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Q1LWG4 (PCAT1_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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.-
Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase
EC=2.3.1.23
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 names
Name:lpcat1
Synonyms:aytl2
ORF Names:si:dkey-261i16.4, zgc:158232
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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) By similarity.

Catalytic activity

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.

Pathway

Lipid metabolism; phospholipid metabolism.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

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 1 EF-hand domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Lysophosphatidylcholine acyltransferase 1
PRO_0000247067

Regions

Topological domain1 – 5252Cytoplasmic Potential
Transmembrane53 – 7321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain74 – 517444Lumenal Potential
Domain443 – 47836EF-hand
Motif129 – 1346HXXXXD motif
Motif514 – 5174Di-lysine motif

Amino acid modifications

Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation5111N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3471Q → R in AAI29168. Ref.2
Sequence conflict3511C → S in AAI29168. Ref.2
Sequence conflict4671E → D in AAI29168. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q1LWG4 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: DA4A17F30B6D39CD

FASTA51758,727
        10         20         30         40         50         60 
MRFPNRKLHT AVNGGDSGVS THFRNPFVHE LRFTTLQKLK IAVMTVTLFP VRLLFAAFMM 

        70         80         90        100        110        120 
LLAWPFAFVA TVGRSENAVE PLSWWRWLVD LALKAIMRAM WFSGGFHWVR VKGRPALPSE 

       130        140        150        160        170        180 
APILTMAPHS SYFDAIPVTM TMASIVMKAE SKDIPVWGTL IKFIRPVFVS RSDQDSRRKT 

       190        200        210        220        230        240 
VEEIKRRASS NGEWPQIMIF PEGTCTNRSC LIAFKPGAFI PGVPVQPVVL RYPNELDTIS 

       250        260        270        280        290        300 
WTWQGPGAFK ILWLTLCQLH NFVEIEYLPT YTPSEEEKKD PALFASNVRR IMAKALGLPI 

       310        320        330        340        350        360 
IDYSFEDCQL AMAKGPLRLP KHTCLLEFAR LVRLLGLKTK VTDEVLQEEA CSARQLCGRR 

       370        380        390        400        410        420 
LDMEGFAQYL HQPMTEAVQD IFSLFEEHGM MDVREYVIAL SVVCRPFRYL DTVKLAFRMF 

       430        440        450        460        470        480 
EAQEDGAIVE DELTVILKTA LGVGDLAVSE LFRAIDSQDK GKITFDELCS FMEKCPDLVE 

       490        500        510 
QYHCLCESIS QHSRESTSSS NGFCADFSPR NHSKKQD

« Hide

References

[1]The Danio rerio sequencing project at the Sanger Institute
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX571830 Genomic DNA. Translation: CAK10868.1.
BC129167 mRNA. Translation: AAI29168.1.
IPIIPI00497621.
RefSeqNP_001037806.2. NM_001044341.2.
UniGeneDr.80588.

3D structure databases

ProteinModelPortalQ1LWG4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1LWG4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000103855; ENSDARP00000094631; ENSDARG00000011506.
ENSDART00000139433; ENSDARP00000120048; ENSDARG00000011506.
GeneID555969.
KEGGdre:555969.

Organism-specific databases

CTD79888.
ZFINZDB-GENE-060503-915. lpcat1.

Phylogenomic databases

eggNOGfiNOG11461.
GeneTreeENSGT00390000004914.
HOGENOMHBG446767.
HOVERGENHBG060273.
InParanoidQ1LWG4.
OMARAQSNGK.
OrthoDBEOG49GKGF.

Gene expression databases

ArrayExpressQ1LWG4.
BgeeQ1LWG4.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR011992. EF-hand-like_dom.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 2 hits.
KOK13510.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCAT1_DANRE
AccessionPrimary (citable) accession number: Q1LWG4
Secondary accession number(s): A1L1Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 30, 2006
Last modified: November 16, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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