Q3UN02 (LCLT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysocardiolipin acyltransferase 1
EC=2.3.1.-
EC=2.3.1.51

Alternative name(s):
Acyl-CoA:lysocardiolipin acyltransferase 1

Gene names

Name:	Lclat1
Synonyms:	Alcat1, Gm91, Lycat

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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.4 Ref.5
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.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Developmental protein Transferase
PTM	Acetylation Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	Lysocardiolipin acyltransferase 1		PRO_0000291578
Regions
	Transmembrane	9 – 29	21	Helical; Potential
	Transmembrane	48 – 68	21	Helical; Potential
	Transmembrane	309 – 329	21	Helical; Potential
	Transmembrane	336 – 356	21	Helical; Potential
	Motif	85 – 90	6	HXXXXD motif
Amino acid modifications
	Modified residue	183	1	N6-acetyllysine By similarity
	Glycosylation	35	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q3UN02 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: C2E7AAC40145CD7E	FASTA	376	44,400
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] 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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC112949 Genomic DNA. No translation available. AK144580 mRNA. Translation: BAE25946.1.
IPI	IPI00408986.
RefSeq	NP_001074540.1. NM_001081071.2. NP_001171438.1. NM_001177967.1. NP_001171439.1. NM_001177968.1.
UniGene	Mm.329194.
3D structure databases
ProteinModelPortal	Q3UN02.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3UN02.
PTM databases
PhosphoSite	Q3UN02.
Proteomic databases
PRIDE	Q3UN02.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067545; ENSMUSP00000068690; ENSMUSG00000054469.
GeneID	225010.
KEGG	mmu:225010.
NMPDR	fig|10090.3.peg.3374.
Organism-specific databases
CTD	253558.
MGI	MGI:2684937. Lclat1.
Phylogenomic databases
eggNOG	roNOG08547.
GeneTree	ENSGT00530000062943.
HOGENOM	HBG444100.
HOVERGEN	HBG055624.
InParanoid	Q3UN02.
OMA	CDIREPL.
OrthoDB	EOG4R7V9T.
Gene expression databases
ArrayExpress	Q3UN02.
Bgee	Q3UN02.
CleanEx	MM_LYCAT.
Genevestigator	Q3UN02.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
KO	K13513.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	377498.
SOURCE	Search...

Entry information

Entry name

LCLT1_MOUSE

Accession

Primary (citable) accession number: Q3UN02

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	November 16, 2011
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program