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Reviewed, UniProtKB/Swiss-Prot Q9XFW4 (LPAT2_BRANA)

Last modified October 13, 2009. Version 40. 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 2
    EC=2.3.1.51
Alternative name(s):
    Lysophosphatidyl acyltransferase 2
Gene names
Name: LPAT2
Synonyms: LPAAT2
OrganismBrassica napus (Rape)
Taxonomic identifier3708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeBrassica

Protein attributes

Sequence length390 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 acyl moiety at the 2 position 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

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

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 componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-KW

integral 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 – 3903901-acyl-sn-glycerol-3-phosphate acyltransferase 2
PRO_0000208180

Regions

Transmembrane2 – 2221 Potential
Transmembrane305 – 32521 Potential
Transmembrane333 – 35321 Potential
Motif91 – 966HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q9XFW4-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: F1446E1B30009C37

FASTA39043,771
        10         20         30         40         50         60 
MAMAAAVIVP LGILFFISGL VVNLLQAVCY VLVRPMSKNT YRKINRVVAE TLWLELVWIV 

        70         80         90        100        110        120 
DWWAGVKIQV FADDETFNRM GKEHALVVCN HRSDIDWLVG WILAQRSGCL GSALAVMKKS 

       130        140        150        160        170        180 
SKFLPVIGWS MWFSEYLFLE RNWAKDESTL QSGLQRLNDF PRPFWLALFV EGTRFTEAKL 

       190        200        210        220        230        240 
KAAQEYAASS ELPVPRNVLI PRTKGFVSAV SNMRSFVPAI YDMTVAIPKT SPPPTMLRLF 

       250        260        270        280        290        300 
KGQPSVVHVH IKCHSMKDLP EPEDEIAQWC RDQFVAKDAL LDKHIAADTF PGQKEQNIGR 

       310        320        330        340        350        360 
PIKSLAVVVS WACLLTLGAM KFLHWSNLFS SWKGIALSAF GLGIITLCMQ ILIRSSQSER 

       370        380        390 
STPAKVAPAK PKDNHQSGPS SQTEVEEKQK 

« Hide

References

[1]"A cDNA encoding a microsomal 1-acylglycerol-3-phosphate acyltransferase of Brassica napus L."
Graefin zu Muenster A., Wolter F.P., Frentzen M.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Silique.

Cross-references

Sequence databases

Z95637 mRNA. Translation: CAB09138.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.51. 393.

Family and domain databases

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

Entry information

Entry nameLPAT2_BRANA
AccessionPrimary (citable) accession number: Q9XFW4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1999
Last modified: October 13, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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