FUT5 fucosyltransferase 5 [Homo sapiens (human)] - Gene

Summary

Official Symbol: FUT5provided by HGNC
Official Full Name: fucosyltransferase 5provided by HGNC
Primary source: HGNC:HGNC:4016
See related: Ensembl:ENSG00000130383 MIM:136835; AllianceGenome:HGNC:4016
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: FUC-TV
Summary: Enables 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity and 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity. Involved in ceramide metabolic process; oligosaccharide metabolic process; and protein glycosylation. Predicted to be located in Golgi membrane. [provided by Alliance of Genome Resources, Oct 2024]
Expression: Biased expression in colon (RPKM 6.2), esophagus (RPKM 5.3) and 8 other tissues See more
Orthologs: all
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Genomic context

Location:: 19p13.3

Exon count:: 2

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	19	NC_000019.10 (5865826..5870540, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	19	NC_060943.1 (5853268..5857965, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	19	NC_000019.9 (5865837..5870551, complement)

Chromosome 19 - NC_000019.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Overexpressed N-fucosylation on cell surface promotes the migration and invasion of metastatic pancreatic cancer cells. Overexpressed N-fucosylation is driven by gene FUT3, 5, and 6 in metastatic pancreatic cancer cells.
Title: Overexpressed N-fucosylation on the cell surface driven by FUT3, 5, and 6 promotes cell motilities in metastatic pancreatic cancer cell lines.
data suggest that both FUT5 and FUT6 can promote the development of colorectal cancer (CRC) via the PI3K/Akt signalling pathway, which is regulated by miR-125a-3p. miR-125a-3p may serve as a predictive biomarker and a potential therapeutic target in CRC treatment.
Title: miR-125a-3p/FUT5-FUT6 axis mediates colorectal cancer cell proliferation, migration, invasion and pathological angiogenesis via PI3K-Akt pathway.
FUT5 was expressed on spermatid membranes and in serum, but not in seminal plasma, vaginal fluid and saliva. Expression was localized on head of spermatids.
Title: [Distribution specificity of human fucosyltransferase 5 and its expression and localization in spermatids].
down-regulation of FUT3 and FUT5 reduces the expression of sialyl-Lewis antigens and the adhesion capacities of gastric cancer cells and allows to identify the specific alpha1-3,4 fucosyltransferases implicated in the Lewis antigens synthesis
Title: Down-regulation of FUT3 and FUT5 by shRNA alters Lewis antigens expression and reduces the adhesion capacities of gastric cancer cells.
Observational study of genotype prevalence. (HuGE Navigator)
Title: [The genetic diversity in the full coding region of human FUT5 gene in a Chinese Han population].
results suggested that PKR is the primary target for HSV-1 early RNA during induction of FUT3, FUT5, and FUT6
Title: Activation of host antiviral RNA-sensing factors necessary for herpes simplex virus type 1-activated transcription of host cell fucosyltransferase genes FUT3, FUT5, and FUT6 and subsequent expression of sLe(x) in virus-infected cells.
Prostatic cancer cell transfected with this enzyme adhered to prostatic stromal cells in vitro with higher affinity than mock-transfected cancer cells.
Title: Gene transfer of alpha1,3-fucosyltransferase increases tumor growth of the PC-3 human prostate cancer cell line through enhanced adhesion to prostatic stromal cells.
FUT5 is a receptor of glycodelin-A and zona pellucida proteins, and glycodelin-A inhibits spermatozoa-zona binding by blocking the binding of sperm FUT5 to the zona pellucida
Title: Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding.

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Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

General gene information

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Markers

RH79134 (e-PCR)
- UniSTS:67428

NoName (e-PCR)
- UniSTS:494522

NoName (e-PCR)
- UniSTS:481991

NoName (e-PCR)
- UniSTS:480725

NoName (e-PCR)
- UniSTS:489711

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables alpha-(1->3)-fucosyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables alpha-(1->3)-fucosyltransferase activity	TAS Traceable Author Statement more info	PubMed
enables fucosyltransferase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in L-fucose catabolic process	NAS Non-traceable Author Statement more info	PubMed
involved_in carbohydrate metabolic process	TAS Traceable Author Statement more info	PubMed
involved_in ceramide metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in fucosylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in oligosaccharide biosynthetic process	TAS Traceable Author Statement more info
involved_in oligosaccharide metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in protein N-linked glycosylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein O-linked glycosylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein glycosylation	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	TAS Traceable Author Statement more info	PubMed
located_in Golgi cisterna membrane	IEA Inferred from Electronic Annotation more info
located_in Golgi membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5

Names: 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5; alpha (1,3) fucosyltransferase; alpha-(1,3)-fucosyltransferase 5; fucT-V; fucosyltransferase V; galactoside 3-L-fucosyltransferase

NP_002025.2

EC 2.4.1.152

EC 2.4.1.65

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_002034.2 → NP_002025.2 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5

Status: VALIDATED

Source sequence(s)

AC024592

Consensus CDS

CCDS12154.1

UniProtKB/Swiss-Prot

A8K4X2, K7ENC0, Q11128

UniProtKB/TrEMBL

A0A9E8S311

Related

ENSP00000466880.1, ENST00000588525.1

Conserved Domains (2) summary

pfam00852
Location:202 → 370

Glyco_transf_10; Glycosyltransferase family 10 (fucosyltransferase) C-term

pfam17039
Location:73 → 183

Glyco_tran_10_N; Fucosyltransferase, N-terminal