Full text data of LPCAT1
LPCAT1
(AYTL2, PFAAP3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Lysophosphatidylcholine acyltransferase 1; LPC acyltransferase 1; LPCAT-1; LysoPC acyltransferase 1; 2.3.1.23 (1-acylglycerophosphocholine O-acyltransferase; 1-alkylglycerophosphocholine O-acetyltransferase; 2.3.1.67; Acetyl-CoA:lyso-platelet-activating factor acetyltransferase; Acetyl-CoA:lyso-PAF acetyltransferase; Lyso-PAF acetyltransferase; LysoPAFAT; Acyltransferase-like 2; Phosphonoformate immuno-associated protein 3)
Lysophosphatidylcholine acyltransferase 1; LPC acyltransferase 1; LPCAT-1; LysoPC acyltransferase 1; 2.3.1.23 (1-acylglycerophosphocholine O-acyltransferase; 1-alkylglycerophosphocholine O-acetyltransferase; 2.3.1.67; Acetyl-CoA:lyso-platelet-activating factor acetyltransferase; Acetyl-CoA:lyso-PAF acetyltransferase; Lyso-PAF acetyltransferase; LysoPAFAT; Acyltransferase-like 2; Phosphonoformate immuno-associated protein 3)
hRBCD
IPI00171626
IPI00171626 Hypothetical protein FLJ00365 protein, acyltransferase activity, calcium ion binding, metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00171626 Hypothetical protein FLJ00365 protein, acyltransferase activity, calcium ion binding, metabolism soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q8NF37
ID PCAT1_HUMAN Reviewed; 534 AA.
AC Q8NF37; Q1HAQ1; Q7Z4G6; Q8N3U7; Q8WUL8; Q9GZW6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-JUL-2006, sequence version 2.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 1;
DE Short=LPC acyltransferase 1;
DE Short=LPCAT-1;
DE Short=LysoPC acyltransferase 1;
DE EC=2.3.1.23;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67;
DE AltName: Full=Acetyl-CoA:lyso-platelet-activating factor acetyltransferase;
DE Short=Acetyl-CoA:lyso-PAF acetyltransferase;
DE Short=Lyso-PAF acetyltransferase;
DE Short=LysoPAFAT;
DE AltName: Full=Acyltransferase-like 2;
DE AltName: Full=Phosphonoformate immuno-associated protein 3;
GN Name=LPCAT1; Synonyms=AYTL2, PFAAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16704971; DOI=10.1074/jbc.M600225200;
RA Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R.,
RA Suwabe A., Taguchi R., Shimizu T.;
RT "Cloning and characterization of mouse lung-type acyl-
RT CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1): expression in
RT alveolar type II cells and possible involvement in surfactant
RT production.";
RL J. Biol. Chem. 281:20140-20147(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-534.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-534.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-534.
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 298-534.
RA Liu Y., Cheng J., Lu Y.;
RT "Screening and cloning of a new immuno-associated gene regulated by
RT phosphonoformate.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-534.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=16864775; DOI=10.1073/pnas.0604946103;
RA Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M.;
RT "Identification and characterization of a lysophosphatidylcholine
RT acyltransferase in alveolar type II cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11724-11729(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=21498505; DOI=10.1074/jbc.M110.202424;
RA Moessinger C., Kuerschner L., Spandl J., Shevchenko A., Thiele C.;
RT "Human lysophosphatidylcholine acyltransferases 1 and 2 are located in
RT lipid droplets where they catalyze the formation of
RT phosphatidylcholine.";
RL J. Biol. Chem. 286:21330-21339(2011).
CC -!- FUNCTION: Possesses both acyltransferase and acetyltransferase
CC activities. Activity is calcium-independent. Mediates the
CC conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into
CC phosphatidylcholine (PC). Displays a clear preference for
CC saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as
CC acyl donors and acceptors, respectively. May synthesize
CC phosphatidylcholine in pulmonary surfactant, thereby playing a
CC pivotal role in respiratory physiology.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CC = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 1-alkyl-sn-glycero-3-
CC phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-
CC phosphocholine.
