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Reviewed, UniProtKB/Swiss-Prot Q41745 (LPAT_MAIZE)

Last modified March 3, 2009. 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 PLS1
    EC=2.3.1.51
Alternative name(s):
    Phospholipid synthesis protein 1
Gene names
Name: PLS1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACCAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length374 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.

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.1

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

Subcellular location

Membrane; Multi-pass membrane protein Probable.

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-KW

   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 – 3743741-acyl-sn-glycerol-3-phosphate acyltransferase PLS1
PRO_0000208188

Regions

Transmembrane15 – 3723 Potential
Transmembrane48 – 6821 Potential
Transmembrane121 – 14121 Potential
Transmembrane305 – 32521 Potential
Transmembrane335 – 35521 Potential
Motif92 – 976HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q41745-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F1F5492CAFF24F93

FASTA37442,571
        10         20         30         40         50         60 
MAIPLVLVVL PLGLLFLLSG LIVNAIQAVL FVTIRPFSKS FYRRINRFLA ELLWLQLVWV 

        70         80         90        100        110        120 
VDWWAGVKVQ LHADEETYRS MGKEHALIIS NHRSDIDWLI GWILAQRSGC LGSTLAVMKK 

       130        140        150        160        170        180 
SSKFLPVIGW SMWFAEYLFL ERSWAKDEKT LKWGLQRLKD FPRPFWLALF VEGTRFTPAK 

       190        200        210        220        230        240 
LLAAQEYAAS QGLPAPRNVL IPRTKGFVSA VSIMRDFVPA IYDTTVIVPK DSPQPTMLRI 

       250        260        270        280        290        300 
LKGQSSVIHV RMKRHAMSEM PKSDEDVSKW CKDIFVAKDA LLDKHLATGT FDEEIRPIGR 

       310        320        330        340        350        360 
PVKSLLVTLF WSCLLLFGAI EFFKWTQLLS TWRGVAFTAA GMALVTGVMH VFIMFSQAER 

       370 
SSSARAARNR VKKE 

« Hide

References

[1]"Isolation and characterization of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of E.coli and encodes a protein which has similarities to other acyltransferases."
Brown A.P., Coleman J., Tommey A.M., Watson M.D., Slabas A.R.
Plant Mol. Biol. 26:211-223(1994) [PubMed: 7948871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY.
Strain: cv. Black Mexican Sweet.
Tissue: Endosperm.

Cross-references

Sequence databases

Z29518 mRNA. Translation: CAA82638.1.
PIRS52645.
RefSeqNP_001105919.1.
UniGeneZm.95920

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID732844.

Organism-specific databases

GrameneQ41745.
MaizeGDB98837.

Enzyme and pathway databases

BRENDA2.3.1.51. 289.

Family and domain databases

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

Entry information

Entry nameLPAT_MAIZE
AccessionPrimary (citable) accession number: Q41745
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1996
Last modified: March 3, 2009
This is version 47 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