FUT3
3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
Also known as: CD174, FUT3_HUMAN, LE
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P21217
- Gene
- FUT3
- Ensembl
- ENSG00000171124
- Chromosome
- 19
- Canonical length
- 361 aa
- Protein class
- Blood group antigen proteins, Enzymes, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins
OverviewNCBI Gene
The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Differences in the expression of this gene are associated with host susceptibility to viral infection. [provided by RefSeq, Aug 2020]
Canonical amino-acid sequenceUniProt
361 residues, UniProt reviewed canonical sequence.
>P21217|FUT3
1 MDPLGAAKPQ WPWRRCLAAL LFQLLVAVCF FSYLRVSRDD ATGSPRAPSG SSRQDTTPTR
61 PTLLILLRTW PFHIPVALSR CSEMVPGTAD CHITADRKVY PQADMVIVHH WDIMSNPKSR
121 LPPSPRPQGQ RWIWFNLEPP PNCQHLEALD RYFNLTMSYR SDSDIFTPYG WLEPWSGQPA
181 HPPLNLSAKT ELVAWAVSNW KPDSARVRYY QSLQAHLKVD VYGRSHKPLP KGTMMETLSR
241 YKFYLAFENS LHPDYITEKL WRNALEAWAV PVVLGPSRSN YERFLPPDAF IHVDDFQSPK
301 DLARYLQELD KDHARYLSYF RWRETLRPRS FSWALDFCKA CWKLQQESRY QTVRSIAAWF
361 TLocalizationUniProt · AlphaFold · HPA
Whether an antibody against FUT3 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)
- 0.32
- Highest tissue expression
- 151 nTPM
Expression across tissuesHPA
Tissue
- esophagus: 151 nTPM
- salivary gland: 79 nTPM
- retina: 76 nTPM
- colon: 68 nTPM
- small intestine: 53 nTPM
- vagina: 52 nTPM
Single-cell type
- esophageal apical cells: 1,029 nCPM
- colonocytes: 145 nCPM
- tuft cells: 138 nCPM
- esophageal suprabasal cells: 119 nCPM
- goblet cells: 113 nCPM
- enterocytes: 102 nCPM
Immune cell
- plasmacytoid DC: 0.2 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
Brain region
- hypothalamus: 3.9 nTPM
- cerebral cortex: 3.1 nTPM
- medulla oblongata: 2.9 nTPM
- pons: 2.7 nTPM
- white matter: 2.6 nTPM
- thalamus: 2.4 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)
- 1.95
- gnomAD pLI
- 0
- gnomAD missense Z
- -0.26
- DepMap mean gene effect
- 0.06
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell-cell recognition
- ceramide metabolic process
- oligosaccharide biosynthetic process
- oligosaccharide metabolic process
- positive regulation of cell-cell adhesion
- protein N-linked glycosylation
- protein O-linked glycosylation
- regulation of cell migration
- regulation of cell population proliferation
- carbohydrate derivative biosynthetic process
- Lewis a epitope biosynthetic process
Molecular functions
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity
- alpha-(1->3)-fucosyltransferase activity
- fucosyltransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of FUT3 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads FUT3 as an antibody target. Whether an autoantibody or antibody against FUT3 could matter depends on whether native FUT3 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
FUT3 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 FUT3 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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