ID   LCLT1_MOUSE             Reviewed;         376 AA.
AC   Q3UN02;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Lysocardiolipin acyltransferase 1;
DE            EC=2.3.1.51;
DE            EC=2.3.1.-;
DE   AltName: Full=Acyl-CoA:lysocardiolipin acyltransferase 1;
GN   Name=Lclat1; Synonyms=Alcat1, Gm91, Lycat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RG   The mouse genome sequencing consortium;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-281.
RC   TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15152008; DOI=10.1074/jbc.M402930200;
RA   Cao J., Liu Y., Lockwood J., Burn P., Shi Y.;
RT   "A novel cardiolipin-remodeling pathway revealed by a gene encoding an
RT   endoplasmic reticulum-associated acyl-CoA:lysocardiolipin
RT   acyltransferase (ALCAT1) in mouse.";
RL   J. Biol. Chem. 279:31727-31734(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16620771; DOI=10.1016/j.abb.2006.03.014;
RA   Agarwal A.K., Barnes R.I., Garg A.;
RT   "Functional characterization of human 1-acylglycerol-3-phosphate
RT   acyltransferase isoform 8: cloning, tissue distribution, gene
RT   structure, and enzymatic activity.";
RL   Arch. Biochem. Biophys. 449:64-76(2006).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17675553; DOI=10.1182/blood-2007-04-086827;
RA   Wang C., Faloon P.W., Tan Z., Lv Y., Zhang P., Ge Y., Deng H.,
RA   Xiong J.-W.;
RT   "Mouse lysocardiolipin acyltransferase controls the development of
RT   hematopoietic and endothelial lineages during in vitro embryonic stem-
RT   cell differentiation.";
RL   Blood 110:3601-3609(2007).
CC   -!- FUNCTION: Acyl-CoA:lysocardiolipin acyltransferase. Possesses both
CC       lysophosphatidylinositol acyltransferase (LPIAT) and
CC       lysophosphatidylglycerol acyltransferase (LPGAT) activities.
CC       Recognizes both monolysocardiolipin and dilysocardiolipin as
CC       substrates with a preference for linoleoyl-CoA and oleoyl-CoA as
CC       acyl donors. Acts as a remodeling enzyme for cardiolipin, a major
CC       membrane polyglycerophospholipid. Converts lysophosphatidic acid
CC       (LPA) into phosphatidic acid (PA) with a relatively low activity.
CC       Required for establishment of the hematopoietic and endothelial
CC       lineages.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest expression in
CC       heart, liver and E12.5 aorta-gonad-mesonephros and lower levels in
CC       the E16 fetal liver and adult bone marrow. In bone marrow, highest
CC       levels are found in B-cells compared with whole bone marrow, T-
CC       cells, erythrocytes, and granulocytes.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
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DR   EMBL; AC112949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK144580; BAE25946.1; -; mRNA.
DR   IPI; IPI00408986; -.
DR   RefSeq; NP_001074540.1; -.
DR   UniGene; Mm.329194; -.
DR   Ensembl; ENSMUSG00000054469; Mus musculus.
DR   GeneID; 225010; -.
DR   KEGG; mmu:225010; -.
DR   NMPDR; fig|10090.3.peg.3374; -.
DR   MGI; MGI:2684937; Lclat1.
DR   HOGENOM; Q3UN02; -.
DR   HOVERGEN; Q3UN02; -.
DR   OMA; Q3UN02; CDIREPL.
DR   BRENDA; 2.3.1.51; 244.
DR   NextBio; 377498; -.
DR   ArrayExpress; Q3UN02; -.
DR   Bgee; Q3UN02; -.
DR   CleanEx; MM_LYCAT; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IEA:EC.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Developmental protein; Endoplasmic reticulum;
KW   Glycoprotein; Membrane; Phospholipid biosynthesis; Transferase;
KW   Transmembrane.
FT   CHAIN         1    376       Lysocardiolipin acyltransferase 1.
FT                                /FTId=PRO_0000291578.
FT   TRANSMEM      9     29       Potential.
FT   TRANSMEM     48     68       Potential.
FT   TRANSMEM    309    329       Potential.
FT   TRANSMEM    336    356       Potential.
FT   MOTIF        85     90       HXXXXD motif.
FT   CARBOHYD     35     35       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   376 AA;  44400 MW;  C2E7AAC40145CD7E CRC64;
     MVSWKGIYFI LFLFAGSFFG SIFMLGPILP LMFINLSWYR WISSRLVATW LTLPVALLET
     MFGVRVVITG DAFVPGERSV IIMNHRTRVD WMFLWNCLMR YSYLRVEKIC LKSSLKSVPG
     FGWAMQVAAF IFIHRKWKDD KSHFEDMIDY FCAIHEPLQL LIFPEGTDLT ENNKARSNDF
     AEKNGLQKYE YVLHPRTTGF TFVVDRLREG KNLDAVHDIT VAYPYNIPQT EKHLLLGDFP
     KEIHFHVQRY PADSLPTSKE DLQLWCHRRW EEKEERLRSF YQGEKNFHFT GQSTVPPCKS
     ELRVLVVKLL SIVYWALFCS AMCLLIYLYS PVRWYFIISI VFFVLQERIF GGLEIIELAC
     YRFLHKHPHL NSKKNE
//