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Q61586

- GPAT1_MOUSE

UniProt

Q61586 - GPAT1_MOUSE

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Protein
Glycerol-3-phosphate acyltransferase 1, mitochondrial
Gene
Gpam, Gpat1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. glycerol-3-phosphate O-acyltransferase activity Source: MGI

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  2. acyl-CoA metabolic process Source: MGI
  3. defense response to virus Source: MGI
  4. fatty acid homeostasis Source: MGI
  5. fatty acid metabolic process Source: MGI
  6. glycerophospholipid metabolic process Source: MGI
  7. interleukin-2 secretion Source: MGI
  8. negative regulation of activation-induced cell death of T cells Source: MGI
  9. phospholipid homeostasis Source: MGI
  10. positive regulation of activated T cell proliferation Source: MGI
  11. positive regulation of multicellular organism growth Source: MGI
  12. regulation of cytokine secretion Source: MGI
  13. response to glucose Source: MGI
  14. triglyceride biosynthetic process Source: Ensembl
  15. triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.15. 3474.
ReactomeiREACT_188640. Synthesis of PA.
REACT_198969. Activation of gene expression by SREBF (SREBP).
SABIO-RKQ61586.
UniPathwayiUPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 1, mitochondrial (EC:2.3.1.15)
Short name:
GPAT-1
Alternative name(s):
P90
Gene namesi
Name:Gpam
Synonyms:Gpat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:109162. Gpam.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini? – 471Mitochondrial intermembrane Reviewed prediction
Transmembranei472 – 49423Helical; Reviewed prediction
Add
BLAST
Topological domaini495 – 57480Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei575 – 59319Helical; Reviewed prediction
Add
BLAST
Topological domaini594 – 827234Mitochondrial intermembrane Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. mitochondrion Source: MGI
  5. plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 827Glycerol-3-phosphate acyltransferase 1, mitochondrialPRO_0000024691
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei380 – 3801Phosphoserine By similarity
Modified residuei687 – 6871Phosphoserine1 Publication
Modified residuei694 – 6941Phosphoserine2 Publications
Modified residuei779 – 7791N6-acetyllysine1 Publication
Modified residuei783 – 7831N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ61586.
PaxDbiQ61586.
PRIDEiQ61586.

PTM databases

PhosphoSiteiQ61586.

Expressioni

Tissue specificityi

Highest levels in liver, intermediate levels in muscle and kidney, and lowest levels in lung and brain.

Gene expression databases

ArrayExpressiQ61586.
BgeeiQ61586.
GenevestigatoriQ61586.

Interactioni

Protein-protein interaction databases

BioGridi200011. 1 interaction.
IntActiQ61586. 1 interaction.
MINTiMINT-4119610.

Structurei

3D structure databases

ProteinModelPortaliQ61586.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi230 – 2356HXXXXD motif

Domaini

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 similaritiesi

Belongs to the GPAT/DAPAT family.

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2937.
GeneTreeiENSGT00520000055570.
HOVERGENiHBG000102.
InParanoidiQ8VCT2.
KOiK00629.
OMAiKKNESLW.
OrthoDBiEOG74R1PZ.
TreeFamiTF313360.

Family and domain databases

InterProiIPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PANTHERiPTHR12563. PTHR12563. 1 hit.
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFiPIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61586-1 [UniParc]FASTAAdd to Basket

« Hide

MEESSVTVGT IDVSYLPSSS EYSLGRCKHT SEDWVDCGFK PTFFRSATLK    50
WKESLMSRKR PFVGRCCYSC TPQSWERFFN PSIPSLGLRN VIYINETHTR 100
HRGWLARRLS YILFVQERDV HKGMFATSVT ENVLSSSRVQ EAIAEVAAEL 150
NPDGSAQQQS KAIQKVKRKA RKILQEMVAT VSPGMIRLTG WVLLKLFNSF 200
FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT FILFCHNIKA 250
PYIASGNNLN IPVFSTLIHK LGGFFIRRRL DETPDGRKDI LYRALLHGHV 300
VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS SNTIPDILVI 350
PVGISYDRII EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGYVRVDF 400
AQPFSLKEYL EGQSQKPVSA PLSLEQALLP AILPSRPNDV ADEHQDLSSN 450
ESRNPADEAF RRRLIANLAE HILFTASKSC AIMSTHIVAC LLLYRHRQGI 500
HLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL GNCVTITHTS 550
RKDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSI YAVLNKRCSG 600
GSAGGLGNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF 650
IQYGILTVAE QDDQEDVSPG LAEQQWDKKL PELNWRSDEE DEDSDFGEEQ 700
RDCYLKVSQS KEHQQFITFL QRLLGPLLEA YSSAAIFVHN FSGPVPESEY 750
LQKLHRYLIT RTERNVAVYA ESATYCLVKN AVKMFKDIGV FKETKQKRVS 800
VLELSSTFLP QCNRQKLLEY ILSFVVL 827
Length:827
Mass (Da):93,705
Last modified:July 27, 2011 - v2
Checksum:i4C177AA15374EE9B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti331 – 3311L → V in AAA37647. 1 Publication
Sequence conflicti337 – 3371D → N in AAA37647. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS29906.1.
PIRiA41672.
RefSeqiNP_032175.2. NM_008149.3.
XP_006526755.1. XM_006526692.1.
XP_006526756.1. XM_006526693.1.
XP_006526757.1. XM_006526694.1.
UniGeneiMm.210196.

Genome annotation databases

EnsembliENSMUST00000061856; ENSMUSP00000057635; ENSMUSG00000024978.
GeneIDi14732.
KEGGimmu:14732.
UCSCiuc008hxk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS29906.1.
PIRi A41672.
RefSeqi NP_032175.2. NM_008149.3.
XP_006526755.1. XM_006526692.1.
XP_006526756.1. XM_006526693.1.
XP_006526757.1. XM_006526694.1.
UniGenei Mm.210196.

3D structure databases

ProteinModelPortali Q61586.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200011. 1 interaction.
IntActi Q61586. 1 interaction.
MINTi MINT-4119610.

PTM databases

PhosphoSitei Q61586.

Proteomic databases

MaxQBi Q61586.
PaxDbi Q61586.
PRIDEi Q61586.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000061856 ; ENSMUSP00000057635 ; ENSMUSG00000024978 .
GeneIDi 14732.
KEGGi mmu:14732.
UCSCi uc008hxk.1. mouse.

Organism-specific databases

CTDi 57678.
MGIi MGI:109162. Gpam.

Phylogenomic databases

eggNOGi COG2937.
GeneTreei ENSGT00520000055570.
HOVERGENi HBG000102.
InParanoidi Q8VCT2.
KOi K00629.
OMAi KKNESLW.
OrthoDBi EOG74R1PZ.
TreeFami TF313360.

Enzyme and pathway databases

UniPathwayi UPA00557 ; UER00612 .
BRENDAi 2.3.1.15. 3474.
Reactomei REACT_188640. Synthesis of PA.
REACT_198969. Activation of gene expression by SREBF (SREBP).
SABIO-RK Q61586.

Miscellaneous databases

NextBioi 286773.
PROi Q61586.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61586.
Bgeei Q61586.
Genevestigatori Q61586.

Family and domain databases

InterProi IPR022284. GPAT/DHAPAT.
IPR028354. GPAT_PlsB.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
PANTHERi PTHR12563. PTHR12563. 1 hit.
Pfami PF01553. Acyltransferase. 1 hit.
[Graphical view ]
PIRSFi PIRSF500064. GPAT. 1 hit.
PIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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] [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. 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.

Entry informationi

Entry nameiGPAT1_MOUSE
AccessioniPrimary (citable) accession number: Q61586
Secondary accession number(s): Q8VCT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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