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Protein

Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1

Gene

acl-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.By similarity

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathwayi: CDP-diacylglycerol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Probable glycerol-3-phosphate acyltransferase, mitochondrial (acl-6)
  2. Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-2 (acl-2), Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1 (acl-1), Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-12 (acl-12)
  3. Phosphatidate cytidylyltransferase (cdgs-1), Phosphatidate cytidylyltransferase, mitochondrial (Y71F9B.2)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid 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

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1 (EC:2.3.1.51)
Short name:
1-AGP acyltransferase
Short name:
1-AGPAT
Alternative name(s):
Lysophosphatidic acid acyltransferase
Short name:
LPAAT
Gene namesi
Name:acl-1
ORF Names:F59F4.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF59F4.4; CE11552; WBGene00010339; acl-1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei3 – 2321HelicalSequence analysisAdd
BLAST
Transmembranei29 – 4921HelicalSequence analysisAdd
BLAST
Transmembranei89 – 10921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1PRO_0000208202Add
BLAST

Proteomic databases

EPDiQ93841.
PaxDbiQ93841.
PRIDEiQ93841.

Interactioni

Protein-protein interaction databases

STRINGi6239.F59F4.4.

Structurei

3D structure databases

ProteinModelPortaliQ93841.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 996HXXXXD motif

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2848. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00390000008726.
HOGENOMiHOG000026375.
InParanoidiQ93841.
KOiK13509.
OMAiFQAMTWP.
OrthoDBiEOG780RNF.
PhylomeDBiQ93841.

Family and domain databases

InterProiIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00530. AGP_acyltrn. 1 hit.

Sequencei

Sequence statusi: Complete.

Q93841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFLAILFVI AVLLLLAQLP VIGFYIRAVY FGMCLIIGGF LGGLASIPFG
60 70 80 90 100
KSPNNHFRMF KIFQAMTWPM GVRFELRNSE ILHDKKPYII IANHQSALDV
110 120 130 140 150
LGMSFAWPVD CVVMLKSSLK YLPGFNLCAY LCDSVYINRF SKEKALKTVD
160 170 180 190 200
TTLHEIVTKK RKVWIYPEGT RNAEPELLPF KKGAFILAKQ AKIPIVPCVF
210 220 230 240 250
SSHKFFYSHA EKRLTSGNCI IDILPEVDSS KFDSIDDLSA HCRKIMQAHR
260
EKLDAEAANL NI
Length:262
Mass (Da):29,638
Last modified:December 15, 1998 - v2
Checksum:i0361FE6C9710593E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z81095, Z81089 Genomic DNA. Translation: CAB03160.1.
PIRiT22599.
RefSeqiNP_510606.1. NM_078205.5.
UniGeneiCel.823.

Genome annotation databases

EnsemblMetazoaiF59F4.4; F59F4.4; WBGene00010339.
GeneIDi181671.
KEGGicel:CELE_F59F4.4.
UCSCiF59F4.4. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z81095, Z81089 Genomic DNA. Translation: CAB03160.1.
PIRiT22599.
RefSeqiNP_510606.1. NM_078205.5.
UniGeneiCel.823.

3D structure databases

ProteinModelPortaliQ93841.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F59F4.4.

Proteomic databases

EPDiQ93841.
PaxDbiQ93841.
PRIDEiQ93841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF59F4.4; F59F4.4; WBGene00010339.
GeneIDi181671.
KEGGicel:CELE_F59F4.4.
UCSCiF59F4.4. c. elegans.

Organism-specific databases

CTDi181671.
WormBaseiF59F4.4; CE11552; WBGene00010339; acl-1.

Phylogenomic databases

eggNOGiKOG2848. Eukaryota.
COG0204. LUCA.
GeneTreeiENSGT00390000008726.
HOGENOMiHOG000026375.
InParanoidiQ93841.
KOiK13509.
OMAiFQAMTWP.
OrthoDBiEOG780RNF.
PhylomeDBiQ93841.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00613.

Miscellaneous databases

PROiQ93841.

Family and domain databases

InterProiIPR004552. AGP_acyltrans.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiPLC1_CAEEL
AccessioniPrimary (citable) accession number: Q93841
Secondary accession number(s): Q93783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: July 6, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.