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Reviewed, UniProtKB/Swiss-Prot Q8K4X7 (PLCD_MOUSE)

Last modified June 16, 2009. Version 49. 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

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Names and origin

Protein namesRecommended 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 names
Name: Agpat4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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.

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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-KW

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3783781-acyl-sn-glycerol-3-phosphate acyltransferase delta
PRO_0000208198

Regions

Transmembrane11 – 3121 Potential
Transmembrane125 – 14521 Potential
Transmembrane311 – 33121 Potential
Transmembrane338 – 35821 Potential
Motif96 – 1016HXXXXD motif

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Sequences

Sequence LengthMass (Da)Tools
Q8K4X7-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 3D9EF15B6A5E49BC

FASTA37843,810
        10         20         30         40         50         60 
MDLIGLLKSQ FLCHLVFCYV FIASGLIVNA IQLCTLVIWP INKQLFRKIN ARLCYCVSSQ 

        70         80         90        100        110        120 
LVMLLEWWSG TECTIYTDPK ACPHYGKENA IVVLNHKFEI DFLCGWSLAE RLGILGNSKV 

       130        140        150        160        170        180 
LAKKELAYVP IIGWMWYFVE MIFCTRKWEQ DRQTVAKSLL HLRDYPEKYL FLIHCEGTRF 

       190        200        210        220        230        240 
TEKKHQISMQ VAQAKGLPSL KHHLLPRTKG FAITVKCLRD VVPAVYDCTL NFRNNENPTL 

       250        260        270        280        290        300 
LGVLNGKKYH ADCYVRRIPM EDIPEDEDKC SAWLHKLYQE KDAFQEEYYR TGVFPETPWV 

       310        320        330        340        350        360 
PPRRPWSLVN WLFWASLLLY PFFQFLVSMV SSGSSVTLAS LVLIFCMASM GVRWMIGVTE 

       370 
IDKGSAYGNI DNKRKQTD

« Hide

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References

[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. 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.
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.

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Cross-references

Sequence databases

AK005139 mRNA. Translation: BAB23837.2.
AK166917 mRNA. Translation: BAE39115.1.
AF485269 Genomic DNA. Translation: AAM33375.1.
BC047281 mRNA. Translation: AAH47281.1.
IPIIPI00173168.
RefSeqNP_080920.2.
UniGeneMm.258300

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8K4X7. 1 interaction.

Proteomic databases

PRIDEQ8K4X7.

Genome annotation databases

EnsemblENSMUSG00000023827. Mus musculus. [Contig view]
GeneID68262.
KEGGmmu:68262.

Organism-specific databases

MGIMGI:1915512. Agpat4.

Phylogenomic databases

HOGENOMQ8K4X7.
HOVERGENQ8K4X7.
OMAQ8K4X7. LVNWLFW.

Enzyme and pathway databases

BRENDA2.3.1.51. 244.

Gene expression databases

ArrayExpressQ8K4X7.
BgeeQ8K4X7.
GermOnlineENSMUSG00000023827. 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

NextBio326850.
SOURCESearch...

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Entry information

Entry namePLCD_MOUSE
AccessionPrimary (citable) accession number: Q8K4X7
Secondary accession number(s): Q3TKN0, Q9DB84
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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