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Protein

1-acyl-sn-glycerol-3-phosphate acyltransferase gamma

Gene

Agpat3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:15367102). Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor. Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (By similarity). Has a preference for arachidonoyl-CoA as a donor (PubMed:19114731). Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (PubMed:19114731).By similarity2 Publications

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Enzyme regulationi

In males, activity increases in an age-dependent fashion, maybe derived from the induction by sex-hormones.1 Publication

Kineticsi

  1. KM=15.9 µM for arachidonoyl-CoA1 Publication
  2. KM=26.3 µM for palmitoyl-LPA1 Publication
  1. Vmax=50.4 nmol/min/mg enzyme toward arachidonoyl-CoA1 Publication
  2. Vmax=21.8 nmol/min/mg enzyme toward palmitoyl-LPA1 Publication

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 1, mitochondrial (Gpam), Glycerol-3-phosphate acyltransferase 4 (Gpat4), Glycerol-3-phosphate acyltransferase 3 (Gpat3), Glycerol-3-phosphate acyltransferase 2, mitochondrial (Gpat2)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (Agpat3), 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (Agpat2), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (Agpat1), Lysocardiolipin acyltransferase 1 (Lclat1), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (Agpat5), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (Agpat4)
  3. Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 2 (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 1 (Cds1)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.51. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.
R-MMU-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00557; UER00613.

Chemistry

SwissLipidsiSLP:000000097.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 3
Short name:
1-AGP acyltransferase 3
Short name:
1-AGPAT 3
Lysophosphatidic acid acyltransferase gamma
Short name:
LPAAT-gamma
Gene namesi
Name:Agpat3Imported
Synonyms:Lpaat31 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1336186. Agpat3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 124124CytoplasmicSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Topological domaini146 – 316171LumenalSequence analysisAdd
BLAST
Transmembranei317 – 33923HelicalSequence analysisAdd
BLAST
Topological domaini340 – 37637CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi96 – 961H → A: Loss of LPA acyltransferase and LPI acyltransferase activities. 1 Publication
Mutagenesisi101 – 1011D → A: Loss of LPA acyltransferase and LPI acyltransferase activities. 1 Publication
Mutagenesisi176 – 1761E → A: Loss of LPA acyltransferase and LPI acyltransferase activities. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3763761-acyl-sn-glycerol-3-phosphate acyltransferase gammaPRO_0000208195Add
BLAST

Proteomic databases

EPDiQ9D517.
MaxQBiQ9D517.
PaxDbiQ9D517.
PRIDEiQ9D517.

PTM databases

iPTMnetiQ9D517.
PhosphoSiteiQ9D517.

Expressioni

Tissue specificityi

Widely expressed. Mainly expressed in testis, kidney and liver (at protein level).1 Publication

Inductioni

Up-regulated in the heart by clofibrate, a PPAR-alpha agonist.1 Publication

Gene expression databases

BgeeiQ9D517.
CleanExiMM_AGPAT3.
ExpressionAtlasiQ9D517. baseline and differential.
GenevisibleiQ9D517. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001240.

Structurei

3D structure databases

ProteinModelPortaliQ9D517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1016HXXXXD 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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000006110.
HOVERGENiHBG008205.
InParanoidiQ9D517.
KOiK13523.
OMAiMEVAESK.
OrthoDBiEOG7H7928.
PhylomeDBiQ9D517.
TreeFamiTF314065.

Family and domain databases

InterProiIPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLAYLKTQ FVVHLLIGFV FVVSGLIINF TQLCTLALWP ISKHLYRRIN
60 70 80 90 100
CRLAYSLWSQ LVMLLEWWSC TECTLFTDQA TVDHFGKEHV VVILNHNFEI
110 120 130 140 150
DFLCGWTMCE RFGVLGSSKV LAKRELLCVP LIGWTWYFLE IVFCKRKWEE
160 170 180 190 200
DRDTVIEGLR RLADYPEYMW FLLYCEGTRF TETKHRISME VAASKGLPPL
210 220 230 240 250
KYHLLPRTKG FTTAVQCLRG TVAAIYDVTL NFRGNKNPSL LGILYGKKYE
260 270 280 290 300
ADMCVRRFPL EDIPADETSA AQWLHKLYQE KDALQEMYKQ KGVFPGEQFK
310 320 330 340 350
PARRPWTLLN FLCWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF
360 370
GVRRLIGVTE IEKGSSYGNQ ELKKKE
Length:376
Mass (Da):43,296
Last modified:March 1, 2003 - v2
Checksum:i6F8C8970404B2EC1
GO

Sequence cautioni

The sequence BAC27043.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211F → V in AAH52382 (PubMed:15489334).Curated
Sequence conflicti21 – 211F → V in AAH58519 (PubMed:15489334).Curated
Sequence conflicti249 – 2491Y → N in BAC27043 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY167588 mRNA. Translation: AAN75574.1.
AB377215 mRNA. Translation: BAH59614.1.
AK015906 mRNA. Translation: BAB30025.2.
AK030607 mRNA. Translation: BAC27043.1. Different initiation.
AK075715 mRNA. Translation: BAC35905.1.
AK076414 mRNA. Translation: BAC36329.1.
CH466553 Genomic DNA. Translation: EDL31738.1.
CH466553 Genomic DNA. Translation: EDL31739.1.
CH466553 Genomic DNA. Translation: EDL31740.1.
CH466553 Genomic DNA. Translation: EDL31742.1.
BC052382 mRNA. Translation: AAH52382.1.
BC058519 mRNA. Translation: AAH58519.1.
CCDSiCCDS23963.1.
RefSeqiNP_443747.2. NM_053014.3.
XP_006513779.1. XM_006513716.2.
XP_006513780.1. XM_006513717.2.
XP_006513781.1. XM_006513718.1.
XP_006513782.1. XM_006513719.2.
XP_006513783.1. XM_006513720.1.
XP_006513784.1. XM_006513721.1.
XP_006513785.1. XM_006513722.2.
XP_006513786.1. XM_006513723.2.
UniGeneiMm.141230.

