLC12_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-12

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-12
ORF Names:C01C10.3
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
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
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlipid storage

Inferred from mutant phenotype. Source: WormBase

phospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 391391Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-12
PRO_0000065097

Regions

Transmembrane47 – 6721Helical; Potential
Transmembrane84 – 10421Helical; Potential
Motif124 – 1296HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q11087 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: FB5C062A0172A8C1

FASTA39144,718
        10         20         30         40         50         60 
MLKSGLMDTD DQKVGVRVAN IDMSERTDNV HLIEIRRIIS LVGAAYFFFM TAWVVPVACV 

        70         80         90        100        110        120 
ITVSLLFPLM LFSTPLFNYL EHKLCAMVNA HWNAVSVFVG ATVTEYGTNL AGYAEEKCLL 

       130        140        150        160        170        180 
LANHLGLLDH FVLMQSLNGK GSIRSRWMWV IYNIWKYTPL GVMWTSHGNF FVNGGVSKRD 

       190        200        210        220        230        240 
SVLSSFRDHL KNSFYKYDYG WVIMYPEGSR LYLVKNSGRT FAEKNGLKPL DNCVYPRTGA 

       250        260        270        280        290        300 
AHAVLDVLGP TDDSLSMSKC GKGEPIKYII DATIGYRKGA VPDICDVMMG DWESVEASQF 

       310        320        330        340        350        360 
AVHYDVIPVK PEWSDENLLK EFLYERYIIK DKLLAEFYKT GHFPGDKTKV IPNNYEMMFA 

       370        380        390 
QVFWGCLYYA HYVYWLRPLI VHSWTSFLSI F 

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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

EMBL
GenBank
DDBJ
FO080255 Genomic DNA. Translation: CCD62384.1.
PIRT15366.
RefSeqNP_509260.1. NM_076859.3.
UniGeneCel.7660.

3D structure databases

ProteinModelPortalQ11087.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC01C10.3.1; C01C10.3.1; C01C10.3.
C01C10.3.2; C01C10.3.2; C01C10.3.
GeneID181001.
KEGGcel:C01C10.3.
NMPDRfig|6239.3.peg.23768.
UCSCC01C10.3. c. elegans.

Organism-specific databases

CTD181001.
WormBaseC01C10.3; CE02449; WBGene00015295; acl-12.

Phylogenomic databases

eggNOGmeNOG07015.
GeneTreeEMGT00050000014205.
HOGENOMHBG388516.
InParanoidQ11087.
OMAWVIYNIW.
PhylomeDBQ11087.

Gene expression databases

ArrayExpressQ11087.

Family and domain databases

InterProIPR002123. Acyltransferase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio911926.

Entry information

Entry namePLC12_CAEEL
AccessionPrimary (citable) accession number: Q11087
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis 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