FAR1

Protein identityUniProt · HPA

UniProt accession

Q8WVX9

Gene

FAR1

Ensembl

ENSG00000197601

Chromosome

11

Canonical length

515 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins

Subcellular location

Peroxisomes

OverviewNCBI Gene

The protein encoded by this gene is required for the reduction of fatty acids to fatty alcohols, a process that is required for the synthesis of monoesters and ether lipids. NADPH is required as a cofactor in this reaction, and 16-18 carbon saturated and unsaturated fatty acids are the preferred substrate. This is a peroxisomal membrane protein, and studies suggest that the N-terminus contains a large catalytic domain located on the outside of the peroxisome, while the C-terminus is exposed to the matrix of the peroxisome. Studies indicate that the regulation of this protein is dependent on plasmalogen levels. Mutations in this gene have been associated with individuals affected by severe intellectual disability, early-onset epilepsy, microcephaly, congenital cataracts, growth retardation, and spasticity (PMID: 25439727). A pseudogene of this gene is located on chromosome 13. [provided by RefSeq, Jan 2015]

Canonical amino-acid sequenceUniProt

515 residues, UniProt reviewed canonical sequence.

>Q8WVX9|FAR1
     1  MVSIPEYYEG KNVLLTGATG FLGKVLLEKL LRSCPKVNSV YVLVRQKAGQ TPQERVEEVL
    61  SGKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEV IIDSTNIIFH CAATVRFNEN
   121  LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS
   181  LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF
   241  PGWIDNFNGP SGLFIAAGKG ILRTIRASNN ALADLVPVDV VVNMSLAAAW YSGVNRPRNI
   301  MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP
   361  AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTENVNMLM NQLNPEDKKT
   421  FNIDVRQLHW AEYIENYCLG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR
   481  IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against FAR1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Other membrane

Secreted

No

Transmembrane segments

1

Mean surface accessibility (rSASA)

0.24

Highest tissue expression

62 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about FAR1.

Disease | AllUniProt

Conditions FAR1 is implicated in, by any mechanism.

• Peroxisomal fatty acyl-CoA reductase 1 disorder (PFCRD) MIM:616154
• Cataracts, spastic paraparesis, and speech delay (CSPSD) MIM:619338

Disease | GeneticClinVar

16 pathogenic / likely-pathogenic of 430 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Fatty acyl-CoA reductase 1 deficiency
• Spastic paraparesis-cataracts-speech delay syndrome
• CATARACTS, SPASTIC PARAPLEGIA, AND SPEECH DELAY
• FAR1-related neurodevelopmental disorder

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.3

gnomAD pLI

0.99

gnomAD missense Z

3.3

DepMap mean gene effect

0.04

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• ether lipid biosynthetic process
• glycerophospholipid biosynthetic process
• long-chain fatty-acyl-CoA metabolic process
• wax biosynthetic process

Molecular functions

• alcohol-forming long-chain fatty acyl-CoA reductase activity
• alcohol-forming very long-chain fatty acyl-CoA reductase activity
• oxidoreductase activity

Cellular components

• peroxisomal membrane
• peroxisome

Protein domainsUniProt · Pfam · InterPro

• Fatty acyl-CoA reductase-like, NAD-binding domain
• Fatty acyl-CoA reductase
• Fatty acyl-CoA reductase, C-terminal
• NAD(P)-binding domain superfamily
• Male sterility protein
• Male sterility protein

KeywordsUniProt

• Cataract
• Epilepsy
• Intellectual disability
• Lipid biosynthesis
• Lipid metabolism
• Membrane
• NADP
• Oxidoreductase
• Peroxisome
• Transmembrane
• Transmembrane helix

InteractionsUniProt · HPA

Protein binding partners of FAR1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• PEX19