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Reviewed, UniProtKB/Swiss-Prot Q5RA57 (PLCC_PONAB)

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 gamma
    EC=2.3.1.51
Alternative name(s):
    1-acylglycerol-3-phosphate O-acyltransferase 3
      Short name=1-AGP acyltransferase 3
      Short name=1-AGPAT 3
    Lysophosphatidic acid acyltransferase gamma
      Short name=LPAAT-gamma
Gene names
Name: AGPAT3
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length376 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 – 3763761-acyl-sn-glycerol-3-phosphate acyltransferase gamma
PRO_0000208196

Regions

Transmembrane11 – 3121 Potential
Transmembrane124 – 14421 Potential
Transmembrane308 – 33023 Potential
Transmembrane335 – 35723 Potential
Motif96 – 1016HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q5RA57-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 847A5A1442081A79

FASTA37643,365
        10         20         30         40         50         60 
MGLLAFLKTQ FVLHPLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN CRLAYSLWSQ 

        70         80         90        100        110        120 
LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI DFLCGWTMCE RFGVLGSSKV 

       130        140        150        160        170        180 
LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF 

       190        200        210        220        230        240 
TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL 

       250        260        270        280        290        300 
LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK 

       310        320        330        340        350        360 
PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE 

       370 
IEKGSSYGNQ EFKKKE 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

CR859164 mRNA. Translation: CAH91353.1.
RefSeqNP_001127407.1.
UniGenePab.8061

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID100174477.

Organism-specific databases

CTD100174477.

Phylogenomic databases

HOVERGENQ5RA57.

Enzyme and pathway databases

BRENDA2.3.1.51. 269192.

Family and domain databases

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

Entry information

Entry namePLCC_PONAB
AccessionPrimary (citable) accession number: Q5RA57
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 21, 2004
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