Q9NRZ7 · PLCC_HUMAN
- Protein1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- GeneAGPAT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids376 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (PubMed:21173190).
Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (PubMed:21173190).
Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190).
Has a preference for arachidonoyl-CoA as a donor (By similarity).
Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity).
Acts on LPA containing saturated or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using C18:1, C20:4 or C18:2-CoA as the acyl donor (PubMed:21173190).
Also acts on lysophosphatidylcholine, lysophosphatidylinositol and lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190).
Has a preference for arachidonoyl-CoA as a donor (By similarity).
Has also a modest lysophosphatidylinositol acyltransferase (LPIAT) activity, converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By similarity).
Catalytic activity
- a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + nonadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-nonadecanoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-icosatetraenoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) = 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-1D-myo-inositol + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-heptadecanoyl-sn-glycero-3-phosphate = 1-heptadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-(9Z-octadecenyl)-sn-glycero-3-phosphate = 1-O-(9Z-octadecenyl)-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoAThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
4.78 μM | LPA sn-1 C18:1 | |||||
21.53 μM | C18:1-CoA |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
6.35 nmol/min/mg | toward LPA sn-1 C18:1 | ||||
0.74 nmol/min/mg | toward C18:1-CoA |
Pathway
Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endomembrane system | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | membrane | |
Cellular Component | nuclear envelope | |
Cellular Component | plasma membrane | |
Molecular Function | 1-acylglycerol-3-phosphate O-acyltransferase activity | |
Biological Process | CDP-diacylglycerol biosynthetic process | |
Biological Process | phosphatidic acid biosynthetic process | |
Biological Process | phospholipid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended name1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NRZ7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-124 | Cytoplasmic | ||||
Sequence: MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKK | ||||||
Transmembrane | 125-145 | Helical | ||||
Sequence: ELLYVPLIGWTWYFLEIVFCK | ||||||
Topological domain | 146-316 | Lumenal | ||||
Sequence: RKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSLLGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWAT | ||||||
Transmembrane | 317-339 | Helical | ||||
Sequence: ILLSPLFSFVLGVFASGSPLLIL | ||||||
Topological domain | 340-376 | Cytoplasmic | ||||
Sequence: TFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 318 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000208194 | 1-376 | 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma | |||
Sequence: MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQLVMLLEWWSCTECTLFTDQATVERFGKEHAVIILNHNFEIDFLCGWTMCERFGVLGSSKVLAKKELLYVPLIGWTWYFLEIVFCKRKWEEDRDTVVEGLRRLSDYPEYMWFLLYCEGTRFTETKHRVSMEVAAAKGLPVLKYHLLPRTKGFTTAVKCLRGTVAAVYDVTLNFRGNKNPSLLGILYGKKYEADMCVRRFPLEDIPLDEKEAAQWLHKLYQEKDALQEIYNQKGMFPGEQFKPARRPWTLLNFLSWATILLSPLFSFVLGVFASGSPLLILTFLGFVGAASFGVRRLIGVTEIEKGSSYGNQEFKKKE |
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed with highest levels in testis, pancreas and kidney, followed by spleen, lung, adipose tissue and liver.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 96-101 | HXXXXD motif | ||||
Sequence: HNFEID |
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 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9NRZ7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsGamma-1
- Length376
- Mass (Da)43,381
- Last updated2000-10-01 v1
- ChecksumC12CDBB7CC363852
Q9NRZ7-2
- Name2
- SynonymsGamma-2
- Differences from canonical
- 1-62: Missing
Q9NRZ7-3
- Name3
- Differences from canonical
- 1-60: MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ → MQSGGSLPFCCYLPSVSSQLLLRESYCNFIKRTQCKSSKLMFSRDFLSGQKYCRCLLWALPDHPRRRGPTSANALPLSAE
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_013144 | 1-60 | in isoform 3 | |||
Sequence: MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCRLAYSLWSQ → MQSGGSLPFCCYLPSVSSQLLLRESYCNFIKRTQCKSSKLMFSRDFLSGQKYCRCLLWALPDHPRRRGPTSANALPLSAE | ||||||
Alternative sequence | VSP_005072 | 1-62 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 74 | in Ref. 7; CAD38635 | ||||
Sequence: T → P | ||||||
Sequence conflict | 358-376 | in Ref. 3; AAQ89067 | ||||
Sequence: VTEIEKGSSYGNQEFKKKE → ESLEPGRWRLQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF156774 EMBL· GenBank· DDBJ | AAF80336.1 EMBL· GenBank· DDBJ | mRNA | ||
AF156775 EMBL· GenBank· DDBJ | AAF80337.1 EMBL· GenBank· DDBJ | mRNA | ||
AB040138 EMBL· GenBank· DDBJ | BAB18943.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358704 EMBL· GenBank· DDBJ | AAQ89067.1 EMBL· GenBank· DDBJ | mRNA | ||
AP001054 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471079 EMBL· GenBank· DDBJ | EAX09461.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09463.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09464.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471079 EMBL· GenBank· DDBJ | EAX09465.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011971 EMBL· GenBank· DDBJ | AAH11971.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040603 EMBL· GenBank· DDBJ | AAH40603.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063552 EMBL· GenBank· DDBJ | AAH63552.1 EMBL· GenBank· DDBJ | mRNA | ||
AK125804 EMBL· GenBank· DDBJ | BAC86299.1 EMBL· GenBank· DDBJ | mRNA | ||
AL832919 EMBL· GenBank· DDBJ | CAD38635.2 EMBL· GenBank· DDBJ | mRNA |