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Q8NF37 (PCAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysophosphatidylcholine acyltransferase 1

Short name=LPC acyltransferase 1
Short name=LPCAT-1
Short name=LysoPC acyltransferase 1
EC=2.3.1.23
Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase
1-alkylglycerophosphocholine O-acetyltransferase
EC=2.3.1.67
Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
Short name=Acetyl-CoA:lyso-PAF acetyltransferase
Short name=Lyso-PAF acetyltransferase
Short name=LysoPAFAT
Acyltransferase-like 2
Phosphonoformate immuno-associated protein 3
Gene names
Name:LPCAT1
Synonyms:AYTL2, PFAAP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology. Ref.7 Ref.9

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Ref.9

Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine. Ref.9

Enzyme regulation

Not activated by inflammatory stimulation. Inhibited by Cu2+ and Fe2+. Activity is not affected by Co2+, Mg2+ or Mn2+ By similarity.

Pathway

Lipid metabolism; phospholipid metabolism. Ref.9

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Lipid droplet. Note: May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm. Ref.9

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine By similarity.

The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins By similarity.

Sequence similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Contains 2 EF-hand domains.

Sequence caution

The sequence BAB14061.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentEndoplasmic reticulum
Golgi apparatus
Lipid droplet
Membrane
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular lipid metabolic process

Traceable author statement. Source: Reactome

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

negative regulation of phosphatidylcholine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylcholine acyl-chain remodeling

Inferred from direct assay Ref.9. Source: UniProtKB

phosphatidylglycerol acyl-chain remodeling

Traceable author statement. Source: Reactome

phospholipid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

surfactant homeostasis

Inferred from electronic annotation. Source: Ensembl

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay Ref.9. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lipid particle

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_function1-acylglycerophosphocholine O-acyltransferase activity

Inferred from direct assay Ref.9. Source: UniProtKB

1-alkenylglycerophosphocholine O-acyltransferase activity

Inferred from electronic annotation. Source: Ensembl

1-alkylglycerophosphocholine O-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

1-alkylglycerophosphocholine O-acyltransferase activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 534534Lysophosphatidylcholine acyltransferase 1
PRO_0000247064

Regions

Topological domain1 – 5757Cytoplasmic Potential
Transmembrane58 – 7821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain79 – 534456Lumenal Potential
Domain379 – 41436EF-hand 1
Domain451 – 48636EF-hand 2
Calcium binding392 – 403121 Potential
Motif135 – 1406HXXXXD motif
Motif531 – 5344Di-lysine motif

Sequences

Sequence LengthMass (Da)Tools
Q8NF37 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 69A9C3AEC698F6BD

FASTA53459,151
        10         20         30         40         50         60 
MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT LTLFPVRLLV 

        70         80         90        100        110        120 
AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR 

       130        140        150        160        170        180 
QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ 

       190        200        210        220        230        240 
DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN 

       250        260        270        280        290        300 
KLDTITWTWQ GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE 

       310        320        330        340        350        360 
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK DLDRYSERAR 

       370        380        390        400        410        420 
MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD LRECVVALSV VCRPARTLDT 

       430        440        450        460        470        480 
IQLAFKMYGA QEDGSVGEGD LSCILKTALG VAELTVTDLF RAIDQEEKGK ITFADFHRFA 

       490        500        510        520        530 
EMYPAFAEEY LYPDQTHFES CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD 

« Hide

References

« Hide 'large scale' references
[1]"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."
Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R., Suwabe A., Taguchi R., Shimizu T.
J. Biol. Chem. 281:20140-20147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-534.
Tissue: Spleen.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-534.
Tissue: Eye.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-534.
Tissue: Teratocarcinoma.
[5]"Screening and cloning of a new immuno-associated gene regulated by phosphonoformate."
Liu Y., Cheng J., Lu Y.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 298-534.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-534.
Tissue: Amygdala.
[7]"Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells."
Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:11724-11729(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, FUNCTION.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Human lysophosphatidylcholine acyltransferases 1 and 2 are located in lipid droplets where they catalyze the formation of phosphatidylcholine."
Moessinger C., Kuerschner L., Spandl J., Shevchenko A., Thiele C.
J. Biol. Chem. 286:21330-21339(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB244719 mRNA. Translation: BAE94688.1.
AK090444 mRNA. Translation: BAC03425.1.
BC020166 mRNA. Translation: AAH20166.3.
AK022505 mRNA. Translation: BAB14065.1. Different initiation.
AK022499 mRNA. Translation: BAB14061.1. Different initiation.
AF530061 mRNA. Translation: AAQ09945.1.
AL831864 mRNA. Translation: CAD38556.1.
RefSeqNP_079106.3. NM_024830.3.
UniGeneHs.368853.

3D structure databases

ProteinModelPortalQ8NF37.
SMRQ8NF37. Positions 348-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122973. 13 interactions.
IntActQ8NF37. 4 interactions.
STRING9606.ENSP00000283415.

PTM databases

PhosphoSiteQ8NF37.

Polymorphism databases

DMDM110815902.

Proteomic databases

PaxDbQ8NF37.
PeptideAtlasQ8NF37.
PRIDEQ8NF37.

Protocols and materials databases

DNASU79888.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283415; ENSP00000283415; ENSG00000153395.
ENST00000475622; ENSP00000423472; ENSG00000153395.
GeneID79888.
KEGGhsa:79888.
UCSCuc003jcm.3. human.

Organism-specific databases

CTD79888.
GeneCardsGC05M001516.
HGNCHGNC:25718. LPCAT1.
HPAHPA012501.
HPA022268.
MIM610472. gene.
neXtProtNX_Q8NF37.
PharmGKBPA162394232.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236173.
HOGENOMHOG000234374.
HOVERGENHBG060273.
InParanoidQ8NF37.
KOK13510.
OMASNVRRVM.
OrthoDBEOG7NCV5G.
PhylomeDBQ8NF37.
TreeFamTF323244.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00085.

Gene expression databases

ArrayExpressQ8NF37.
BgeeQ8NF37.
CleanExHS_LPCAT1.
GenevestigatorQ8NF37.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLPCAT1. human.
GenomeRNAi79888.
NextBio69702.
PROQ8NF37.
SOURCESearch...

Entry information

Entry namePCAT1_HUMAN
AccessionPrimary (citable) accession number: Q8NF37
Secondary accession number(s): Q1HAQ1 expand/collapse secondary AC list , Q7Z4G6, Q8N3U7, Q8WUL8, Q9GZW6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: April 16, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM