Q86VF5 · MOGT3_HUMAN
- Protein2-acylglycerol O-acyltransferase 3
- GeneMOGAT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids341 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Also able to catalyze the terminal step in triacylglycerol synthesis by using diacylglycerol and fatty acyl-CoA as substrates. Has a preference toward palmitoyl-CoA and oleoyl-CoA. May be involved in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705).
Catalytic activity
- a 2-acylglycerol + an acyl-CoA = a 1,2-diacylglycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + CoAThis reaction proceeds in the forward direction.
- all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecyl)-3-(9Z-octadecenoyl)-glycerol = 1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol + CoAThis reaction proceeds in the forward direction.
Kinetics
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
9.3 nmol/min/mg | with diacylglycerol as substrate | ||||
22.8 nmol/min/mg | with 2-monoacylglycerol as substrate |
Pathway
Glycerolipid metabolism; triacylglycerol biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | perinuclear endoplasmic reticulum membrane | |
Molecular Function | 2-acylglycerol O-acyltransferase activity | |
Molecular Function | diacylglycerol O-acyltransferase activity | |
Biological Process | glycerol metabolic process | |
Biological Process | monoacylglycerol biosynthetic process | |
Biological Process | triglyceride biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended name2-acylglycerol O-acyltransferase 3
- 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 accessionQ86VF5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 29-49 | Helical | ||||
Sequence: YVLTFLFMGPFFSLLVFVLLF | ||||||
Transmembrane | 50-70 | Helical | ||||
Sequence: TSLWPFSVFYLVWLYVDWDTP | ||||||
Transmembrane | 137-157 | Helical | ||||
Sequence: LFPGLRPWLAVLAGLFYLPVY |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 265 | Reduces 60% 2-acylglycerol O-acyltransferase activity. No effect on diacylglycerol O-acyltransferase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 265 | Catalitically inactive. No 2-acylglycerol O-acyltransferase neither diacylglycerol O-acyltransferase activities. | ||||
Sequence: C → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 473 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, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000249067 | 1-341 | 2-acylglycerol O-acyltransferase 3 | |||
Sequence: MGVATTLQPPTTSKTLQKQHLEAVGAYQYVLTFLFMGPFFSLLVFVLLFTSLWPFSVFYLVWLYVDWDTPNQGGRRSEWIRNRAIWRQLRDYYPVKLVKTAELPPDRNYVLGAHPHGIMCTGFLCNFSTESNGFSQLFPGLRPWLAVLAGLFYLPVYRDYIMSFGLCPVSRQSLDFILSQPQLGQAVVIMVGGAHEALYSVPGEHCLTLQKRKGFVRLALRHGASLVPVYSFGENDIFRLKAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLLPFAVPITTVVGRPIPVPQRLHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI | ||||||
Glycosylation | 126 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Ubiquitinated. Ubiquitination leads to proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Selectively expressed in the digestive system. Highly expressed in the ileum, and at lower level in jejunum, duodenum, colon, cecum and the rectum. Not expressed in the stomach and the esophagus and trachea. Expressed at very low level in liver.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86VF5-3 | CTSD P07339 | 3 | EBI-25840143, EBI-2115097 | |
BINARY | Q86VF5-3 | DMWD G5E9A7 | 3 | EBI-25840143, EBI-10976677 | |
BINARY | Q86VF5-3 | GRN P28799 | 3 | EBI-25840143, EBI-747754 | |
BINARY | Q86VF5-3 | SPRED1 Q7Z699 | 3 | EBI-25840143, EBI-5235340 | |
BINARY | Q86VF5-3 | WFS1 O76024 | 3 | EBI-25840143, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q86VF5-1
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
- Length341
- Mass (Da)38,730
- Last updated2003-06-01 v1
- Checksum3F4981AE0D05B613
Q86VF5-2
- Name2
Q86VF5-3
- Name3
- Differences from canonical
- 291-341: VGRPIPVPQRLHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI → GECPPPGGRPPAAAWASGIPRPPVSLSLQWAAPSPSPSASTPPRRKSITITPST
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_020361 | 224-281 | in isoform 2 | |||
Sequence: ASLVPVYSFGENDIFRLKAFATGSWQHWCQLTFKKLMGFSPCIFWGRGLFSATSWGLL → GPPHPRPPAPPPHRGGSQSLSRPLHDGPGAALRGAQGKLWGPRFHLPHLHLGLAAAFR | ||||||
Sequence conflict | 265 | in Ref. 4; AAI00954 | ||||
Sequence: C → Y | ||||||
Alternative sequence | VSP_020362 | 282-341 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_020363 | 291-341 | in isoform 3 | |||
Sequence: VGRPIPVPQRLHPTEEEVNHYHALYMTALEQLFEEHKESCGVPASTCLTFI → GECPPPGGRPPAAAWASGIPRPPVSLSLQWAAPSPSPSASTPPRRKSITITPST |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY229854 EMBL· GenBank· DDBJ | AAO63579.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358200 EMBL· GenBank· DDBJ | AAQ88567.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004876 EMBL· GenBank· DDBJ | AAD45832.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC100953 EMBL· GenBank· DDBJ | AAI00954.1 EMBL· GenBank· DDBJ | mRNA | ||
BC100954 EMBL· GenBank· DDBJ | AAI00955.1 EMBL· GenBank· DDBJ | mRNA | ||
BC100955 EMBL· GenBank· DDBJ | AAI00956.1 EMBL· GenBank· DDBJ | mRNA |