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Protein

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

Gene

Agpat4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.1 Publication

Catalytic activityi

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

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

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

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase delta (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 4
Short name:
1-AGP acyltransferase 4
Short name:
1-AGPAT 4
Lysophosphatidic acid acyltransferase delta
Short name:
LPAAT-delta
Gene namesi
Name:Agpat4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1915512. Agpat4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Transmembranei311 – 33121HelicalSequence analysisAdd
BLAST
Transmembranei338 – 35821HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3783781-acyl-sn-glycerol-3-phosphate acyltransferase deltaPRO_0000208198Add
BLAST

Proteomic databases

EPDiQ8K4X7.
MaxQBiQ8K4X7.
PaxDbiQ8K4X7.
PRIDEiQ8K4X7.

PTM databases

iPTMnetiQ8K4X7.
PhosphoSiteiQ8K4X7.

Expressioni

Tissue specificityi

Expressed at a high levels in the brain, at intermediate or low levels in skeletal muscles, gut, kidney, spleen and lung. Barely detectable in heart and liver.1 Publication

Gene expression databases

BgeeiQ8K4X7.
ExpressionAtlasiQ8K4X7. baseline and differential.
GenevisibleiQ8K4X7. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8K4X7. 1 interaction.
STRINGi10090.ENSMUSP00000024594.

Structurei

3D structure databases

ProteinModelPortaliQ8K4X7.
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.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000006110.
HOVERGENiHBG008205.
InParanoidiQ8K4X7.
KOiK13523.
OMAiCISSQMV.
PhylomeDBiQ8K4X7.
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.

Q8K4X7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLIGLLKSQ FLCHLVFCYV FIASGLIVNA IQLCTLVIWP INKQLFRKIN
60 70 80 90 100
ARLCYCVSSQ LVMLLEWWSG TECTIYTDPK ACPHYGKENA IVVLNHKFEI
110 120 130 140 150
DFLCGWSLAE RLGILGNSKV LAKKELAYVP IIGWMWYFVE MIFCTRKWEQ
160 170 180 190 200
DRQTVAKSLL HLRDYPEKYL FLIHCEGTRF TEKKHQISMQ VAQAKGLPSL
210 220 230 240 250
KHHLLPRTKG FAITVKCLRD VVPAVYDCTL NFRNNENPTL LGVLNGKKYH
260 270 280 290 300
ADCYVRRIPM EDIPEDEDKC SAWLHKLYQE KDAFQEEYYR TGVFPETPWV
310 320 330 340 350
PPRRPWSLVN WLFWASLLLY PFFQFLVSMV SSGSSVTLAS LVLIFCMASM
360 370
GVRWMIGVTE IDKGSAYGNI DNKRKQTD
Length:378
Mass (Da):43,810
Last modified:October 1, 2002 - v1
Checksum:i3D9EF15B6A5E49BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005139 mRNA. Translation: BAB23837.2.
AK166917 mRNA. Translation: BAE39115.1.
AF485269 Genomic DNA. Translation: AAM33375.1.
BC047281 mRNA. Translation: AAH47281.1.
CCDSiCCDS28389.1.
RefSeqiNP_080920.2. NM_026644.2.
XP_006523408.2. XM_006523345.2.
XP_006523409.2. XM_006523346.2.
UniGeneiMm.258300.

Genome annotation databases

EnsembliENSMUST00000024594; ENSMUSP00000024594; ENSMUSG00000023827.
GeneIDi68262.
KEGGimmu:68262.
UCSCiuc008akm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005139 mRNA. Translation: BAB23837.2.
AK166917 mRNA. Translation: BAE39115.1.
AF485269 Genomic DNA. Translation: AAM33375.1.
BC047281 mRNA. Translation: AAH47281.1.
CCDSiCCDS28389.1.
RefSeqiNP_080920.2. NM_026644.2.
XP_006523408.2. XM_006523345.2.
XP_006523409.2. XM_006523346.2.
UniGeneiMm.258300.

3D structure databases

ProteinModelPortaliQ8K4X7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K4X7. 1 interaction.
STRINGi10090.ENSMUSP00000024594.

PTM databases

iPTMnetiQ8K4X7.
PhosphoSiteiQ8K4X7.

Proteomic databases

EPDiQ8K4X7.
MaxQBiQ8K4X7.
PaxDbiQ8K4X7.
PRIDEiQ8K4X7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024594; ENSMUSP00000024594; ENSMUSG00000023827.
GeneIDi68262.
KEGGimmu:68262.
UCSCiuc008akm.1. mouse.

Organism-specific databases

CTDi56895.
MGIiMGI:1915512. Agpat4.

Phylogenomic databases

eggNOGiKOG1505. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000006110.
HOVERGENiHBG008205.
InParanoidiQ8K4X7.
KOiK13523.
OMAiCISSQMV.
PhylomeDBiQ8K4X7.
TreeFamiTF314065.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiAgpat4. mouse.
PROiQ8K4X7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K4X7.
ExpressionAtlasiQ8K4X7. baseline and differential.
GenevisibleiQ8K4X7. 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. "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: Cerebellum.
  2. "Genomic sequence analysis in the mouse T-complex region."
    Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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: Colon.
  4. "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: FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Testis.

Entry informationi

Entry nameiPLCD_MOUSE
AccessioniPrimary (citable) accession number: Q8K4X7
Secondary accession number(s): Q3TKN0, Q9DB84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 100 of the entry and version 1 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

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.