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Protein

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

Gene

Agpat5

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

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable.1 Publication

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. acylglycerol metabolic process Source: MGI
  2. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  3. hematopoietic progenitor cell differentiation 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

ReactomeiREACT_188640. Synthesis of PA.
REACT_237947. Triglyceride Biosynthesis.
UniPathwayiUPA00557; UER00613.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (EC:2.3.1.51)
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 5
Short name:
1-AGP acyltransferase 5
Short name:
1-AGPAT 5
Lysophosphatidic acid acyltransferase epsilon
Short name:
LPAAT-epsilon
Gene namesi
Name:Agpat5
Synonyms:D8Ertd319e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1196345. Agpat5.

Subcellular locationi

Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Nucleus envelope By similarity. Mitochondrion By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei15 – 3521HelicalSequence AnalysisAdd
BLAST
Transmembranei345 – 36521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrion Source: MGI
  4. nuclear envelope Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3653651-acyl-sn-glycerol-3-phosphate acyltransferase epsilonPRO_0000208201Add
BLAST

Proteomic databases

MaxQBiQ9D1E8.
PaxDbiQ9D1E8.
PRIDEiQ9D1E8.

PTM databases

PhosphoSiteiQ9D1E8.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9D1E8.
ExpressionAtlasiQ9D1E8. baseline and differential.
GenevestigatoriQ9D1E8.

Interactioni

Protein-protein interaction databases

BioGridi206392. 1 interaction.
IntActiQ9D1E8. 1 interaction.
STRINGi10090.ENSMUSP00000117025.

Structurei

3D structure databases

ProteinModelPortaliQ9D1E8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi93 – 986HXXXXD 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

eggNOGiCOG0204.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000007801.
HOVERGENiHBG039632.
InParanoidiQ9D1E8.
OMAiWFPATIM.
OrthoDBiEOG7QK0C7.
PhylomeDBiQ9D1E8.
TreeFamiTF314346.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D1E8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLSLVLHTY SMRYLLPSVL LLGSAPTYLL AWTLWRVLSA LMPARLYQRV
60 70 80 90 100
DDRLYCVYQN MVLFFFENYT GVQILLYGDL PKNKENVIYL ANHQSTVDWI
110 120 130 140 150
VADMLAARQD ALGHVRYVLK DKLKWLPLYG FYFAQHGGIY VKRSAKFNDK
160 170 180 190 200
EMRSKLQSYV NAGTPMYLVI FPEGTRYNAT YTKLLSASQA FAAQRGLAVL
210 220 230 240 250
KHVLTPRIKA THVAFDSMKS HLDAIYDVTV VYEGNEKGSG KYSNPPSMTE
260 270 280 290 300
FLCKQCPKLH IHFDRIDRNE VPEEQEHMKK WLHERFEIKD RLLIEFYDSP
310 320 330 340 350
DPERRNKFPG KSVHSRLSVK KTLPSVLILG SLTAVMLMTE SGRKLYMGTW
360
LYGTLLGCLW FVIKA
Length:365
Mass (Da):42,202
Last modified:May 16, 2003 - v2
Checksum:iC13E14759610E19B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801L → W in AAN75571. 1 PublicationCurated
Sequence conflicti128 – 1281L → M in AAN75571. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY161042 mRNA. Translation: AAN75571.1.
AK003649 mRNA. Translation: BAB22915.2.
AK082137 mRNA. Translation: BAC38421.1.
AK089885 mRNA. Translation: BAC40983.1.
AK152709 mRNA. Translation: BAE31436.1.
AK152889 mRNA. Translation: BAE31572.1.
AK155378 mRNA. Translation: BAE33229.1.
BC031987 mRNA. Translation: AAH31987.2.
CCDSiCCDS22126.1.
RefSeqiNP_081068.1. NM_026792.3.
UniGeneiMm.24117.

Genome annotation databases

EnsembliENSMUST00000149565; ENSMUSP00000117025; ENSMUSG00000031467.
GeneIDi52123.
KEGGimmu:52123.
UCSCiuc009kzv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY161042 mRNA. Translation: AAN75571.1.
AK003649 mRNA. Translation: BAB22915.2.
AK082137 mRNA. Translation: BAC38421.1.
AK089885 mRNA. Translation: BAC40983.1.
AK152709 mRNA. Translation: BAE31436.1.
AK152889 mRNA. Translation: BAE31572.1.
AK155378 mRNA. Translation: BAE33229.1.
BC031987 mRNA. Translation: AAH31987.2.
CCDSiCCDS22126.1.
RefSeqiNP_081068.1. NM_026792.3.
UniGeneiMm.24117.

3D structure databases

ProteinModelPortaliQ9D1E8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206392. 1 interaction.
IntActiQ9D1E8. 1 interaction.
STRINGi10090.ENSMUSP00000117025.

PTM databases

PhosphoSiteiQ9D1E8.

Proteomic databases

MaxQBiQ9D1E8.
PaxDbiQ9D1E8.
PRIDEiQ9D1E8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000149565; ENSMUSP00000117025; ENSMUSG00000031467.
GeneIDi52123.
KEGGimmu:52123.
UCSCiuc009kzv.1. mouse.

Organism-specific databases

CTDi55326.
MGIiMGI:1196345. Agpat5.

Phylogenomic databases

eggNOGiCOG0204.
GeneTreeiENSGT00530000062943.
HOGENOMiHOG000007801.
HOVERGENiHBG039632.
InParanoidiQ9D1E8.
OMAiWFPATIM.
OrthoDBiEOG7QK0C7.
PhylomeDBiQ9D1E8.
TreeFamiTF314346.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.
ReactomeiREACT_188640. Synthesis of PA.
REACT_237947. Triglyceride Biosynthesis.

Miscellaneous databases

NextBioi308524.
PROiQ9D1E8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D1E8.
ExpressionAtlasiQ9D1E8. baseline and differential.
GenevestigatoriQ9D1E8.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of 1-acylglycerolphosphate acyltransferase-epsilon."
    Lu B., Jiang Y.J., Chan M., Choy P.C.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NMRI.
  2. "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 and NOD.
    Tissue: Bone marrow, Cerebellum, Dendritic cell, Embryo and Spleen.
  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: Czech II.
    Tissue: Mammary gland.
  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.

Entry informationi

Entry nameiPLCE_MOUSE
AccessioniPrimary (citable) accession number: Q9D1E8
Secondary accession number(s): Q3U702, Q8BG61, Q8CGN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 16, 2003
Last modified: January 7, 2015
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-12 is the initiator.Curated

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

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 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.