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Reviewed, UniProtKB/Swiss-Prot Q9D1E8 (PLCE_MOUSE)

Last modified January 19, 2010. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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 By similarity.

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

Membrane; Multi-pass membrane protein Potential.

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.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay. Source: MGI

   Molecular function1-acylglycerol-3-phosphate O-acyltransferase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Transmembrane15 – 3521 Potential
Transmembrane345 – 36521 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
Q9D1E8-1 [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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
+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.
IPIIPI00221486.
RefSeqNP_081068.1.
UniGeneMm.24117

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D1E8.

Proteomic databases

PRIDEQ9D1E8.

Genome annotation databases

EnsemblENSMUST00000033847; ENSMUSP00000033847; ENSMUSG00000031467; Mus musculus. [Genome view]
GeneID52123.
KEGGmmu:52123.
UCSCuc009kzv.1. mouse.

Organism-specific databases

CTD52123.
MGIMGI:1196345. Agpat5.

Phylogenomic databases

HOGENOMHBG714220.
HOVERGENQ9D1E8.
InParanoidQ9D1E8.
OMAHVLTPRV.
OrthoDBEOG9NKFG3.
PhylomeDBQ9D1E8.

Enzyme and pathway databases

BRENDA2.3.1.51. 244.

Gene expression databases

ArrayExpressQ9D1E8.
BgeeQ9D1E8.
GenevestigatorQ9D1E8.
GermOnlineENSMUSG00000031467. Mus musculus.

Family and domain databases

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

Other Resources

NextBio308524.
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: January 19, 2010
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents