Q5GJ77 · GPAT1_BOVIN
- ProteinGlycerol-3-phosphate acyltransferase 1, mitochondrial
- GeneGPAM
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids825 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipids biosynthesis such as triglycerides, phosphatidic acids and lysophosphatidic acids.
Catalytic activity
- an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z,12Z)-octadecadienoyl-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.
- octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-glycerol 3-phosphate + CoAThis reaction proceeds in the forward direction.
- 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + 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 | mitochondrial membrane | |
Cellular Component | mitochondrial outer membrane | |
Cellular Component | plasma membrane | |
Molecular Function | glycerol-3-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 | diacylglycerol biosynthetic process | |
Biological Process | fatty acid metabolic process | |
Biological Process | glycerol-3-phosphate metabolic process | |
Biological Process | phosphatidic acid biosynthetic process | |
Biological Process | phosphatidylglycerol biosynthetic process | |
Biological Process | phospholipid biosynthetic process | |
Biological Process | triglyceride biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol-3-phosphate acyltransferase 1, mitochondrial
- EC number
- Short namesGPAT-1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ5GJ77
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | ?-470 | Mitochondrial intermembrane | ||||
Sequence: MDESALTLGTIDVSYLPNSSEYSIGRCKHATEEWGECGSRPTVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAGELNPDGSAQQQSKAVNKVKKKARKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKISCARAGLLSVVVDTLSTNTIPDILIIPGGISYDRIIEGHYNGEQLGKPKKNESLWSIARGVIRMLRKNYGCVKTDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSGAADEGTDMSINESRNATDESRRRLIAHLAEH | ||||||
Transmembrane | 471-493 | Helical | ||||
Sequence: ILFTASKSCAIMSTHIVACLLLY | ||||||
Topological domain | 494-573 | Cytoplasmic | ||||
Sequence: RHRQGIGLFTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQFLGNCITITHTSKNDEFFITPSTTIPSVFELNFYSN | ||||||
Transmembrane | 574-592 | Helical | ||||
Sequence: GVLHVFIMEAIIACSLYAV | ||||||
Topological domain | 593-825 | Mitochondrial intermembrane | ||||
Sequence: LKKRGPGGPASPSLVSQEQLVHKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILIVAEQDDQEDISPGLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAVFIHNFGGPVPEPEFLQKLHKYLITRTERRVAVYAESATYCLVKNAVKTFKDIGVFKETKQKRVSGLELSNTFLPQCNRQKLLEYILSLVVL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, transit peptide, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000245029 | ?-825 | Glycerol-3-phosphate acyltransferase 1, mitochondrial | |||
Sequence: MDESALTLGTIDVSYLPNSSEYSIGRCKHATEEWGECGSRPTVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAGELNPDGSAQQQSKAVNKVKKKARKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKISCARAGLLSVVVDTLSTNTIPDILIIPGGISYDRIIEGHYNGEQLGKPKKNESLWSIARGVIRMLRKNYGCVKTDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSGAADEGTDMSINESRNATDESRRRLIAHLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIGLFTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQFLGNCITITHTSKNDEFFITPSTTIPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGPGGPASPSLVSQEQLVHKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILIVAEQDDQEDISPGLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAVFIHNFGGPVPEPEFLQKLHKYLITRTERRVAVYAESATYCLVKNAVKTFKDIGVFKETKQKRVSGLELSNTFLPQCNRQKLLEYILSLVVL | ||||||
Transit peptide | 1-? | Mitochondrion | ||||
Modified residue | 380 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 685 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 692 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 777 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 781 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Highly expressed in adipose tissues and lung. Low expression in liver.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 230-235 | HXXXXD motif | ||||
Sequence: HRSHID | ||||||
Region | 435-455 | Disordered | ||||
Sequence: SRPSGAADEGTDMSINESRNA |
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
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length825
- Mass (Da)93,144
- Last updated2005-03-01 v1
- Checksum01D294B9DE03CC04
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY515690 EMBL· GenBank· DDBJ | AAS79429.1 EMBL· GenBank· DDBJ | mRNA | ||
AY945228 EMBL· GenBank· DDBJ | AAY24765.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY945226 EMBL· GenBank· DDBJ | AAY24765.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY945227 EMBL· GenBank· DDBJ | AAY24765.1 EMBL· GenBank· DDBJ | Genomic DNA |