Q922J9 · FACR1_MOUSE
- ProteinFatty acyl-CoA reductase 1
- GeneFar1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids515 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reduction of saturated and unsaturated C16 or C18 fatty acyl-CoA to fatty alcohols (PubMed:15220348, PubMed:15220349).
It plays an essential role in the production of ether lipids/plasmalogens which synthesis requires fatty alcohols (By similarity).
In parallel, it is also required for wax monoesters production since fatty alcohols also constitute a substrate for their synthesis (PubMed:15220349).
It plays an essential role in the production of ether lipids/plasmalogens which synthesis requires fatty alcohols (By similarity).
In parallel, it is also required for wax monoesters production since fatty alcohols also constitute a substrate for their synthesis (PubMed:15220349).
Catalytic activity
- a long-chain fatty acyl-CoA + 2 H+ + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP+This reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 2 H+ + 2 NADPH = (9Z)-octadecen-1-ol + CoA + 2 NADP+This reaction proceeds in the forward direction.
- (9Z,12Z)-octadecadienoyl-CoA + 2 H+ + 2 NADPH = (9Z,12Z)-octadecadien-1-ol + CoA + 2 NADP+This reaction proceeds in the forward direction.
pH Dependence
Optimum pH is 7.4.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisomal membrane | |
Cellular Component | peroxisome | |
Molecular Function | alcohol-forming long-chain fatty acyl-CoA reductase activity | |
Molecular Function | alcohol-forming very long-chain fatty acyl-CoA reductase activity | |
Biological Process | ether lipid biosynthetic process | |
Biological Process | glycerophospholipid biosynthetic process | |
Biological Process | long-chain fatty-acyl-CoA metabolic process | |
Biological Process | wax biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameFatty acyl-CoA reductase 1
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ922J9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Peroxisome membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-465 | Cytoplasmic | ||||
Sequence: MVSIPEYYEGKNILLTGATGFLGKVLLEKLLRSCPRVNSVYVLVRQKAGQTPQERVEEILSSKLFDRLRDENPDFREKIIAINSELTQPKLALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYIENYCMGTKKYVLNEEMSGLPAARKHLNKLRN | ||||||
Transmembrane | 466-483 | Helical | ||||
Sequence: IRYGFNTILVILIWRIFI | ||||||
Topological domain | 484-515 | Peroxisomal | ||||
Sequence: ARSQMARNIWYFVVSLCYKFLSYFRASSTMRY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000261395 | 1-515 | Fatty acyl-CoA reductase 1 | |||
Sequence: MVSIPEYYEGKNILLTGATGFLGKVLLEKLLRSCPRVNSVYVLVRQKAGQTPQERVEEILSSKLFDRLRDENPDFREKIIAINSELTQPKLALSEEDKEIIIDSTNVIFHCAATVRFNENLRDAVQLNVIATRQLILLAQQMKNLEVFMHVSTAYAYCNRKHIDEVVYPPPVDPKKLIDSLEWMDDGLVNDITPKLIGDRPNTYIYTKALAEYVVQQEGAKLNVAIVRPSIVGASWKEPFPGWIDNFNGPSGLFIAAGKGILRTMRASNNALADLVPVDVVVNTSLAAAWYSGVNRPRNIMVYNCTTGSTNPFHWGEVEYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAPAFLYDIYLRMTGRSPRMMKTITRLHKAMVFLEYFTSNSWVWNTDNVNMLMNQLNPEDKKTFNIDVRQLHWAEYIENYCMGTKKYVLNEEMSGLPAARKHLNKLRNIRYGFNTILVILIWRIFIARSQMARNIWYFVVSLCYKFLSYFRASSTMRY |
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Expressed in all tissues examined. Highest expression seen in preputial gland. Expressed in the brain where large quantities of ether lipids are synthesized.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 451-507 | Necessary and sufficient for PEX19-mediated localization into peroxisome membrane | ||||
Sequence: SGLPAARKHLNKLRNIRYGFNTILVILIWRIFIARSQMARNIWYFVVSLCYKFLSYF |
Sequence similarities
Belongs to the fatty acyl-CoA reductase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q922J9-1
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
- Length515
- Mass (Da)59,435
- Last updated2001-12-01 v1
- Checksum6A9E9EF9A2F835A4
Q922J9-2
- Name2
Q922J9-3
- Name3
- Differences from canonical
- 319-376: EYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAPAFLYDIYLRMTGRSPR → GDYLNHSFKMNPLNQVFRHPYVKFCSNNLMLHYWKGVKHTVPALLLDLALRLTGQKPW
Q922J9-4
- Name4
- Differences from canonical
- 515-515: Y → RRPRI
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 35 | in Ref. 1; BAB24102 | ||||
Sequence: P → R | ||||||
Alternative sequence | VSP_021678 | 242-260 | in isoform 2 | |||
Sequence: GWIDNFNGPSGLFIAAGKG → VSSSKLLSSWDSEFQVRTV | ||||||
Alternative sequence | VSP_021679 | 261-515 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_021680 | 319-376 | in isoform 3 | |||
Sequence: EYHVISTFKRNPLEQAFRRPNVNLTSNHLLYHYWIAVSHKAPAFLYDIYLRMTGRSPR → GDYLNHSFKMNPLNQVFRHPYVKFCSNNLMLHYWKGVKHTVPALLLDLALRLTGQKPW | ||||||
Sequence conflict | 364 | in Ref. 1; BAB24102 | ||||
Sequence: Y → H | ||||||
Alternative sequence | VSP_021681 | 515 | in isoform 4 | |||
Sequence: Y → RRPRI |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK005531 EMBL· GenBank· DDBJ | BAB24102.1 EMBL· GenBank· DDBJ | mRNA | ||
AK011187 EMBL· GenBank· DDBJ | BAB27453.1 EMBL· GenBank· DDBJ | mRNA | ||
AK014486 EMBL· GenBank· DDBJ | BAB29388.1 EMBL· GenBank· DDBJ | mRNA | ||
AK033674 EMBL· GenBank· DDBJ | BAC28423.1 EMBL· GenBank· DDBJ | mRNA | ||
AK030067 EMBL· GenBank· DDBJ | BAC26766.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007178 EMBL· GenBank· DDBJ | AAH07178.1 EMBL· GenBank· DDBJ | mRNA |