Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D1E8 (PLCE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. 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:
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 names
Name:Agpat5
Synonyms:D8Ertd319e
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

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

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

Subcellular location

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

Tissue specificity

Widely expressed. Ref.4

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 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3653651-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
PRO_0000208201

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane345 – 36521Helical; Potential
Motif93 – 986HXXXXD motif

Experimental info

Sequence conflict801L → W in AAN75571. Ref.1
Sequence conflict1281L → M in AAN75571. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D1E8 [UniParc].

Last modified May 16, 2003. Version 2.
Checksum: C13E14759610E19B

FASTA36542,202
        10         20         30         40         50         60 
MLLSLVLHTY SMRYLLPSVL LLGSAPTYLL AWTLWRVLSA LMPARLYQRV DDRLYCVYQN 

        70         80         90        100        110        120 
MVLFFFENYT GVQILLYGDL PKNKENVIYL ANHQSTVDWI VADMLAARQD ALGHVRYVLK 

       130        140        150        160        170        180 
DKLKWLPLYG FYFAQHGGIY VKRSAKFNDK EMRSKLQSYV NAGTPMYLVI FPEGTRYNAT 

       190        200        210        220        230        240 
YTKLLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDSMKS HLDAIYDVTV VYEGNEKGSG 

       250        260        270        280        290        300 
KYSNPPSMTE FLCKQCPKLH IHFDRIDRNE VPEEQEHMKK WLHERFEIKD RLLIEFYDSP 

       310        320        330        340        350        360 
DPERRNKFPG KSVHSRLSVK KTLPSVLILG SLTAVMLMTE SGRKLYMGTW LYGTLLGCLW 


FVIKA 

« Hide

References

« Hide 'large scale' references
[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. 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 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22126.1.
RefSeqNP_081068.1. NM_026792.3.
UniGeneMm.24117.

3D structure databases

ProteinModelPortalQ9D1E8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206392. 1 interaction.
IntActQ9D1E8. 1 interaction.
STRING10090.ENSMUSP00000117025.

PTM databases

PhosphoSiteQ9D1E8.

Proteomic databases

MaxQBQ9D1E8.
PaxDbQ9D1E8.
PRIDEQ9D1E8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000149565; ENSMUSP00000117025; ENSMUSG00000031467.
GeneID52123.
KEGGmmu:52123.
UCSCuc009kzv.1. mouse.

Organism-specific databases

CTD55326.
MGIMGI:1196345. Agpat5.

Phylogenomic databases

eggNOGCOG0204.
GeneTreeENSGT00530000062943.
HOGENOMHOG000007801.
HOVERGENHBG039632.
InParanoidQ9D1E8.
OMADWIIADM.
OrthoDBEOG7QK0C7.
PhylomeDBQ9D1E8.
TreeFamTF314346.

Enzyme and pathway databases

UniPathwayUPA00557; UER00613.

Gene expression databases

ArrayExpressQ9D1E8.
BgeeQ9D1E8.
GenevestigatorQ9D1E8.

Family and domain databases

InterProIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio308524.
PROQ9D1E8.
SOURCESearch...

Entry information

Entry namePLCE_MOUSE
AccessionPrimary (citable) accession number: Q9D1E8
Secondary accession number(s): Q3U702, Q8BG61, Q8CGN6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 16, 2003
Last modified: July 9, 2014
This is version 92 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