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Protein

Lysophosphatidylcholine acyltransferase 1

Gene

lpcat1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC) (By similarity).By similarity

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.

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.

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

Enzyme and pathway databases

ReactomeiR-DRE-1482788. Acyl chain remodelling of PC.
R-DRE-1482925. Acyl chain remodelling of PG.
R-DRE-1483166. Synthesis of PA.
R-DRE-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00085.

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
ORF Names:si:dkey-261i16.4, zgc:158232
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 19

Organism-specific databases

ZFINiZDB-GENE-060503-915. lpcat1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5252CytoplasmicSequence analysisAdd
BLAST
Transmembranei53 – 7321Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini74 – 517444LumenalSequence 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 – 517517Lysophosphatidylcholine acyltransferase 1PRO_0000247067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence analysis
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ1LWG4.

Expressioni

Gene expression databases

BgeeiQ1LWG4.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000094631.

Structurei

3D structure databases

ProteinModelPortaliQ1LWG4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini443 – 47836EF-handPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi129 – 1346HXXXXD motif
Motifi514 – 5174Di-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 1 EF-hand domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ1LWG4.
KOiK13510.
OMAiEIEYLPT.
PhylomeDBiQ1LWG4.
TreeFamiTF323244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1LWG4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFPNRKLHT AVNGGDSGVS THFRNPFVHE LRFTTLQKLK IAVMTVTLFP
60 70 80 90 100
VRLLFAAFMM LLAWPFAFVA TVGRSENAVE PLSWWRWLVD LALKAIMRAM
110 120 130 140 150
WFSGGFHWVR VKGRPALPSE APILTMAPHS SYFDAIPVTM TMASIVMKAE
160 170 180 190 200
SKDIPVWGTL IKFIRPVFVS RSDQDSRRKT VEEIKRRASS NGEWPQIMIF
210 220 230 240 250
PEGTCTNRSC LIAFKPGAFI PGVPVQPVVL RYPNELDTIS WTWQGPGAFK
260 270 280 290 300
ILWLTLCQLH NFVEIEYLPT YTPSEEEKKD PALFASNVRR IMAKALGLPI
310 320 330 340 350
IDYSFEDCQL AMAKGPLRLP KHTCLLEFAR LVRLLGLKTK VTDEVLQEEA
360 370 380 390 400
CSARQLCGRR LDMEGFAQYL HQPMTEAVQD IFSLFEEHGM MDVREYVIAL
410 420 430 440 450
SVVCRPFRYL DTVKLAFRMF EAQEDGAIVE DELTVILKTA LGVGDLAVSE
460 470 480 490 500
LFRAIDSQDK GKITFDELCS FMEKCPDLVE QYHCLCESIS QHSRESTSSS
510
NGFCADFSPR NHSKKQD
Length:517
Mass (Da):58,727
Last modified:May 30, 2006 - v1
Checksum:iDA4A17F30B6D39CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471Q → R in AAI29168 (Ref. 2) Curated
Sequence conflicti351 – 3511C → S in AAI29168 (Ref. 2) Curated
Sequence conflicti467 – 4671E → D in AAI29168 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571830 Genomic DNA. Translation: CAK10868.1.
BC129167 mRNA. Translation: AAI29168.1.
RefSeqiNP_001037806.2. NM_001044341.2.
XP_005170093.1. XM_005170036.2.
UniGeneiDr.80588.

Genome annotation databases

EnsembliENSDART00000103855; ENSDARP00000094631; ENSDARG00000011506.
ENSDART00000163382; ENSDARP00000133893; ENSDARG00000011506.
GeneIDi555969.
KEGGidre:555969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX571830 Genomic DNA. Translation: CAK10868.1.
BC129167 mRNA. Translation: AAI29168.1.
RefSeqiNP_001037806.2. NM_001044341.2.
XP_005170093.1. XM_005170036.2.
UniGeneiDr.80588.

3D structure databases

ProteinModelPortaliQ1LWG4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000094631.

Proteomic databases

PaxDbiQ1LWG4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000103855; ENSDARP00000094631; ENSDARG00000011506.
ENSDART00000163382; ENSDARP00000133893; ENSDARG00000011506.
GeneIDi555969.
KEGGidre:555969.

Organism-specific databases

CTDi79888.
ZFINiZDB-GENE-060503-915. lpcat1.

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ1LWG4.
KOiK13510.
OMAiEIEYLPT.
PhylomeDBiQ1LWG4.
TreeFamiTF323244.

Enzyme and pathway databases

UniPathwayiUPA00085.
ReactomeiR-DRE-1482788. Acyl chain remodelling of PC.
R-DRE-1482925. Acyl chain remodelling of PG.
R-DRE-1483166. Synthesis of PA.
R-DRE-75109. Triglyceride Biosynthesis.

Miscellaneous databases

PROiQ1LWG4.

Gene expression databases

BgeeiQ1LWG4.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  2. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiPCAT1_DANRE
AccessioniPrimary (citable) accession number: Q1LWG4
Secondary accession number(s): A1L1Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 30, 2006
Last modified: June 8, 2016
This is version 83 of the entry and version 1 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.