Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q924S1 (PLCD_RAT)

Last modified January 19, 2010. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    1-acyl-sn-glycerol-3-phosphate acyltransferase delta
    EC=2.3.1.51
Alternative name(s):
    1-acylglycerol-3-phosphate O-acyltransferase 4
      Short name=1-AGP acyltransferase 4
      Short name=1-AGPAT 4
    Lysophosphatidic acid acyltransferase delta
      Short name=LPAAT-delta
Gene names
Name: Agpat4
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length378 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
   Molecular functionAcyltransferase
Transferase
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 – 3783781-acyl-sn-glycerol-3-phosphate acyltransferase delta
PRO_0000208199

Regions

Transmembrane11 – 3121 Potential
Transmembrane125 – 14521 Potential
Transmembrane311 – 33121 Potential
Transmembrane338 – 35821 Potential
Motif96 – 1016HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q924S1-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 389AA01B7327AE2B

FASTA37843,794
        10         20         30         40         50         60 
MDLIGLLKSQ FLCHLVFCYV FIASGLIVNA IQLCTLVIWP INKQLFRKIN ARLCYCVSSQ 

        70         80         90        100        110        120 
LVMLLEWWSG TECTIYTDPK ASPHYGKENA IVVLNHKFEI DFLCGWSLAE RLGILGNSKV 

       130        140        150        160        170        180 
LAKKELAYVP IIGWMWYFVE MIFCTRKWEQ DRQTVAKSLL HLRDYPEKYL FLIHCEGTRF 

       190        200        210        220        230        240 
TEKKHQISMQ VAQAKGLPSL KHHLLPRTKG FAITVKCLRD VVPAVYDCTL NFRNNENPTL 

       250        260        270        280        290        300 
LGVLNGKKYH ADCYVRRIPM EDIPEDEDKC SAWLHKLYQE KDAFQEEYYR TGVFPETPWV 

       310        320        330        340        350        360 
PPRRPWSLVN WLFWASLLLY PFFQFLVSMV SSGSSVTLAS LVLIFCMASM GVRWMIGVTE 

       370 
IDKGSAYGNI DNKRKQTD 

« Hide

References

« Hide 'large scale' references
[1]"Rattus norvegicus mRNA for lysophosphatidic acid acyltransferase-delta, complete cds."
Li W., Suzuki T.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB067572 mRNA. Translation: BAB62290.1.
BC086992 mRNA. Translation: AAH86992.1.
IPIIPI00205071.
RefSeqNP_596897.1.
UniGeneRn.41595

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ924S1.

Genome annotation databases

EnsemblENSRNOT00000024213; ENSRNOP00000024213; ENSRNOG00000017731; Rattus norvegicus. [Genome view]
GeneID170919.
KEGGrno:170919.
UCSCNM_133406. rat.

Organism-specific databases

CTD170919.
RGD619916. Agpat4.

Phylogenomic databases

eggNOGroNOG06478.
HOVERGENQ924S1.
InParanoidQ924S1.
OMAWMWYFLE.
OrthoDBEOG9DFS6X.
PhylomeDBQ924S1.

Enzyme and pathway databases

BRENDA2.3.1.51. 248.

Gene expression databases

ArrayExpressQ924S1.
GenevestigatorQ924S1.
GermOnlineENSRNOG00000017731. Rattus norvegicus.

Family and domain databases

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

Other Resources

NextBio621403.

Entry information

Entry namePLCD_RAT
AccessionPrimary (citable) accession number: Q924S1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 1, 2001
Last modified: January 19, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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