Genome annotation databases

EnsembliENSMUST00000001240; ENSMUSP00000001240; ENSMUSG00000001211.
ENSMUST00000105387; ENSMUSP00000101026; ENSMUSG00000001211.
ENSMUST00000105388; ENSMUSP00000101027; ENSMUSG00000001211.
ENSMUST00000105389; ENSMUSP00000101028; ENSMUSG00000001211.
ENSMUST00000105390; ENSMUSP00000101029; ENSMUSG00000001211.
ENSMUST00000166360; ENSMUSP00000132954; ENSMUSG00000001211.
GeneIDi28169.
KEGGimmu:28169.
UCSCiuc007fxo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY167588 mRNA. Translation: AAN75574.1.
AB377215 mRNA. Translation: BAH59614.1.
AK015906 mRNA. Translation: BAB30025.2.
AK030607 mRNA. Translation: BAC27043.1. Different initiation.
AK075715 mRNA. Translation: BAC35905.1.
AK076414 mRNA. Translation: BAC36329.1.
CH466553 Genomic DNA. Translation: EDL31738.1.
CH466553 Genomic DNA. Translation: EDL31739.1.
CH466553 Genomic DNA. Translation: EDL31740.1.
CH466553 Genomic DNA. Translation: EDL31742.1.
BC052382 mRNA. Translation: AAH52382.1.
BC058519 mRNA. Translation: AAH58519.1.
CCDSiCCDS23963.1.
RefSeqiNP_443747.2. NM_053014.3.
XP_006513779.1. XM_006513716.2.
XP_006513780.1. XM_006513717.2.
XP_006513781.1. XM_006513718.1.
XP_006513782.1. XM_006513719.2.
XP_006513783.1. XM_006513720.1.
XP_006513784.1. XM_006513721.1.
XP_006513785.1. XM_006513722.2.
XP_006513786.1. XM_006513723.2.
UniGeneiMm.141230.

3D structure databases

ProteinModelPortaliQ9D517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000001240.

Chemistry

SwissLipidsiSLP:000000097.

PTM databases

iPTMnetiQ9D517.
PhosphoSiteiQ9D517.

Proteomic databases

EPDiQ9D517.
MaxQBiQ9D517.
PaxDbiQ9D517.
PRIDEiQ9D517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001240; ENSMUSP00000001240; ENSMUSG00000001211.
ENSMUST00000105387; ENSMUSP00000101026; ENSMUSG00000001211.
ENSMUST00000105388; ENSMUSP00000101027; ENSMUSG00000001211.
ENSMUST00000105389; ENSMUSP00000101028; ENSMUSG00000001211.
ENSMUST00000105390; ENSMUSP00000101029; ENSMUSG00000001211.
ENSMUST00000166360; ENSMUSP00000132954; ENSMUSG00000001211.
GeneIDi28169.
KEGGimmu:28169.
UCSCiuc007fxo.1. mouse.

Organism-specific databases

CTDi56894.
MGIiMGI:1336186. Agpat3.

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000006110.
HOVERGENiHBG008205.
InParanoidiQ9D517.
KOiK13523.
OMAiMEVAESK.
OrthoDBiEOG7H7928.
PhylomeDBiQ9D517.
TreeFamiTF314065.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
BRENDAi2.3.1.51. 3474.
ReactomeiR-MMU-1483166. Synthesis of PA.
R-MMU-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiAgpat3. mouse.
NextBioi306746.
PROiQ9D517.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D517.
CleanExiMM_AGPAT3.
ExpressionAtlasiQ9D517. baseline and differential.
GenevisibleiQ9D517. MM.

Family and domain databases

InterProiIPR032098. Acyltransf_C.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF16076. Acyltransf_C. 1 hit.
PF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart."
    Lu B., Jiang Y.J., Zhou Y., Xu F.Y., Hatch G.M., Choy P.C.
    Biochem. J. 385:469-477(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    Strain: C57BL/6J.
  2. "Characterization of mouse lysophosphatidic acid acyltransferase 3: an enzyme with dual functions in the testis."
    Yuki K., Shindou H., Hishikawa D., Shimizu T.
    J. Lipid Res. 50:860-869(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-96; ASP-101 AND GLU-176, ENZYME REGULATION.
  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: Head, Liver, Pituitary and Testis.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-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: C57BL/6J.
    Tissue: Embryonic brain.
  6. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 237-248, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPLCC_MOUSE
AccessioniPrimary (citable) accession number: Q9D517
Secondary accession number(s): C4B4E7, Q7TT39, Q8BST2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2003
Last modified: March 16, 2016
This is version 107 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, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.