CC -!- ENZYME REGULATION: Not activated by inflammatory stimulation.
CC Inhibited by Cu(2+) and Fe(2+). Activity is not affected by
CC Co(2+), Mg(2+) or Mn(2+) (By similarity).
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type II membrane protein. Golgi apparatus membrane; Single-pass
CC type II membrane protein. Lipid droplet. Note=May adopt a
CC monotopic topology when embedded in the lipid monolayer of the
CC lipid droplet, with both termini exposed to the cytoplasm.
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-phosphocholine (By similarity).
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC localization for type I membrane proteins (By similarity).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14061.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14065.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB244719; BAE94688.1; -; mRNA.
DR EMBL; AK090444; BAC03425.1; -; mRNA.
DR EMBL; BC020166; AAH20166.3; -; mRNA.
DR EMBL; AK022505; BAB14065.1; ALT_INIT; mRNA.
DR EMBL; AK022499; BAB14061.1; ALT_INIT; mRNA.
DR EMBL; AF530061; AAQ09945.1; -; mRNA.
DR EMBL; AL831864; CAD38556.1; -; mRNA.
DR RefSeq; NP_079106.3; NM_024830.3.
DR UniGene; Hs.368853; -.
DR ProteinModelPortal; Q8NF37; -.
DR SMR; Q8NF37; 326-482.
DR IntAct; Q8NF37; 4.
DR STRING; 9606.ENSP00000283415; -.
DR PhosphoSite; Q8NF37; -.
DR DMDM; 110815902; -.
DR PaxDb; Q8NF37; -.
DR PeptideAtlas; Q8NF37; -.
DR PRIDE; Q8NF37; -.
DR DNASU; 79888; -.
DR Ensembl; ENST00000283415; ENSP00000283415; ENSG00000153395.
DR Ensembl; ENST00000475622; ENSP00000423472; ENSG00000153395.
DR GeneID; 79888; -.
DR KEGG; hsa:79888; -.
DR UCSC; uc003jcm.3; human.
DR CTD; 79888; -.
DR GeneCards; GC05M001516; -.
DR HGNC; HGNC:25718; LPCAT1.
DR HPA; HPA012501; -.
DR HPA; HPA022268; -.
DR MIM; 610472; gene.
DR neXtProt; NX_Q8NF37; -.
DR PharmGKB; PA162394232; -.
DR eggNOG; NOG236173; -.
DR HOGENOM; HOG000234374; -.
DR HOVERGEN; HBG060273; -.
DR InParanoid; Q8NF37; -.
DR KO; K13510; -.
DR OMA; SNVRRVM; -.
DR OrthoDB; EOG7NCV5G; -.
DR PhylomeDB; Q8NF37; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00085; -.
DR ChiTaRS; LPCAT1; human.
DR GenomeRNAi; 79888; -.
DR NextBio; 69702; -.
DR PRO; PR:Q8NF37; -.
DR ArrayExpress; Q8NF37; -.
DR Bgee; Q8NF37; -.
DR CleanEx; HS_LPCAT1; -.
DR Genevestigator; Q8NF37; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00563; PlsC; 1.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Calcium; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 534 Lysophosphatidylcholine acyltransferase
FT 1.
FT /FTId=PRO_0000247064.
FT TOPO_DOM 1 57 Cytoplasmic (Potential).
FT TRANSMEM 58 78 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 79 534 Lumenal (Potential).
FT DOMAIN 379 414 EF-hand 1.
FT DOMAIN 451 486 EF-hand 2.
FT CA_BIND 392 403 1 (Potential).
FT MOTIF 135 140 HXXXXD motif.
FT MOTIF 531 534 Di-lysine motif.
