P32784 · GPT1_YEAST
- ProteinGlycerol-3-phosphate O-acyltransferase 1
- GeneSCT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids759 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Prefers Gly-3-P over dihydroxyacetone phosphate and has a marked preference for 16-carbon fatty acyl chains. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology (PubMed:11544256).
SCT1 is the primary supplier of diacylglycerols (DAG), used mainly in TAG synthesis and phosphatidylcholine (PC) synthesis through the CDP-choline pathway (PubMed:12167660).
Regulates fatty acid desaturation, that is, the ratio of unsaturated versus saturated fatty acyl chains, by competing with the desaturase OLE1 for the common substrate C16:0-CoA. Sequesters C16:0-CoA into lipids, thereby shielding it from desaturation by OLE1 (PubMed:22323296).
SCT1 is the primary supplier of diacylglycerols (DAG), used mainly in TAG synthesis and phosphatidylcholine (PC) synthesis through the CDP-choline pathway (PubMed:12167660).
Regulates fatty acid desaturation, that is, the ratio of unsaturated versus saturated fatty acyl chains, by competing with the desaturase OLE1 for the common substrate C16:0-CoA. Sequesters C16:0-CoA into lipids, thereby shielding it from desaturation by OLE1 (PubMed:22323296).
Miscellaneous
Present with 1050 molecules/cell in log phase SD medium.
Catalytic activity
- an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoA
- hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (9Z)-hexadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-hexadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
Pathway
Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | glycerol-3-phosphate O-acyltransferase activity | |
Molecular Function | glycerone-phosphate O-acyltransferase activity | |
Molecular Function | sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | phospholipid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameGlycerol-3-phosphate O-acyltransferase 1
- EC number
- Short namesG-3-P acyltransferase 1; GPAT 1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32784
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Localizes to both perinuclear and cortical endoplasmic reticulum.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-48 | Lumenal | ||||
Sequence: MPAPKLTEKFASSKSTQKTTNYSSIEAKSVKTSADQAYIYQEPSATKK | ||||||
Transmembrane | 49-69 | Helical | ||||
Sequence: ILYSIATWLLYNIFHCFFREI | ||||||
Topological domain | 70-434 | Cytoplasmic | ||||
Sequence: RGRGSFKVPQQGPVIFVAAPHANQFVDPVILMGEVKKSVNRRVSFLIAESSLKQPPIGFLASFFMAIGVVRPQDNLKPAEGTIRVDPTDYKRVIGHDTHFLTDCMPKGLIGLPKSMGFGEIQSIESDTSLTLRKEFKMAKPEIKTALLTGTTYKYAAKVDQSCVYHRVFEHLAHNNCIGIFPEGGSHDRTNLLPLKAGVAIMALGCMDKHPDVNVKIVPCGMNYFHPHKFRSRAVVEFGDPIEIPKELVAKYHNPETNRDAVKELLDTISKGLQSVTVTCSDYETLMVVQTIRRLYMTQFSTKLPLPLIVEMNRRMVKGYEFYRNDPKIADLTKDIMAYNAALRHYNLPDHLVEEAKVNFAKNLG | ||||||
Transmembrane | 435-449 | Helical | ||||
Sequence: LVFFRSIGLCILFSL | ||||||
Topological domain | 450 | Lumenal | ||||
Sequence: A | ||||||
Transmembrane | 451-465 | Helical | ||||
Sequence: MPGIIMFSPVFILAK | ||||||
Topological domain | 466-493 | Cytoplasmic | ||||
Sequence: RISQEKARTALSKSTVKIKANDVIATWK | ||||||
Transmembrane | 494-514 | Helical | ||||
Sequence: ILIGMGFAPLLYIFWSVLITY | ||||||
Topological domain | 515-523 | Lumenal | ||||
Sequence: YLRHKPWNK | ||||||
Transmembrane | 524-544 | Helical | ||||
Sequence: IYVFSGSYISCVIVTYSALIV | ||||||
Topological domain | 545-759 | Cytoplasmic | ||||
Sequence: GDIGMDGFKSLRPLVLSLTSPKGLQKLQKDRRNLAERIIEVVNNFGSELFPDFDSAALREEFDVIDEEEEDRKTSELNRRKMLRKQKIKRQEKDSSSPIISQRDNHDAYEHHNQDSDGVSLVNSDNSLSNIPLFSSTFHRKSESSLASTSVAPSSSSEFEVENEILEEKNGLASKIAQAVLNKRIGENTAREEEEEEEEEEEEEEEEEEGKEGDA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000195257 | 1-759 | Glycerol-3-phosphate O-acyltransferase 1 | |||
Sequence: MPAPKLTEKFASSKSTQKTTNYSSIEAKSVKTSADQAYIYQEPSATKKILYSIATWLLYNIFHCFFREIRGRGSFKVPQQGPVIFVAAPHANQFVDPVILMGEVKKSVNRRVSFLIAESSLKQPPIGFLASFFMAIGVVRPQDNLKPAEGTIRVDPTDYKRVIGHDTHFLTDCMPKGLIGLPKSMGFGEIQSIESDTSLTLRKEFKMAKPEIKTALLTGTTYKYAAKVDQSCVYHRVFEHLAHNNCIGIFPEGGSHDRTNLLPLKAGVAIMALGCMDKHPDVNVKIVPCGMNYFHPHKFRSRAVVEFGDPIEIPKELVAKYHNPETNRDAVKELLDTISKGLQSVTVTCSDYETLMVVQTIRRLYMTQFSTKLPLPLIVEMNRRMVKGYEFYRNDPKIADLTKDIMAYNAALRHYNLPDHLVEEAKVNFAKNLGLVFFRSIGLCILFSLAMPGIIMFSPVFILAKRISQEKARTALSKSTVKIKANDVIATWKILIGMGFAPLLYIFWSVLITYYLRHKPWNKIYVFSGSYISCVIVTYSALIVGDIGMDGFKSLRPLVLSLTSPKGLQKLQKDRRNLAERIIEVVNNFGSELFPDFDSAALREEFDVIDEEEEDRKTSELNRRKMLRKQKIKRQEKDSSSPIISQRDNHDAYEHHNQDSDGVSLVNSDNSLSNIPLFSSTFHRKSESSLASTSVAPSSSSEFEVENEILEEKNGLASKIAQAVLNKRIGENTAREEEEEEEEEEEEEEEEEEGKEGDA |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 414-419 | HXXXXD motif | ||||
Sequence: HYNLPD | ||||||
Region | 613-667 | Disordered | ||||
Sequence: EEDRKTSELNRRKMLRKQKIKRQEKDSSSPIISQRDNHDAYEHHNQDSDGVSLVN | ||||||
Compositional bias | 632-658 | Basic and acidic residues | ||||
Sequence: IKRQEKDSSSPIISQRDNHDAYEHHNQ | ||||||
Compositional bias | 684-704 | Polar residues | ||||
Sequence: RKSESSLASTSVAPSSSSEFE | ||||||
Region | 684-705 | Disordered | ||||
Sequence: RKSESSLASTSVAPSSSSEFEV | ||||||
Region | 729-759 | Disordered | ||||
Sequence: IGENTAREEEEEEEEEEEEEEEEEEGKEGDA | ||||||
Compositional bias | 735-759 | Acidic residues | ||||
Sequence: REEEEEEEEEEEEEEEEEEGKEGDA |
Domain
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence similarities
Belongs to the GPAT/DAPAT family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length759
- Mass (Da)85,694
- Last updated2004-08-31 v3
- ChecksumCCB0D11E8ED7D728
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10 | in Ref. 1; BAA07409 and 2; CAC85390 | ||||
Sequence: F → S | ||||||
Sequence conflict | 30-38 | in Ref. 2; CAC85390 | ||||
Sequence: Missing | ||||||
Sequence conflict | 88 | in Ref. 1; BAA07409 | ||||
Sequence: A → R | ||||||
Sequence conflict | 125 | in Ref. 1; BAA07409 | ||||
Sequence: P → A | ||||||
Sequence conflict | 278 | in Ref. 2; CAC85390 | ||||
Sequence: K → R | ||||||
Sequence conflict | 324 | in Ref. 2; CAC85390 | ||||
Sequence: P → S | ||||||
Sequence conflict | 574 | in Ref. 2; CAC85390 | ||||
Sequence: D → N | ||||||
Compositional bias | 632-658 | Basic and acidic residues | ||||
Sequence: IKRQEKDSSSPIISQRDNHDAYEHHNQ | ||||||
Compositional bias | 684-704 | Polar residues | ||||
Sequence: RKSESSLASTSVAPSSSSEFE | ||||||
Sequence conflict | 730 | in Ref. 1; BAA07409 | ||||
Sequence: G → S | ||||||
Compositional bias | 735-759 | Acidic residues | ||||
Sequence: REEEEEEEEEEEEEEEEEEGKEGDA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38256 EMBL· GenBank· DDBJ | BAA07409.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ314608 EMBL· GenBank· DDBJ | CAC85390.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35773 EMBL· GenBank· DDBJ | CAA84831.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S47695 EMBL· GenBank· DDBJ | AAB23987.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006936 EMBL· GenBank· DDBJ | DAA07108.1 EMBL· GenBank· DDBJ | Genomic DNA |