Glycerol-3-phosphate acyltransferase 1, mitochondrial precursor

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase 1, mitochondrial
      Short name=GPAT-1
    EC=2.3.1.15

Gene names

Name:	GPAM
Synonyms:	GPAT1, KIAA1560

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	828 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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. Ref.4
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
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 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 GPAT/DAPAT family.

Hide | Top

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW triglyceride biosynthetic process Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	glycerol-3-phosphate O-acyltransferase activity Ref.4 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 828

Glycerol-3-phosphate acyltransferase 1, mitochondrial

PRO_0000024690

Regions

Topological domain

? – 471

Mitochondrial intermembrane Potential

Transmembrane

472 – 494

23

Potential

Topological domain

495 – 574

80

Cytoplasmic Potential

Transmembrane

575 – 593

19

Potential

Topological domain

594 – 828

235

Mitochondrial intermembrane Potential

Motif

230 – 235

6

HXXXXD motif

Amino acid modifications

Modified residue

111

1

Phosphotyrosine Ref.3

Modified residue

695

1

Phosphoserine Ref.5

Natural variations

Natural variant

4

1

S → Y: dbSNP rs11549703.

VAR_050585

Natural variant

43

1

I → V: dbSNP rs2792751.

VAR_050586

Natural variant

131

1

E → G: dbSNP rs10787428.

VAR_050587

Natural variant

386

1

I → T: dbSNP rs35019520.

VAR_050588

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q9HCL2-1 [UniParc].

Last modified February 15, 2005. Version 3.
Checksum: 7AADD21BC8684693
Show »

FASTA

828

93,795

        10         20         30         40         50         60 
MDESALTLGT IDVSYLPHSS EYSVGRCKHT SEEWGECGFR PTIFRSATLK WKESLMSRKR 

        70         80         90        100        110        120 
PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV 

       130        140        150        160        170        180 
HKGMFATNVT ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KRILQEMVAT 

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

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

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

       370        380        390        400        410        420 
EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA 

       430        440        450        460        470        480 
LLSLEQALLP AILPSRPSDA ADEGRDTSIN ESRNATDESL RRRLIANLAE HILFTASKSC 

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

       550        560        570        580        590        600 
GNCVTITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG 

       610        620        630        640        650        660 
GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE 

       670        680        690        700        710        720 
HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE QRDCYLKVSQ SKEHQQFITF 

       730        740        750        760        770        780 
LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE YLQKLHKYLI TRTERNVAVY AESATYCLVK 

       790        800        810        820 
NAVKMFKDIG VFKETKQKRV SVLELSSTFL PQCNRQKLLE YILSFVVL

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O. DNA Res. 7:273-281(2000) [PubMed: 10997877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-828. Tissue: Brain.
[3]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-111, MASS SPECTROMETRY. Tissue: Epithelium.
[4]	"AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase." Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E., Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E., Konrad R.J., Beigneux A.P., Young S.G., Cao G. J. Biol. Chem. 283:10048-10057(2008) [PubMed: 18238778] [Abstract] Cited for: FUNCTION.
[5]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL391986 Genomic DNA. Translation: CAH73716.1. AB046780 mRNA. Translation: BAB13386.1.
IPI	IPI00844249.
RefSeq	NP_065969.3.
UniGene	Hs.42586
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9HCL2.
PTM databases
PhosphoSite	Q9HCL2.
Proteomic databases
PRIDE	Q9HCL2.
Genome annotation databases
Ensembl	ENST00000348367; ENSP00000265276; ENSG00000119927; Homo sapiens. [Genome view] ENST00000423155; ENSP00000409242; ENSG00000119927; Homo sapiens. [Genome view]
GeneID	57678.
KEGG	hsa:57678.
NMPDR	fig\|9606.3.peg.4647.
UCSC	uc001kzp.2. human.
Organism-specific databases
CTD	57678.
GeneCards	GC10M113899.
H-InvDB	HIX0009205.
HGNC	HGNC:24865. GPAM.
MIM	602395. gene.
PharmGKB	PA134983031.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12513.
HOGENOM	HBG443870.
HOVERGEN	Q9HCL2.
InParanoid	Q9HCL2.
OMA	DCYLKVS.
OrthoDB	EOG9JWZ0T.
PhylomeDB	Q9HCL2.
Enzyme and pathway databases
BioCyc	MetaCyc:57678-MONOMER.
BRENDA	2.3.1.15. 247.
Reactome	REACT_602. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q9HCL2.
Bgee	Q9HCL2.
CleanEx	HS_GPAM.
Genevestigator	Q9HCL2.
GermOnline	ENSG00000119927. Homo sapiens.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	64486.
SOURCE	Search...

Hide | Top

Entry information

Entry name

GPAT1_HUMAN

Accession

Primary (citable) accession number: Q9HCL2
Secondary accession number(s): Q5VW51

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	February 15, 2005
Last modified:	February 9, 2010
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Hide | Top