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Q924S1 (PLCD_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
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) [Reference proteome]
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3783781-acyl-sn-glycerol-3-phosphate acyltransferase delta
PRO_0000208199

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q924S1 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB067572 mRNA. Translation: BAB62290.1.
BC086992 mRNA. Translation: AAH86992.1.
RefSeqNP_596897.1. NM_133406.1.
XP_006227919.1. XM_006227857.1.
UniGeneRn.41595.

3D structure databases

ProteinModelPortalQ924S1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000024213.

Proteomic databases

PRIDEQ924S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024213; ENSRNOP00000024213; ENSRNOG00000017731.
GeneID170919.
KEGGrno:170919.

Organism-specific databases

CTD56895.
RGD619916. Agpat4.

Phylogenomic databases

eggNOGCOG0204.
GeneTreeENSGT00530000062943.
HOGENOMHOG000006110.
HOVERGENHBG008205.
InParanoidQ924S1.
KOK13523.
OMAPEKYFFL.
OrthoDBEOG7H7928.
PhylomeDBQ924S1.
TreeFamTF314065.

Enzyme and pathway databases

UniPathwayUPA00557; UER00613.

Gene expression databases

GenevestigatorQ924S1.

Family and domain databases

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

Other

NextBio621403.
PROQ924S1.

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: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways