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Protein

Lysophosphatidylcholine acyltransferase 1

Gene

Lpcat1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Possesses both acyltransferase and acetyltransferase activities (PubMed:16864775). Activity is calcium-independent (By similarity). Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC) (PubMed:16864775). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively (PubMed:16864775). May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology (PubMed:16864775). Involved in the regulation of lipid droplet number and size (By similarity).By similarity1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine.

Enzyme regulationi

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

Pathwayi: phospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi392 – 403121PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi2.3.1.23. 5301.
ReactomeiR-RNO-1482788. Acyl chain remodelling of PC.
R-RNO-1482925. Acyl chain remodelling of PG.
R-RNO-1483166. Synthesis of PA.
R-RNO-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00085.

Chemistry

SwissLipidsiSLP:000000296.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophosphatidylcholine acyltransferase 1 (EC:2.3.1.23)
Short name:
LPC acyltransferase 1
Short name:
LPCAT-1
Short name:
LysoPC acyltransferase 1
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
Gene namesi
Name:Lpcat1
Synonyms:Aytl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1311599. Lpcat1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757CytoplasmicSequence analysisAdd
BLAST
Transmembranei58 – 7821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini79 – 534456LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Lysophosphatidylcholine acyltransferase 1PRO_0000247066Add
BLAST

Proteomic databases

PaxDbiQ1HAQ0.
PRIDEiQ1HAQ0.

PTM databases

SwissPalmiQ1HAQ0.

Expressioni

Tissue specificityi

Enriched in alveolar type II cells of lung. Also highly expressed in stomach.2 Publications

Inductioni

By FGF7.1 Publication

Gene expression databases

GenevisibleiQ1HAQ0. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024111.

Structurei

3D structure databases

ProteinModelPortaliQ1HAQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini379 – 41436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini451 – 48636EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi135 – 1406HXXXXD motif
Motifi531 – 5344Di-lysine motif

Domaini

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 similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ1HAQ0.
KOiK13510.
OMAiDYLYPDQ.
OrthoDBiEOG7NCV5G.
PhylomeDBiQ1HAQ0.
TreeFamiTF323244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1HAQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLRGRGPRA APSSSSGAGD ARRLAPPGRN PFVHELRLSA LQKAQVAFMT
60 70 80 90 100
LTLFPIRLLF AAFMMLLAWP FALVASLGPP DKEPEQPLAL WRKVVDFLLK
110 120 130 140 150
AIMRTMWFAG GFHRVAVKGR QALPTEAAIL TLAPHSSYFD AIPVTMTMSS
160 170 180 190 200
IVMKAESRDI PIWGTLIRYI RPVFVSRSDQ DSRRKTVEEI KRRAQSNGKW
210 220 230 240 250
PQIMIFPEGT CTNRTCLITF KPGAFIPGVP VQPVVLRYPN KLDTITWTWQ
260 270 280 290 300
GPGALKILWL TLCQFQNQVE IEFLPVYCPS EEEKRNPALY ASNVRRVMAK
310 320 330 340 350
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPENLEK
360 370 380 390 400
DLDKYSESAR MKRGEKIRLP EFAAYLEVPV SDALEDMFSL FDESGGGEID
410 420 430 440 450
LREYVVALSV VCRPSQTLAT IQLAFKMYGS PEDGSIDEAD LSCILKTALG
460 470 480 490 500
ISELTVTDLF QAIDQEERGR ITFDDFCGFA EMYPDFAEDY LYPDQTHSDS
510 520 530
CAQTPPAPTP NGFCIDFSPE HSDFGRKNSC KKVD
Length:534
Mass (Da):59,762
Last modified:July 25, 2006 - v2
Checksum:i952C0478DC66738A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03001349 Genomic DNA. No translation available.
AABR03001854 Genomic DNA. No translation available.
AB244983 mRNA. Translation: BAE94689.2.
RefSeqiNP_001094205.1. NM_001100735.1.
UniGeneiRn.16547.

Genome annotation databases

EnsembliENSRNOT00000024111; ENSRNOP00000024111; ENSRNOG00000017930.
GeneIDi361467.
KEGGirno:361467.
UCSCiRGD:1311599. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03001349 Genomic DNA. No translation available.
AABR03001854 Genomic DNA. No translation available.
AB244983 mRNA. Translation: BAE94689.2.
RefSeqiNP_001094205.1. NM_001100735.1.
UniGeneiRn.16547.

3D structure databases

ProteinModelPortaliQ1HAQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024111.

Chemistry

SwissLipidsiSLP:000000296.

PTM databases

SwissPalmiQ1HAQ0.

Proteomic databases

PaxDbiQ1HAQ0.
PRIDEiQ1HAQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024111; ENSRNOP00000024111; ENSRNOG00000017930.
GeneIDi361467.
KEGGirno:361467.
UCSCiRGD:1311599. rat.

Organism-specific databases

CTDi79888.
RGDi1311599. Lpcat1.

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ1HAQ0.
KOiK13510.
OMAiDYLYPDQ.
OrthoDBiEOG7NCV5G.
PhylomeDBiQ1HAQ0.
TreeFamiTF323244.

Enzyme and pathway databases

UniPathwayiUPA00085.
BRENDAi2.3.1.23. 5301.
ReactomeiR-RNO-1482788. Acyl chain remodelling of PC.
R-RNO-1482925. Acyl chain remodelling of PG.
R-RNO-1483166. Synthesis of PA.
R-RNO-75109. Triglyceride Biosynthesis.

Miscellaneous databases

NextBioi676408.
PROiQ1HAQ0.

Gene expression databases

GenevisibleiQ1HAQ0. RN.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "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] OF 46-534, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPCAT1_RAT
AccessioniPrimary (citable) accession number: Q1HAQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: May 11, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.