FMO5
Flavin-containing monooxygenase 5
Also known as: FMO5_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P49326
- Gene
- FMO5
- Ensembl
- ENSG00000131781
- Chromosome
- 1
- Canonical length
- 533 aa
- Protein class
- Cancer-related genes, Enzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Endoplasmic reticulum,Cytosol
OverviewNCBI Gene
Metabolic N-oxidation of the diet-derived amino-trimethylamine (TMA) is mediated by flavin-containing monooxygenase and is subject to an inherited FMO3 polymorphism in man resulting in a small subpopulation with reduced TMA N-oxidation capacity resulting in fish odor syndrome Trimethylaminuria. Three forms of the enzyme, FMO1 found in fetal liver, FMO2 found in adult liver, and FMO3 are encoded by genes clustered in the 1q23-q25 region. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2009]
Canonical amino-acid sequenceUniProt
533 residues, UniProt reviewed canonical sequence.
>P49326|FMO5
1 MTKKRIAVIG GGVSGLSSIK CCVEEGLEPV CFERTDDIGG LWRFQENPEE GRASIYKSVI
61 INTSKEMMCF SDYPIPDHYP NFMHNAQVLE YFRMYAKEFD LLKYIRFKTT VCSVKKQPDF
121 ATSGQWEVVT ESEGKKEMNV FDGVMVCTGH HTNAHLPLES FPGIEKFKGQ YFHSRDYKNP
181 EGFTGKRVII IGIGNSGGDL AVEISQTAKQ VFLSTRRGAW ILNRVGDYGY PADVLFSSRL
241 THFIWKICGQ SLANKYLEKK INQRFDHEMF GLKPKHRALS QHPTLNDDLP NRIISGLVKV
301 KGNVKEFTET AAIFEDGSRE DDIDAVIFAT GYSFDFPFLE DSVKVVKNKI SLYKKVFPPN
361 LERPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKTLP SQSEMMAEIS KAQEEIDKRY
421 VESQRHTIQG DYIDTMEELA DLVGVRPNLL SLAFTDPKLA LHLLLGPCTP IHYRVQGPGK
481 WDGARKAILT TDDRIRKPLM TRVVERSSSM TSTMTIGKFM LALAFFAIII AYFLocalizationUniProt · AlphaFold · HPA
Whether an antibody against FMO5 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)
- 0.23
- Highest tissue expression
- 639 nTPM
Expression across tissuesHPA
Tissue
- liver: 639 nTPM
- stomach: 117 nTPM
- small intestine: 70 nTPM
- duodenum: 67 nTPM
- parathyroid gland: 64 nTPM
- kidney: 48 nTPM
Single-cell type
- hepatocytes: 434 nCPM
- cardiomyocytes: 238 nCPM
- alveolar cells type 2: 234 nCPM
- cholangiocytes: 221 nCPM
- gastric chief cells: 214 nCPM
- enterocytes: 163 nCPM
Immune cell
- classical monocyte: 13 nTPM
- naive B-cell: 8.6 nTPM
- basophil: 7.1 nTPM
- intermediate monocyte: 5.9 nTPM
- myeloid DC: 5.4 nTPM
- memory B-cell: 4.8 nTPM
Brain region
- white matter: 15 nTPM
- pons: 13 nTPM
- medulla oblongata: 13 nTPM
- cerebellum: 11 nTPM
- spinal cord: 10 nTPM
- thalamus: 9.8 nTPM
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)
- 1.45
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.63
- DepMap mean gene effect
- 0.02
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
Molecular functions
- flavin adenine dinucleotide binding
- monooxygenase activity
- N,N-dimethylaniline monooxygenase activity
- NAD(P)H oxidase H2O2-forming activity
- NADP binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads FMO5 as an antibody target. Whether an autoantibody or antibody against FMO5 could matter depends on whether native FMO5 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
FMO5 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label FMO5 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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