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Reviewed, UniProtKB/Swiss-Prot Q5E9R2 (PLCD_BOVIN)

Last modified October 13, 2009. Version 25. 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length378 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
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_0000239116

Regions

Transmembrane11 – 3121 Potential
Transmembrane125 – 14521 Potential
Transmembrane307 – 32721 Potential
Transmembrane338 – 35821 Potential
Motif96 – 1016HXXXXD motif

Experimental info

Sequence conflict2901R → H in AAX08708. Ref.1
Sequence conflict3271I → V in AAX08708. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5E9R2-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 2E7903D835D7F0A5

FASTA37843,907
        10         20         30         40         50         60 
MDLVALLKSH FLCHLIFCYV FIVSGLIINT IQLCTLLLWP VNKQLFRKIN CRLSYCVSSQ 

        70         80         90        100        110        120 
LVMLLEWWSG TECVIYTDPR AYPKYGKENA IVVLNHKFEI DFLCGWSLAE RFGVLGGSKV 

       130        140        150        160        170        180 
LAKKELAYVP IIGWMWYFTE MVFCTRKWEQ DRKTVSESLL HLRDYPEKYF FLIHCEGTRF 

       190        200        210        220        230        240 
TEKKHQISMQ VAQAKGLPSL KHHLLPRTKG FAVTVRSLRN VVSAVYDCTL NFRNNENPTL 

       250        260        270        280        290        300 
LGVLNGKKYH ADLYVRRIPL EEVPEEEDKC AAWLHKLYQE KDAFQEEYSR TGTFPETPVV 

       310        320        330        340        350        360 
PPRRPWTLVN WLFWASMLLY PFFRFVINMV SSGSSLTLAS FVLVFFVASM GVRWMIGVTE 

       370 
IDKGSAYGNM DSKQKHSD 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

BT020691 mRNA. Translation: AAX08708.1.
BT020858 mRNA. Translation: AAX08875.1.
IPIIPI00694418.
UniGeneBt.25871

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5E9R2.

Genome annotation databases

EnsemblENSBTAT00000010089; ENSBTAP00000010089; ENSBTAG00000007668; Bos taurus. [Genome view]

Phylogenomic databases

HOVERGENQ5E9R2.

Enzyme and pathway databases

BRENDA2.3.1.51. 251.

Family and domain databases

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

Entry information

Entry namePLCD_BOVIN
AccessionPrimary (citable) accession number: Q5E9R2
Secondary accession number(s): Q5EA78
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 15, 2005
Last modified: October 13, 2009
This is version 25 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