A0A8P0PCS4 · A0A8P0PCS4_CANLF
- ProteinMultidrug and toxin extrusion protein
- GeneALDH3A2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1248 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
Catalytic activity
- (2E)-hexadecenal + H2O + NAD+ = (E)-hexadec-2-enoate + 2 H+ + NADH
- 2 H+ + hexadecanoate + NADH = H2O + hexadecanal + NAD+
- 2,6,10,14-tetramethylpentadecanal + H2O + NAD+ = 2,6,10,14-tetramethylpentadecanoate + 2 H+ + NADH
- 22-oxodocosanoate + H2O + NAD+ = docosanedioate + 2 H+ + NADH
- H2O + NAD+ + octadecanal = 2 H+ + NADH + octadecanoate
- H2O + NAD+ + octanal = 2 H+ + NADH + octanoate
- H2O + NAD+ + tetradecanal = 2 H+ + NADH + tetradecanoate
- H2O + heptanal + NAD+ = 2 H+ + heptanoate + NADH
- a fatty aldehyde + H2O + NAD+ = a fatty acid + 2 H+ + NADH
- decanal + H2O + NAD+ = decanoate + 2 H+ + NADH
- dodecanoate + 2 H+ + NADH = dodecanal + H2O + NAD+
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 970 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | antiporter activity | |
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | |
Molecular Function | xenobiotic transmembrane transporter activity | |
Biological Process | cellular aldehyde metabolic process | |
Biological Process | fatty acid metabolic process | |
Biological Process | xenobiotic detoxification by transmembrane export across the plasma membrane |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameMultidrug and toxin extrusion protein
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionA0A8P0PCS4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 290-311 | Helical | ||||
Sequence: FLAQLMIFLIGVVSSIFCGHLG | ||||||
Transmembrane | 317-339 | Helical | ||||
Sequence: AVTLAVSVVNVTGISVGTGLASA | ||||||
Transmembrane | 359-378 | Helical | ||||
Sequence: ILQRGILILMLCCFPCWAIF | ||||||
Transmembrane | 398-415 | Helical | ||||
Sequence: AQIYVMIFIPALPAAFLF | ||||||
Transmembrane | 427-453 | Helical | ||||
Sequence: IIMPQVITGIAANVINVGMNALLLYAL | ||||||
Transmembrane | 459-481 | Helical | ||||
Sequence: GSAWANTTSQFLLSALLFLYVWW | ||||||
Transmembrane | 541-562 | Helical | ||||
Sequence: IIYELASAAYMVPLGFGVAASV | ||||||
Transmembrane | 583-609 | Helical | ||||
Sequence: VLLCAGVCALVVGVLLAALKDVVAYIF | ||||||
Transmembrane | 653-674 | Helical | ||||
Sequence: AILNAIGYYVFGFPIGVSLMFA | ||||||
Transmembrane | 680-702 | Helical | ||||
Sequence: IGLWSGLIVCVFFQALFYLVLIW | ||||||
Transmembrane | 1227-1247 | Helical | ||||
Sequence: LSLLVLTFLGILAAVLVKVGY |
Keywords
- Cellular component
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-54 | Disordered | ||||
Sequence: MGDGDAEGLSLGPHCRPRSAPPPPPPASAGNTFCNTPVTRGRGSGHLKSQQRAP | ||||||
Compositional bias | 16-30 | Pro residues | ||||
Sequence: RPRSAPPPPPPASAG | ||||||
Compositional bias | 31-46 | Polar residues | ||||
Sequence: NTFCNTPVTRGRGSGH | ||||||
Region | 87-279 | Disordered | ||||
Sequence: TSHSLDRVRYPPPPPDCDPSPTTSSGVPRPAPNSWGSADGDGWQGASWVRRRDPPASPTSASSPPPPAAGGAGRVGRGGAGPGRPQLTAASRAQSPRRHGGPRRRSRRPRRPRRPGQHPVARRPPLARLPAGPAGRAAARRATRGGRAGGARGPRGECAAPRPRRPPPPPRPRAPAPPAPPRSRSLPGGRLGV | ||||||
Compositional bias | 183-204 | Basic residues | ||||
Sequence: RRHGGPRRRSRRPRRPRRPGQH | ||||||
Compositional bias | 246-270 | Pro residues | ||||
Sequence: APRPRRPPPPPRPRAPAPPAPPRSR | ||||||
Domain | 764-1184 | Aldehyde dehydrogenase | ||||
Sequence: MESRIQRVRAAFASGRSRPVRFRLQQLEALRRMVQEREKDILEAIAGDLCKSELNAYSQEVITVLGELDLVLENLPEWVAAKPAKKNLLTMLDEAYVQPEPLGVVLIIGAWNYPFVLTIQPLIGAIAAGNAVIIKPSELSEKTAKILAELLPRYLDQDLYVVINGGVEETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYVDKDCDLDIACRRITWGKYMNCGQTCIAPDYVLCEPSLQNQIVQKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKIAFGGETDEATRYIAPTILSDVDPESRVMQEEIFGPILPIVPVKNADEAIKFINSREKPLAFYIFSHNDKLVRQMINGTSSGGVTANDVIMHFTLSSLPFGGVGSSGMGAYHGKYSFDTFSH |
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,248
- Mass (Da)135,617
- Last updated2022-10-12 v1
- Checksum7BF14294A818093D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 16-30 | Pro residues | ||||
Sequence: RPRSAPPPPPPASAG | ||||||
Compositional bias | 31-46 | Polar residues | ||||
Sequence: NTFCNTPVTRGRGSGH | ||||||
Compositional bias | 183-204 | Basic residues | ||||
Sequence: RRHGGPRRRSRRPRRPRRPGQH | ||||||
Compositional bias | 246-270 | Pro residues | ||||
Sequence: APRPRRPPPPPRPRAPAPPAPPRSR |