Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P97564 (GPAT1_RAT)

Last modified February 9, 2010. Version 76. 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:
    Glycerol-3-phosphate acyltransferase 1, mitochondrial
      Short name=GPAT-1
    EC=2.3.1.15
Gene names
Name: Gpam
Synonyms: Gpat1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis By similarity.

Catalytic activity

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

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.

Subcellular location

Mitochondrion outer membrane; Multi-pass membrane protein Ref.2.

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 GPAT/DAPAT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 828Glycerol-3-phosphate acyltransferase 1, mitochondrialPRO_0000024692

Regions

Topological domain? – 471Mitochondrial intermembrane Potential
Transmembrane472 – 49423 Potential
Topological domain495 – 57480Cytoplasmic Potential
Transmembrane575 – 59319 Potential
Topological domain594 – 828235Mitochondrial intermembrane Potential
Motif230 – 2356HXXXXD motif

Amino acid modifications

Modified residue1111Phosphotyrosine By similarity
Modified residue6951Phosphoserine By similarity

Experimental info

Sequence conflict371C → F Ref.2
Sequence conflict851S → P in AAB39470. Ref.2
Sequence conflict3001I → V in AAB39470. Ref.2
Sequence conflict3311L → V in AAB39470. Ref.2
Sequence conflict472 – 4743ILF → NLL in AAB39470. Ref.2
Sequence conflict4971R → W in AAB39470. Ref.2
Sequence conflict602 – 6065SAGGL → LPEP in AAB39470. Ref.2
Sequence conflict6441Q → H in AAB39470. Ref.2
Sequence conflict7441G → A in AAB39470. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P97564-1 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: ACA4A087E7DEB12C

FASTA82893,715
        10         20         30         40         50         60 
MEESSVTIGT IDVSYLPNSS EYSLGRCKHT NEDWVDCGFK PTFFRSATLK WKESLMSRKR 

        70         80         90        100        110        120 
PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YILFVQERDV 

       130        140        150        160        170        180 
HKGMFATSIT DNVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAIQKVKRKA RKILQEMVAT 

       190        200        210        220        230        240 
VSPGMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT 

       250        260        270        280        290        300 
FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHI 

       310        320        330        340        350        360 
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS SNTIPDILVI PVGISYDRII 

       370        380        390        400        410        420 
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGYVRVDF AQPFSLKEYL EGQSQKPVSA 

       430        440        450        460        470        480 
PLSLEQALLP AILPSRPDAA AAEHEDMSSN ESRNAADEAF RRRLIANLAE HILFTASKSC 

       490        500        510        520        530        540 
AIMSTHIVAC LLLYRHRQGI HLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL 

       550        560        570        580        590        600 
GNCVTITHTS RKDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSI YAVQNKRGSG 

       610        620        630        640        650        660 
GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCQETVGKF IQYGILTVAE 

       670        680        690        700        710        720 
QDDQEDVSPG LAEQQWNKKL PEPLNWRSDE EDEDSDFGEE QRDCYLKVSQ AKEHQQFITF 

       730        740        750        760        770        780 
LQRLLGPLLE AYSSAAIFVH TFRGPVPESE YLQKLHRYLL TRTERNVAVY AESATYCLVK 

       790        800        810        820 
NAVKMFKDIG VFKETKQKRA SVLELSTTFL PQGSRQKLLE YILSFVVL 

« Hide

References

[1]"Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and characterization of the cDNA and expressed protein."
Bhat B.G., Wang P., Kim J.-H., Black T.M., Lewin T.M., Fiedorek F.T. Jr., Coleman R.A.
Biochim. Biophys. Acta 1439:415-423(1999) [PubMed: 10446428] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
Tissue: Liver.
[2]"Identification of two transmembrane regions and a cytosolic domain of rat mitochondrial glycerophosphate acyltransferase."
Balija V.S., Chakraborty T.R., Nikonov A.V., Morimoto T., Haldar D.
J. Biol. Chem. 275:31668-31673(2000) [PubMed: 10924502] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TOPOLOGY.
Strain: Sprague-Dawley.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF021348 mRNA. Translation: AAB71605.1.
U36771 mRNA. Translation: AAB39470.2. Different initiation.
IPIIPI00205564.
RefSeqNP_058970.1.
UniGeneRn.44456

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP97564.

PTM databases

PhosphoSiteP97564.

Proteomic databases

PRIDEP97564.

Genome annotation databases

EnsemblENSRNOT00000047903; ENSRNOP00000050050; ENSRNOG00000015124; Rattus norvegicus. [Genome view]
GeneID29653.
KEGGrno:29653.
UCSCNM_017274. rat.

Organism-specific databases

CTD29653.
RGD61847. Gpam.

Phylogenomic databases

eggNOGroNOG06258.
HOVERGENP97564.
InParanoidP97564.

Enzyme and pathway databases

BRENDA2.3.1.15. 248.

Gene expression databases

ArrayExpressP97564.
GenevestigatorP97564.
GermOnlineENSRNOG00000015124. Rattus norvegicus.

Family and domain databases

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

Other Resources

NextBio609941.

Entry information

Entry nameGPAT1_RAT
AccessionPrimary (citable) accession number: P97564
Secondary accession number(s): O35349, P97565, P97566
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: February 9, 2010
This is version 76 of the entry and version 3 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