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Q61586 (GPAT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length827 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.

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 processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransit peptide
Transmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCDP-diacylglycerol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

acyl-CoA metabolic process

Inferred from mutant phenotype PubMed 15878874. Source: MGI

defense response to virus

Inferred from mutant phenotype PubMed 19193813. Source: MGI

fatty acid homeostasis

Inferred from mutant phenotype PubMed 18522808. Source: MGI

fatty acid metabolic process

Inferred from mutant phenotype PubMed 12417724. Source: MGI

glycerophospholipid metabolic process

Inferred from mutant phenotype PubMed 18971390. Source: MGI

interleukin-2 secretion

Inferred from mutant phenotype PubMed 18971390. Source: MGI

negative regulation of activation-induced cell death of T cells

Inferred from mutant phenotype PubMed 18971390. Source: MGI

phospholipid homeostasis

Inferred from mutant phenotype PubMed 18522808. Source: MGI

positive regulation of activated T cell proliferation

Inferred from mutant phenotype PubMed 18971390. Source: MGI

positive regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 12417724. Source: MGI

regulation of cytokine secretion

Inferred from mutant phenotype PubMed 18971390. Source: MGI

response to glucose

Inferred from mutant phenotype PubMed 15878874PubMed 16054099. Source: MGI

triglyceride biosynthetic process

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from mutant phenotype PubMed 15878874PubMed 16935266PubMed 18522808. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 12417724PubMed 14651853PubMed 18614015. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionglycerol-3-phosphate O-acyltransferase activity

Inferred from direct assay PubMed 12417724PubMed 15152008. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 827Glycerol-3-phosphate acyltransferase 1, mitochondrialPRO_0000024691

Regions

Topological domain? – 471Mitochondrial intermembrane Potential
Transmembrane472 – 49423Helical; Potential
Topological domain495 – 57480Cytoplasmic Potential
Transmembrane575 – 59319Helical; Potential
Topological domain594 – 827234Mitochondrial intermembrane Potential
Motif230 – 2356HXXXXD motif

Amino acid modifications

Modified residue3801Phosphoserine By similarity
Modified residue6871Phosphoserine Ref.6
Modified residue6941Phosphoserine Ref.6 Ref.7
Modified residue7791N6-acetyllysine Ref.8
Modified residue7831N6-acetyllysine Ref.8

Experimental info

Sequence conflict3311L → V in AAA37647. Ref.1
Sequence conflict3371D → N in AAA37647. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61586 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4C177AA15374EE9B

FASTA82793,705
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687 AND SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-779 AND LYS-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS29906.1.
PIRA41672.
RefSeqNP_032175.2. NM_008149.3.
XP_006526755.1. XM_006526692.1.
XP_006526756.1. XM_006526693.1.
XP_006526757.1. XM_006526694.1.
UniGeneMm.210196.

3D structure databases

ProteinModelPortalQ61586.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200011. 1 interaction.
IntActQ61586. 1 interaction.
MINTMINT-4119610.

PTM databases

PhosphoSiteQ61586.

Proteomic databases

MaxQBQ61586.
PaxDbQ61586.
PRIDEQ61586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061856; ENSMUSP00000057635; ENSMUSG00000024978.
GeneID14732.
KEGGmmu:14732.
UCSCuc008hxk.1. mouse.

Organism-specific databases

CTD57678.
MGIMGI:109162. Gpam.

Phylogenomic databases

eggNOGCOG2937.
GeneTreeENSGT00520000055570.
HOVERGENHBG000102.
InParanoidQ8VCT2.
KOK00629.
OMAKKNESLW.
OrthoDBEOG74R1PZ.
TreeFamTF313360.

Enzyme and pathway databases

BRENDA2.3.1.15. 3474.
SABIO-RKQ61586.
UniPathwayUPA00557; UER00612.

Gene expression databases

ArrayExpressQ61586.
BgeeQ61586.
GenevestigatorQ61586.

Family and domain databases

InterProIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERPTHR12563. PTHR12563. 1 hit.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286773.
PROQ61586.
SOURCESearch...

Entry information

Entry nameGPAT1_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot