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
Mitochondrial membrane protein that catalyzes the essential first step of biosynthesis of glycerolipids such as triglycerides, phosphatidic acids and lysophosphatidic acids (By similarity).
Esterifies acyl-group from acyl-coenzyme A (acyl-CoA) to the sn-1 position of glycerol-3-phosphate, to produce lysophosphatidic acid (By similarity).
Has a narrow hydrophobic binding cleft that selects for a linear acyl chain (By similarity).
Catalytic activity is higher for substrates with a 16-carbon acyl chain (By similarity).
Esterifies acyl-group from acyl-coenzyme A (acyl-CoA) to the sn-1 position of glycerol-3-phosphate, to produce lysophosphatidic acid (By similarity).
Has a narrow hydrophobic binding cleft that selects for a linear acyl chain (By similarity).
Catalytic activity is higher for substrates with a 16-carbon acyl chain (By similarity).
Catalytic activity
- sn-glycerol 3-phosphate + an acyl-CoA = 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.
- sn-glycerol 3-phosphate + (9Z)-octadecenoyl-CoA = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- sn-glycerol 3-phosphate + octadecanoyl-CoA = 1-octadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- sn-glycerol 3-phosphate + hexadecanoyl-CoA = 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 = a 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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 278 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 279 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 288 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 293 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 328 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 461 | CoA (UniProtKB | ChEBI) | ||||
Sequence: R |
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 | |
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 ; Peripheral membrane protein
Note: Associated with the mitochondrion outer membrane of hepatic cells via a patch of basic residues.
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-87 | Cytoplasmic | ||||
Sequence: MDESALTLGTIDVSYLPNSSEYSIGRCKHATEEWGECGSRPTVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLG | ||||||
Intramembrane | 88-118 | |||||
Sequence: LRNVIYINETHTRHRGWLARRLSYVLFIQER | ||||||
Topological domain | 119-825 | Cytoplasmic | ||||
Sequence: DVHKGMFATNVTENVLNSSRVQEAIAEVAGELNPDGSAQQQSKAVNKVKKKARKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKISCARAGLLSVVVDTLSTNTIPDILIIPGGISYDRIIEGHYNGEQLGKPKKNESLWSIARGVIRMLRKNYGCVKTDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSGAADEGTDMSINESRNATDESRRRLIAHLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIGLFTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQFLGNCITITHTSKNDEFFITPSTTIPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGPGGPASPSLVSQEQLVHKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILIVAEQDDQEDISPGLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAVFIHNFGGPVPEPEFLQKLHKYLITRTERRVAVYAESATYCLVKNAVKTFKDIGVFKETKQKRVSGLELSNTFLPQCNRQKLLEYILSLVVL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000245029 | 1-825 | Glycerol-3-phosphate acyltransferase 1, mitochondrial | |||
Sequence: MDESALTLGTIDVSYLPNSSEYSIGRCKHATEEWGECGSRPTVFRSATLKWKESLMSRKRPFVGRCCYSCTPQSWDKFFNPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDVHKGMFATNVTENVLNSSRVQEAIAEVAGELNPDGSAQQQSKAVNKVKKKARKILQEMVATVSPAMIRLTGWVLLKLFNSFFWNIQIHKGQLEMVKAATETNLPLIFLPVHRSHIDYLLLTFILFCHNIKAPYIASGNNLNIPIFSTLIHKLGGFFIRRRLDETPDGRKDILYRALLHGHIVELLRQQQFLEIFLEGTRSRSGKISCARAGLLSVVVDTLSTNTIPDILIIPGGISYDRIIEGHYNGEQLGKPKKNESLWSIARGVIRMLRKNYGCVKTDFAQPFSLKEYLESQSQKPVSAPLSLEQALLPAILPSRPSGAADEGTDMSINESRNATDESRRRLIAHLAEHILFTASKSCAIMSTHIVACLLLYRHRQGIGLFTLVEDFFVMKEEVLARDFDLGFSGNSEDVVMHAIQFLGNCITITHTSKNDEFFITPSTTIPSVFELNFYSNGVLHVFIMEAIIACSLYAVLKKRGPGGPASPSLVSQEQLVHKAASLCYLLSNEGTISLPCQTFYQICHETVGRFIQYGILIVAEQDDQEDISPGLAEQQWDKKLPEPLSWRSDEEDEDSDFGEEQRDCYLKVSQSKEHQQFITFLQRLLGPLLEAYSSAAVFIHNFGGPVPEPEFLQKLHKYLITRTERRVAVYAESATYCLVKNAVKTFKDIGVFKETKQKRVSGLELSNTFLPQCNRQKLLEYILSLVVL | ||||||
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 region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 80-120 | Important for mitochondrial localization | ||||
Sequence: NPSIPSLGLRNVIYINETHTRHRGWLARRLSYVLFIQERDV | ||||||
Motif | 230-235 | HXXXXD motif | ||||
Sequence: HRSHID | ||||||
Region | 435-455 | Disordered | ||||
Sequence: SRPSGAADEGTDMSINESRNA |
Domain
The HXXXXD motif is essential for acyltransferase activity and contributes to the binding of the cysteamine moiety of the acyl-CoA and the phosphate moiety of the glycerol-3-phosphate.
Sequence similarities
Belongs to the GPAT/DAPAT family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- 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 |