SQ SEQUENCE 534 AA; 59151 MW; 69A9C3AEC698F6BD CRC64;
MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT LTLFPVRLLV
AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR
QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ
DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN
KLDTITWTWQ GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK DLDRYSERAR
MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD LRECVVALSV VCRPARTLDT
IQLAFKMYGA QEDGSVGEGD LSCILKTALG VAELTVTDLF RAIDQEEKGK ITFADFHRFA
EMYPAFAEEY LYPDQTHFES CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD
//
ID PCAT1_HUMAN Reviewed; 534 AA.
AC Q8NF37; Q1HAQ1; Q7Z4G6; Q8N3U7; Q8WUL8; Q9GZW6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-JUL-2006, sequence version 2.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 1;
DE Short=LPC acyltransferase 1;
DE Short=LPCAT-1;
DE Short=LysoPC acyltransferase 1;
DE EC=2.3.1.23;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67;
DE AltName: Full=Acetyl-CoA:lyso-platelet-activating factor acetyltransferase;
DE Short=Acetyl-CoA:lyso-PAF acetyltransferase;
DE Short=Lyso-PAF acetyltransferase;
DE Short=LysoPAFAT;
DE AltName: Full=Acyltransferase-like 2;
DE AltName: Full=Phosphonoformate immuno-associated protein 3;
GN Name=LPCAT1; Synonyms=AYTL2, PFAAP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16704971; DOI=10.1074/jbc.M600225200;
RA Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R.,
RA Suwabe A., Taguchi R., Shimizu T.;
RT "Cloning and characterization of mouse lung-type acyl-
RT CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1): expression in
RT alveolar type II cells and possible involvement in surfactant
RT production.";
RL J. Biol. Chem. 281:20140-20147(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-534.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-534.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-534.
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 298-534.
RA Liu Y., Cheng J., Lu Y.;
RT "Screening and cloning of a new immuno-associated gene regulated by
RT phosphonoformate.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-534.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=16864775; DOI=10.1073/pnas.0604946103;
RA Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M.;
RT "Identification and characterization of a lysophosphatidylcholine
RT acyltransferase in alveolar type II cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11724-11729(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=21498505; DOI=10.1074/jbc.M110.202424;
RA Moessinger C., Kuerschner L., Spandl J., Shevchenko A., Thiele C.;
RT "Human lysophosphatidylcholine acyltransferases 1 and 2 are located in
RT lipid droplets where they catalyze the formation of
RT phosphatidylcholine.";
RL J. Biol. Chem. 286:21330-21339(2011).
CC -!- FUNCTION: Possesses both acyltransferase and acetyltransferase
CC activities. Activity is calcium-independent. Mediates the
CC conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into
CC phosphatidylcholine (PC). Displays a clear preference for
CC saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as
CC acyl donors and acceptors, respectively. May synthesize
CC phosphatidylcholine in pulmonary surfactant, thereby playing a
CC pivotal role in respiratory physiology.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CC = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 1-alkyl-sn-glycero-3-
CC phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-
CC phosphocholine.
CC -!- ENZYME REGULATION: Not activated by inflammatory stimulation.
CC Inhibited by Cu(2+) and Fe(2+). Activity is not affected by
CC Co(2+), Mg(2+) or Mn(2+) (By similarity).
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type II membrane protein. Golgi apparatus membrane; Single-pass
CC type II membrane protein. Lipid droplet. Note=May adopt a
CC monotopic topology when embedded in the lipid monolayer of the
CC lipid droplet, with both termini exposed to the cytoplasm.
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-phosphocholine (By similarity).
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC localization for type I membrane proteins (By similarity).
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family.
CC -!- SIMILARITY: Contains 2 EF-hand domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14061.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14065.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB244719; BAE94688.1; -; mRNA.
DR EMBL; AK090444; BAC03425.1; -; mRNA.
DR EMBL; BC020166; AAH20166.3; -; mRNA.
DR EMBL; AK022505; BAB14065.1; ALT_INIT; mRNA.
DR EMBL; AK022499; BAB14061.1; ALT_INIT; mRNA.
DR EMBL; AF530061; AAQ09945.1; -; mRNA.
DR EMBL; AL831864; CAD38556.1; -; mRNA.
DR RefSeq; NP_079106.3; NM_024830.3.
DR UniGene; Hs.368853; -.
DR ProteinModelPortal; Q8NF37; -.
DR SMR; Q8NF37; 326-482.
DR IntAct; Q8NF37; 4.
DR STRING; 9606.ENSP00000283415; -.
DR PhosphoSite; Q8NF37; -.
DR DMDM; 110815902; -.
DR PaxDb; Q8NF37; -.
DR PeptideAtlas; Q8NF37; -.
DR PRIDE; Q8NF37; -.
DR DNASU; 79888; -.
DR Ensembl; ENST00000283415; ENSP00000283415; ENSG00000153395.
DR Ensembl; ENST00000475622; ENSP00000423472; ENSG00000153395.
DR GeneID; 79888; -.
DR KEGG; hsa:79888; -.
DR UCSC; uc003jcm.3; human.
DR CTD; 79888; -.
DR GeneCards; GC05M001516; -.
DR HGNC; HGNC:25718; LPCAT1.
DR HPA; HPA012501; -.
DR HPA; HPA022268; -.
DR MIM; 610472; gene.
DR neXtProt; NX_Q8NF37; -.
DR PharmGKB; PA162394232; -.
DR eggNOG; NOG236173; -.
DR HOGENOM; HOG000234374; -.
DR HOVERGEN; HBG060273; -.
DR InParanoid; Q8NF37; -.
DR KO; K13510; -.
DR OMA; SNVRRVM; -.
DR OrthoDB; EOG7NCV5G; -.
DR PhylomeDB; Q8NF37; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00085; -.
DR ChiTaRS; LPCAT1; human.
DR GenomeRNAi; 79888; -.
DR NextBio; 69702; -.
DR PRO; PR:Q8NF37; -.
DR ArrayExpress; Q8NF37; -.
DR Bgee; Q8NF37; -.
DR CleanEx; HS_LPCAT1; -.
DR Genevestigator; Q8NF37; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid particle; IDA:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00563; PlsC; 1.
DR PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Calcium; Complete proteome; Endoplasmic reticulum;
KW Golgi apparatus; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 534 Lysophosphatidylcholine acyltransferase
FT 1.
FT /FTId=PRO_0000247064.
FT TOPO_DOM 1 57 Cytoplasmic (Potential).
FT TRANSMEM 58 78 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 79 534 Lumenal (Potential).
FT DOMAIN 379 414 EF-hand 1.
FT DOMAIN 451 486 EF-hand 2.
FT CA_BIND 392 403 1 (Potential).
FT MOTIF 135 140 HXXXXD motif.
FT MOTIF 531 534 Di-lysine motif.
SQ SEQUENCE 534 AA; 59151 MW; 69A9C3AEC698F6BD CRC64;
MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT LTLFPVRLLV
AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR
QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ
DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN
KLDTITWTWQ GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK DLDRYSERAR
MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD LRECVVALSV VCRPARTLDT
IQLAFKMYGA QEDGSVGEGD LSCILKTALG VAELTVTDLF RAIDQEEKGK ITFADFHRFA
EMYPAFAEEY LYPDQTHFES CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD
//
MIM
610472
*RECORD*
*FIELD* NO
610472
*FIELD* TI
*610472 ACYLTRANSFERASE-LIKE 2; AYTL2
;;LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE; LPCAT;;
read moreLPC ACYLTRANSFERASE 1; LPCAT1
*FIELD* TX
DESCRIPTION
Lysophosphatidylcholine (LPC) acyltransferase (LPCAT; EC 2.3.1.23)
catalyzes the conversion of LPC to phosphatidylcholine (PC) in the
remodeling pathway of PC biosynthesis (Nakanishi et al., 2006).
CLONING
Nakanishi et al. (2006) cloned mouse Lpcat1 and identified its human
homolog. The deduced 534-amino acid mouse and human proteins contain 3
transmembrane domains, several motifs conserved in members of the LPCAT
family, a putative EF hand domain, and a C-terminal endoplasmic
reticulum (ER) retention signal. They share about 88% amino acid
identity. Real-time RT-PCR of mouse tissues showed that Lpcat1 was
expressed at highest levels in lung, followed by spleen and brain. Other
tissues had low Lpcat1 levels. Confocal microscopy detected
epitope-tagged Lpcat1 mainly in the ER and Golgi of transfected cells.
Independently, Chen et al. (2006) cloned mouse and rat Lpcat1. In situ
hybridization of adult mouse lung detected Lpcat1 in epithelial cells of
the alveolar wall, but not in airway epithelium. RT-PCR showed higher
levels of Lpcat1 in isolated rat alveolar type II cells than in whole
lung.
GENE FUNCTION
Nakanishi et al. (2006) found that mouse Lpcat1 exhibited
Ca(2+)-independent acyltransferase activity, with a pH optimum between
7.4 and 10, when expressed in Chinese hamster ovary cells. Lpcat1
preferred saturated fatty acyl-CoAs as acyl donors and 1-myristoyl- or
1-palmitoyl-LPC as acyl acceptor. Nakanishi et al. (2006) concluded that
LPCAT1 might synthesize PC in pulmonary surfactant.
Chen et al. (2006) showed that rat Lpcat1 preferred LPC over several
other acceptor substrates studied. It preferred palmitoyl-CoA to
oleoyl-CoA as the acyl donor. Expression of Lpcat1 increased with time
in cultured day-16.5 mouse lung explants. Dexamethasone treatment
significantly increased Lpcat expression in lung explants, whereas
inhibition of Fgf (see FGF7; 148180) signaling prevented the increase in
Lpcat expression. Fgf7 increased differentiation of rat alveolar type II
cells, with a concomitant increase in Lpcat mRNA, when they were
cultured on a permissive matrix. Dedifferentiation of alveolar type II
cells reduced Lpcat expression. Chen et al. (2006) proposed that LPCAT
plays a critical role in regulating surfactant phospholipid
biosynthesis.
Soupene et al. (2008) expressed mouse Aytl2 in E. coli membranes and
found that it acylated lysophosphatidylcholine in the presence of
various acyl-CoA donors. It acylated lysophosphatidylethanolamine at a
lower rate, but not other lysophospholipids tested. Formation of
phosphatidylcholine from lysophosphatidylcholine by Aytl2 was inhibited
by calcium and magnesium.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AYTL2
gene to chromosome 5 (TMAP A003B27).
*FIELD* RF
1. Chen, X.; Hyatt, B. A.; Mucenski, M. L.; Mason, R. J.; Shannon,
J. M.: Identification and characterization of a lysophosphatidylcholine
acyltransferase in alveolar type II cells. Proc. Nat. Acad. Sci. 103:
11724-11729, 2006.
2. Nakanishi, H.; Shindou, H.; Hishikawa, D.; Harayama, T.; Ogasawara,
R.; Suwabe, A.; Taguchi, R.; Shimizu, T.: Cloning and characterization
of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase
1 (LPCAT1): expression in alveolar type II cells and possible involvement
in surfactant production. J. Biol. Chem. 281: 20140-20147, 2006.
3. Soupene, E.; Fyrst, H.; Kuypers, F. A.: Mammalian acyl-CoA:lysophosphatidylcholine
acyltransferase enzymes. Proc. Nat. Acad. Sci. 105: 88-93, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 4/18/2008
*FIELD* CD
Patricia A. Hartz: 10/10/2006
*FIELD* ED
mgross: 05/09/2008
terry: 4/18/2008
mgross: 10/10/2006
*RECORD*
*FIELD* NO
610472
*FIELD* TI
*610472 ACYLTRANSFERASE-LIKE 2; AYTL2
;;LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE; LPCAT;;
read moreLPC ACYLTRANSFERASE 1; LPCAT1
*FIELD* TX
DESCRIPTION
Lysophosphatidylcholine (LPC) acyltransferase (LPCAT; EC 2.3.1.23)
catalyzes the conversion of LPC to phosphatidylcholine (PC) in the
remodeling pathway of PC biosynthesis (Nakanishi et al., 2006).
CLONING
Nakanishi et al. (2006) cloned mouse Lpcat1 and identified its human
homolog. The deduced 534-amino acid mouse and human proteins contain 3
transmembrane domains, several motifs conserved in members of the LPCAT
family, a putative EF hand domain, and a C-terminal endoplasmic
reticulum (ER) retention signal. They share about 88% amino acid
identity. Real-time RT-PCR of mouse tissues showed that Lpcat1 was
expressed at highest levels in lung, followed by spleen and brain. Other
tissues had low Lpcat1 levels. Confocal microscopy detected
epitope-tagged Lpcat1 mainly in the ER and Golgi of transfected cells.
Independently, Chen et al. (2006) cloned mouse and rat Lpcat1. In situ
hybridization of adult mouse lung detected Lpcat1 in epithelial cells of
the alveolar wall, but not in airway epithelium. RT-PCR showed higher
levels of Lpcat1 in isolated rat alveolar type II cells than in whole
lung.
GENE FUNCTION
Nakanishi et al. (2006) found that mouse Lpcat1 exhibited
Ca(2+)-independent acyltransferase activity, with a pH optimum between
7.4 and 10, when expressed in Chinese hamster ovary cells. Lpcat1
preferred saturated fatty acyl-CoAs as acyl donors and 1-myristoyl- or
1-palmitoyl-LPC as acyl acceptor. Nakanishi et al. (2006) concluded that
LPCAT1 might synthesize PC in pulmonary surfactant.
Chen et al. (2006) showed that rat Lpcat1 preferred LPC over several
other acceptor substrates studied. It preferred palmitoyl-CoA to
oleoyl-CoA as the acyl donor. Expression of Lpcat1 increased with time
in cultured day-16.5 mouse lung explants. Dexamethasone treatment
significantly increased Lpcat expression in lung explants, whereas
inhibition of Fgf (see FGF7; 148180) signaling prevented the increase in
Lpcat expression. Fgf7 increased differentiation of rat alveolar type II
cells, with a concomitant increase in Lpcat mRNA, when they were
cultured on a permissive matrix. Dedifferentiation of alveolar type II
cells reduced Lpcat expression. Chen et al. (2006) proposed that LPCAT
plays a critical role in regulating surfactant phospholipid
biosynthesis.
Soupene et al. (2008) expressed mouse Aytl2 in E. coli membranes and
found that it acylated lysophosphatidylcholine in the presence of
various acyl-CoA donors. It acylated lysophosphatidylethanolamine at a
lower rate, but not other lysophospholipids tested. Formation of
phosphatidylcholine from lysophosphatidylcholine by Aytl2 was inhibited
by calcium and magnesium.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the AYTL2
gene to chromosome 5 (TMAP A003B27).
*FIELD* RF
1. Chen, X.; Hyatt, B. A.; Mucenski, M. L.; Mason, R. J.; Shannon,
J. M.: Identification and characterization of a lysophosphatidylcholine
acyltransferase in alveolar type II cells. Proc. Nat. Acad. Sci. 103:
11724-11729, 2006.
2. Nakanishi, H.; Shindou, H.; Hishikawa, D.; Harayama, T.; Ogasawara,
R.; Suwabe, A.; Taguchi, R.; Shimizu, T.: Cloning and characterization
of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase
1 (LPCAT1): expression in alveolar type II cells and possible involvement
in surfactant production. J. Biol. Chem. 281: 20140-20147, 2006.
3. Soupene, E.; Fyrst, H.; Kuypers, F. A.: Mammalian acyl-CoA:lysophosphatidylcholine
acyltransferase enzymes. Proc. Nat. Acad. Sci. 105: 88-93, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 4/18/2008
*FIELD* CD
Patricia A. Hartz: 10/10/2006
*FIELD* ED
mgross: 05/09/2008
terry: 4/18/2008
mgross: 10/10/2006