Q9HCL2 (GPAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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.5
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.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Polymorphism
Domain	Transit peptide Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway acyl-CoA metabolic process Inferred from electronic annotation. Source: Compara defense response to virus Inferred from electronic annotation. Source: Compara fatty acid homeostasis Inferred from electronic annotation. Source: Compara fatty acid metabolic process Inferred from electronic annotation. Source: Compara interleukin-2 secretion Inferred from electronic annotation. Source: Compara negative regulation of activation-induced cell death of T cells Inferred from electronic annotation. Source: Compara phosphatidic acid biosynthetic process Traceable author statement. Source: Reactome phospholipid homeostasis Inferred from electronic annotation. Source: Compara positive regulation of activated T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara regulation of cytokine secretion Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome triglyceride biosynthetic process Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial outer membrane Traceable author statement. Source: Reactome
Molecular_function	glycerol-3-phosphate O-acyltransferase activity Inferred from mutant phenotype Ref.5. Source: UniProtKB
Complete GO annotation...

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	Helical; Potential
	Topological domain	495 – 574	80	Cytoplasmic Potential
	Transmembrane	575 – 593	19	Helical; Potential
	Topological domain	594 – 828	235	Mitochondrial intermembrane Potential
	Motif	230 – 235	6	HXXXXD motif
Amino acid modifications
	Modified residue	695	1	Phosphoserine Ref.6
Natural variations
	Natural variant	4	1	S → Y. Corresponds to variant rs11549703 [ dbSNP | Ensembl ].		VAR_050585
	Natural variant	43	1	I → V. Corresponds to variant rs2792751 [ dbSNP | Ensembl ].		VAR_050586
	Natural variant	131	1	E → G. Corresponds to variant rs10787428 [ dbSNP | Ensembl ].		VAR_050587
	Natural variant	386	1	I → T. Corresponds to variant rs35019520 [ dbSNP | Ensembl ].		VAR_050588
Experimental info
	Sequence conflict	204	1	I → F in CAD89932. Ref.1
	Sequence conflict	652	1	Q → R in CAD89932. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9HCL2 [UniParc]. Last modified February 15, 2005. Version 3. Checksum: 7AADD21BC8684693	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spinal cord.
[2]	"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. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-828. Tissue: Brain.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[5]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL833093 mRNA. Translation: CAD89932.1. AL391986 Genomic DNA. Translation: CAH73716.1. AB046780 mRNA. Translation: BAB13386.1.
IPI	IPI00844249.
RefSeq	NP_001231878.1. NM_001244949.1. NP_065969.3. NM_020918.5.
UniGene	Hs.42586.
3D structure databases
ProteinModelPortal	Q9HCL2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000265276.
PTM databases
PhosphoSite	Q9HCL2.
Polymorphism databases
DMDM	59803040.
Proteomic databases
PaxDb	Q9HCL2.
PRIDE	Q9HCL2.
Protocols and materials databases
DNASU	57678.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000348367; ENSP00000265276; ENSG00000119927. ENST00000423155; ENSP00000409242; ENSG00000119927.
GeneID	57678.
KEGG	hsa:57678.
UCSC	uc001kzp.3. human.
Organism-specific databases
CTD	57678.
GeneCards	GC10M113899.
HGNC	HGNC:24865. GPAM.
HPA	HPA046339.
MIM	602395. gene.
neXtProt	NX_Q9HCL2.
PharmGKB	PA134983031.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2937.
HOGENOM	HOG000112780.
HOVERGEN	HBG000102.
InParanoid	Q9HCL2.
KO	K00629.
OMA	CVRVDFA.
OrthoDB	EOG4BZN1X.
Enzyme and pathway databases
BioCyc	MetaCyc:57678-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00557; UER00612.
Gene expression databases
ArrayExpress	Q9HCL2.
Bgee	Q9HCL2.
CleanEx	HS_GPAM.
Genevestigator	Q9HCL2.
GermOnline	ENSG00000119927. Homo sapiens.
Family and domain databases
InterPro	IPR022284. G3P_O-AcylTrfase. IPR002123. Plipid/glycerol_acylTrfase. [Graphical view]
PANTHER	PTHR12563. PTHR12563. 1 hit.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
PIRSF	PIRSF000437. GPAT_DHAPAT. 1 hit.
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GPAM. human.
GenomeRNAi	57678.
NextBio	64486.
SOURCE	Search...

Entry information

Entry name

GPAT1_HUMAN

Accession

Primary (citable) accession number: Q9HCL2
Secondary accession number(s): Q5VW51, Q86TA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	February 15, 2005
Last modified:	April 3, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.