Q41131 · FAH12_RICCO
- ProteinOleate hydroxylase FAH12
- GeneFAH12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids387 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Oleate hydroxylase involved in the biosynthesis of ricinoleate (PubMed:27056057, PubMed:7624314).
It uses cytochrome b5 as an electron donor (PubMed:1417766).
May act on both oleic acid (18:1(9cis)) and eicosenoic acid (20:1(11cis)) (PubMed:8784737).
It uses cytochrome b5 as an electron donor (PubMed:1417766).
May act on both oleic acid (18:1(9cis)) and eicosenoic acid (20:1(11cis)) (PubMed:8784737).
Catalytic activity
- a 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + 2 Fe(II)-[cytochrome b5] + O2 + 2 H+ = a 1-acyl-2-[(R)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + 2 Fe(III)-[cytochrome b5] + H2O
- (9Z)-octadecenoate + AH2 + O2 = (12R)-hydroxy-(9Z)-octadecenoate + A + H2O
Activity regulation
Inhibited by oleoyloxyethyl phosphocholine.
Biotechnology
Promotes the accumulation of hydroxy fatty acids when expressed in A.thaliana.
pH Dependence
Optimum pH is 6.3.
Temperature Dependence
Optimum temperature is 22.5 degrees Celsius.
Pathway
Lipid metabolism; monounsaturated fatty acid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | monooxygenase activity | |
Molecular Function | oxidoreductase activity | |
Molecular Function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water | |
Molecular Function | phosphatidylcholine 12-monooxygenase activity | |
Biological Process | fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOleate hydroxylase FAH12
- EC number
- Short namesRcFAH12
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Euphorbiaceae > Acalyphoideae > Acalypheae > Ricinus
Accessions
- Primary accessionQ41131
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Microsome membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 61-81 | Helical | ||||
Sequence: AYDVCLSFLFYSIATNFFPYI | ||||||
Transmembrane | 88-108 | Helical | ||||
Sequence: VAWLVYWLFQGCILTGLWVIG | ||||||
Transmembrane | 121-141 | Helical | ||||
Sequence: LADDIVGLIVHSALLVPYFSW | ||||||
Transmembrane | 183-203 | Helical | ||||
Sequence: VLTLAATLLLGWPLYLAFNVS | ||||||
Transmembrane | 229-249 | Helical | ||||
Sequence: IYIADLGIFATTFVLYQATMA | ||||||
Transmembrane | 253-273 | Helical | ||||
Sequence: AWVMRIYGVPLLIVNCFLVMI |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 49 | in OLE-1; enhanced accumulation of oleic acid but low ricinoleic acid levels in seeds, high-oleic castor mutant 1; when associated with A-242 and Q-319 | ||||
Sequence: F → S | ||||||
Mutagenesis | 49 | Strongly reduced ricinoleic acid accumulation; when associated with A-242. | ||||
Sequence: F → S | ||||||
Natural variant | 242 | in OLE-1; enhanced accumulation of oleic acid but low ricinoleic acid levels in seeds, high-oleic castor mutant 1; when associated with S-49 and Q-319 | ||||
Sequence: V → A | ||||||
Mutagenesis | 242 | Lower ricinoleic acid accumulation. Strongly reduced ricinoleic acid accumulation; when associated with S-49 or Q-319. | ||||
Sequence: V → A | ||||||
Natural variant | 319 | in OLE-1; enhanced accumulation of oleic acid but low ricinoleic acid levels in seeds, high-oleic castor mutant 1; when associated with S-49 and A-242 | ||||
Sequence: H → Q | ||||||
Mutagenesis | 319 | Strongly reduced ricinoleic acid accumulation; when associated with A-242. | ||||
Sequence: H → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000434633 | 1-387 | Oleate hydroxylase FAH12 | |||
Sequence: MGGGGRMSTVITSNNSEKKGGSSHLKRAPHTKPPFTLGDLKRAIPPHCFERSFVRSFSYVAYDVCLSFLFYSIATNFFPYISSPLSYVAWLVYWLFQGCILTGLWVIGHECGHHAFSEYQLADDIVGLIVHSALLVPYFSWKYSHRRHHSNIGSLERDEVFVPKSKSKISWYSKYLNNPPGRVLTLAATLLLGWPLYLAFNVSGRPYDRFACHYDPYGPIFSERERLQIYIADLGIFATTFVLYQATMAKGLAWVMRIYGVPLLIVNCFLVMITYLQHTHPAIPRYGSSEWDWLRGAMVTVDRDYGVLNKVFHNIADTHVAHHLFATVPHYHAMEATKAIKPIMGEYYRYDGTPFYKALWREAKECLFVEPDEGAPTQGVFWYRNKY |
Expression
Tissue specificity
Expressed in seeds. Barely detected in leaves.
Developmental stage
Accumulates progressively during seeds development.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MGGGGRMSTVITSNNSEKKGGSSHLKRAPHTKPP | ||||||
Motif | 109-113 | Histidine box-1 | ||||
Sequence: HECGH | ||||||
Motif | 145-149 | Histidine box-2 | ||||
Sequence: HRRHH | ||||||
Motif | 319-323 | Histidine box-3 | ||||
Sequence: HVAHH |
Domain
The histidine box domains may contain the active site and/or be involved in metal ion binding.
Sequence similarities
Belongs to the fatty acid desaturase type 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length387
- Mass (Da)44,435
- Last updated2018-02-28 v2
- Checksum85C582CC65FE37D9
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 176 | in Ref. 1; AAC49010 | ||||
Sequence: L → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U22378 EMBL· GenBank· DDBJ | AAC49010.1 EMBL· GenBank· DDBJ | mRNA | ||
EU523112 EMBL· GenBank· DDBJ | ACD39348.1 EMBL· GenBank· DDBJ | mRNA | ||
EQ974077 EMBL· GenBank· DDBJ | EEF34257.1 EMBL· GenBank· DDBJ | Genomic DNA |