Q61586 (GPAT1_MOUSE) 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

Alternative name(s):
P90

Gene names

Name:	Gpam
Synonyms:	Gpat1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	827 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 By similarity.
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.
Tissue specificity	Highest levels in liver, intermediate levels in muscle and kidney, and lowest levels in lung and brain.
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	Phospholipid biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from mutant phenotype. Source: MGI defense response to virus Inferred from mutant phenotype. Source: MGI fatty acid homeostasis Inferred from mutant phenotype. Source: MGI fatty acid metabolic process Inferred from mutant phenotype. Source: MGI glycerophospholipid metabolic process Inferred from mutant phenotype. Source: MGI interleukin-2 secretion Inferred from mutant phenotype. Source: MGI negative regulation of activation-induced cell death of T cells Inferred from mutant phenotype. Source: MGI phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW phospholipid homeostasis Inferred from mutant phenotype. Source: MGI positive regulation of activated T cell proliferation Inferred from mutant phenotype. Source: MGI positive regulation of multicellular organism growth Inferred from mutant phenotype. Source: MGI regulation of cytokine secretion Inferred from mutant phenotype. Source: MGI response to glucose stimulus Inferred from mutant phenotype. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycerol-3-phosphate O-acyltransferase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 827		Glycerol-3-phosphate acyltransferase 1, mitochondrial		PRO_0000024691
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 – 827	234	Mitochondrial intermembrane Potential
	Motif	230 – 235	6	HXXXXD motif
Amino acid modifications
	Modified residue	111	1	Phosphotyrosine By similarity
	Modified residue	694	1	Phosphoserine Ref.6 Ref.7
Experimental info
	Sequence conflict	331	1	L → V in AAA37647. Ref.1
	Sequence conflict	337	1	D → N in AAA37647. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q61586 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 4C177AA15374EE9B	FASTA	827	93,705
	10 20 30 40 50 60 MEESSVTVGT IDVSYLPSSS EYSLGRCKHT SEDWVDCGFK PTFFRSATLK WKESLMSRKR 70 80 90 100 110 120 PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YILFVQERDV 130 140 150 160 170 180 HKGMFATSVT ENVLSSSRVQ EAIAEVAAEL NPDGSAQQQS KAIQKVKRKA RKILQEMVAT 190 200 210 220 230 240 VSPGMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT 250 260 270 280 290 300 FILFCHNIKA PYIASGNNLN IPVFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHV 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 AILPSRPNDV ADEHQDLSSN ESRNPADEAF 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 YAVLNKRCSG 610 620 630 640 650 660 GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE 670 680 690 700 710 720 QDDQEDVSPG LAEQQWDKKL PELNWRSDEE DEDSDFGEEQ RDCYLKVSQS KEHQQFITFL 730 740 750 760 770 780 QRLLGPLLEA YSSAAIFVHN FSGPVPESEY LQKLHRYLIT RTERNVAVYA ESATYCLVKN 790 800 810 820 AVKMFKDIGV FKETKQKRVS VLELSSTFLP QCNRQKLLEY ILSFVVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional regulation of p90 with sequence homology to Escherichia coli glycerol-3-phosphate acyltransferase." Shin D.-H., Paulauskis J.D., Moustaid N., Sul H.S. J. Biol. Chem. 266:23834-23839(1991) [PubMed: 1721057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Positional cloning of Sorcs1, a type 2 diabetes quantitative trait locus." Clee S.M., Yandell B.S., Schueler K.M., Rabaglia M.E., Richards O.C., Raines S.M., Kabara E.A., Klass D.M., Mui E.T.-K., Stapleton D.S., Gray-Keller M.P., Young M.B., Stoehr J.P., Lan H., Boronenkov I., Raess P.W., Flowers M.T., Attie A.D. Nat. Genet. 38:688-693(2006) [PubMed: 16682971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BTBR T+ tf/J.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M77003 mRNA. Translation: AAA37647.1. DQ479922 Genomic DNA. Translation: ABF48501.1. AK137067 mRNA. Translation: BAE23226.1. CH466585 Genomic DNA. Translation: EDL01718.1. CH466585 Genomic DNA. Translation: EDL01719.1. BC019201 mRNA. Translation: AAH19201.1.
IPI	IPI00344626.
PIR	A41672.
RefSeq	NP_032175.2. NM_008149.3.
UniGene	Mm.210196.
3D structure databases
ProteinModelPortal	Q61586.
ModBase	Search...
Protein-protein interaction databases
STRING	Q61586.
PTM databases
PhosphoSite	Q61586.
Proteomic databases
PRIDE	Q61586.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000061856; ENSMUSP00000057635; ENSMUSG00000024978. ENSMUST00000086868; ENSMUSP00000084081; ENSMUSG00000024978.
GeneID	14732.
KEGG	mmu:14732.
Organism-specific databases
CTD	57678.
MGI	MGI:109162. Gpam.
Phylogenomic databases
eggNOG	roNOG06258.
InParanoid	Q61586.
OrthoDB	EOG4BZN1X.
Enzyme and pathway databases
BRENDA	2.3.1.15. 3474.
Gene expression databases
ArrayExpress	Q61586.
Bgee	Q61586.
Genevestigator	Q61586.
GermOnline	ENSMUSG00000024978. Mus musculus.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR022284. G3P_O-AcylTrfase. [Graphical view]
KO	K00629.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
PIRSF	PIRSF000437. GPAT_DHAPAT. 1 hit.
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GPAT1_MOUSE

Accession

Primary (citable) accession number: Q61586
Secondary accession number(s): Q8VCT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program