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Reviewed, UniProtKB/Swiss-Prot Q3UN02 (LCLT1_MOUSE)

Last modified June 16, 2009. Version 29. 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:
    Lysocardiolipin acyltransferase 1
    EC=2.3.1.51
    EC=2.3.1.-
Alternative name(s):
    Acyl-CoA:lysocardiolipin acyltransferase 1
Gene names
Name: Lclat1
Synonyms: Alcat1, Gm91, Lycat
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 length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Acyl-CoA:lysocardiolipin acyltransferase. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Acts as a remodeling enzyme for cardiolipin, a major membrane polyglycerophospholipid. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) with a relatively low activity. Required for establishment of the hematopoietic and endothelial lineages. Ref.3 Ref.5

Catalytic activity

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

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. Ref.3

Tissue specificity

Widely expressed with highest expression in heart, liver and E12.5 aorta-gonad-mesonephros and lower levels in the E16 fetal liver and adult bone marrow. In bone marrow, highest levels are found in B-cells compared with whole bone marrow, T-cells, erythrocytes, and granulocytes. Ref.3 Ref.5 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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Lysocardiolipin acyltransferase 1
PRO_0000291578

Regions

Transmembrane9 – 2921 Potential
Transmembrane48 – 6821 Potential
Transmembrane309 – 32921 Potential
Transmembrane336 – 35621 Potential
Motif85 – 906HXXXXD motif

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q3UN02-1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: C2E7AAC40145CD7E

FASTA37644,400
        10         20         30         40         50         60 
MVSWKGIYFI LFLFAGSFFG SIFMLGPILP LMFINLSWYR WISSRLVATW LTLPVALLET 

        70         80         90        100        110        120 
MFGVRVVITG DAFVPGERSV IIMNHRTRVD WMFLWNCLMR YSYLRVEKIC LKSSLKSVPG 

       130        140        150        160        170        180 
FGWAMQVAAF IFIHRKWKDD KSHFEDMIDY FCAIHEPLQL LIFPEGTDLT ENNKARSNDF 

       190        200        210        220        230        240 
AEKNGLQKYE YVLHPRTTGF TFVVDRLREG KNLDAVHDIT VAYPYNIPQT EKHLLLGDFP 

       250        260        270        280        290        300 
KEIHFHVQRY PADSLPTSKE DLQLWCHRRW EEKEERLRSF YQGEKNFHFT GQSTVPPCKS 

       310        320        330        340        350        360 
ELRVLVVKLL SIVYWALFCS AMCLLIYLYS PVRWYFIISI VFFVLQERIF GGLEIIELAC 

       370 
YRFLHKHPHL NSKKNE

« Hide

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References

« Hide 'large scale' references
[1]The mouse genome sequencing consortium
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] OF 1-281.
Tissue: Lung.
[3]"A novel cardiolipin-remodeling pathway revealed by a gene encoding an endoplasmic reticulum-associated acyl-CoA:lysocardiolipin acyltransferase (ALCAT1) in mouse."
Cao J., Liu Y., Lockwood J., Burn P., Shi Y.
J. Biol. Chem. 279:31727-31734(2004) [PubMed: 15152008] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity."
Agarwal A.K., Barnes R.I., Garg A.
Arch. Biochem. Biophys. 449:64-76(2006) [PubMed: 16620771] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Mouse lysocardiolipin acyltransferase controls the development of hematopoietic and endothelial lineages during in vitro embryonic stem-cell differentiation."
Wang C., Faloon P.W., Tan Z., Lv Y., Zhang P., Ge Y., Deng H., Xiong J.-W.
Blood 110:3601-3609(2007) [PubMed: 17675553] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.

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Cross-references

Sequence databases

AC112949 Genomic DNA. No translation available.
AK144580 mRNA. Translation: BAE25946.1.
IPIIPI00408986.
RefSeqNP_001074540.1.
UniGeneMm.329194

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000054469. Mus musculus. [Contig view]
GeneID225010.
KEGGmmu:225010.
NMPDRfig|10090.3.peg.3374.

Organism-specific databases

MGIMGI:2684937. Lclat1.

Phylogenomic databases

HOGENOMQ3UN02.
HOVERGENQ3UN02.
OMAQ3UN02. CDIREPL.

Enzyme and pathway databases

BRENDA2.3.1.51. 244.

Gene expression databases

ArrayExpressQ3UN02.
BgeeQ3UN02.
CleanExMM_LYCAT.

Family and domain databases

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

Other Resources

NextBio377498.
SOURCESearch...

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Entry information

Entry nameLCLT1_MOUSE
AccessionPrimary (citable) accession number: Q3UN02
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: June 16, 2009
This is version 29 of the entry and version 2 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