Reviewed, UniProtKB/Swiss-Prot Q9BYC5 (FUT8_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-(1,6)-fucosyltransferase
      Short name=alpha1-6FucT
    EC=2.4.1.68
Alternative name(s):
    Glycoprotein 6-alpha-L-fucosyltransferase
    GDP-fucose--glycoprotein fucosyltransferase
    GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
    Fucosyltransferase 8

Gene names

Name:

FUT8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. Ref.1
Catalytic activity	GDP-beta-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein By similarity. Note: Membrane-bound form in trans cisternae of Golgi By similarity.
Sequence similarities	Belongs to the glycosyltransferase 23 family. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	SH3 domain SH3-binding Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	L-fucose catabolic process Non-traceable author statement. Source: UniProtKB N-glycan processing Traceable author statement. Source: UniProtKB in utero embryonic development Non-traceable author statement. Source: UniProtKB oligosaccharide biosynthetic process Ref.1 Traceable author statement. Source: ProtInc protein amino acid glycosylation in Golgi Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW glycoprotein 6-alpha-L-fucosyltransferase activity Ref.1 Traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BYC5-1)

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.

Isoform 2 (identifier: Q9BYC5-2)

Also known as: Retinal;

The sequence of this isoform differs from the canonical sequence as follows:
     280-329: EVKDKNVQVV...HGDPAVWWVS → TPIMNLLVITLFPGQLDCTIDTQKIHFVE
     330-575: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 575

575

Alpha-(1,6)-fucosyltransferase

PRO_0000080526

Regions

Topological domain

1 – 9

9

Cytoplasmic Potential

Transmembrane

10 – 30

21

Signal-anchor for type II membrane protein Potential

Topological domain

31 – 575

545

Lumenal Potential

Domain

502 – 563

62

SH3

Region

365 – 366

2

Important for donor substrate binding

Motif

299 – 305

7

SH3-binding Potential

Natural variations

Alternative sequence

280 – 329

50

EVKDK…VWWVS → TPIMNLLVITLFPGQLDCTI DTQKIHFVE in isoform 2.

VSP_001807

Alternative sequence

330 – 575

246

Missing in isoform 2.

VSP_001808

Natural variant

101

1

K → Q: dbSNP rs2229678.

VAR_054038

Natural variant

267

1

T → K: dbSNP rs35949016.

VAR_033537

Experimental info

Mutagenesis

365

1

R → A or K: Complete loss of activity. Ref.4

Mutagenesis

366

1

R → A or K: Decreases activity to 3%. Ref.4

Secondary structure

1

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575

Helix Strand Turn

Details...

Helix

110 – 138

29

Helix

142 – 172

31

Turn

173 – 175

3

Helix

176 – 199

24

Helix

204 – 206

3

Beta strand

209 – 213

5

Helix

220 – 236

17

Beta strand

240 – 244

5

Helix

255 – 257

3

Helix

282 – 285

4

Beta strand

287 – 291

5

Helix

294 – 296

3

Helix

310 – 312

3

Helix

313 – 319

7

Helix

323 – 335

13

Helix

340 – 353

14

Beta strand

357 – 364

8

Helix

379 – 394

16

Beta strand

403 – 409

7

Helix

411 – 420

10

Beta strand

424 – 427

4

Helix

437 – 441

5

Helix

446 – 459

14

Beta strand

460 – 465

6

Helix

470 – 479

10

Beta strand

482 – 484

3

Beta strand

490 – 494

5

Beta strand

506 – 509

4

Beta strand

528 – 534

7

Beta strand

536 – 544

9

Turn

545 – 547

3

Beta strand

550 – 554

5

Helix

555 – 557

3

Beta strand

558 – 560

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 5, 2002. Version 2. Checksum: 5AE24A93881E18D0	FASTA	575	66,516
	10 20 30 40 50 60 MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL 70 80 90 100 110 120 RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE 130 140 150 160 170 180 NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR 190 200 210 220 230 240 EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT 250 260 270 280 290 300 LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR 310 320 330 340 350 360 PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI 370 380 390 400 410 420 GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PSLLKEAKTK 430 440 450 460 470 480 YPNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ 490 500 510 520 530 540 TLHPDASANF HSLDDIYYFG GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS 550 560 570 KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEAEK
	Isoform 2 (Retinal). Checksum: FB52A33CFD91A366	FASTA	308	35,795
	10 20 30 40 50 60 MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL 70 80 90 100 110 120 RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE 130 140 150 160 170 180 NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR 190 200 210 220 230 240 EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT 250 260 270 280 290 300 LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGT PIMNLLVITL FPGQLDCTID TQKIHFVE

References

[1]	"Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells." Yanagidani S., Uozumi N., Ihara Y., Miyoshi E., Yamaguchi N., Taniguchi N. J. Biochem. 121:626-632(1997) [PubMed: 9133635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]	"Differential splice variants of human FUT8 embryonic cDNA." Cailleau A., Balanzino L., Candelier J.J., Oriol R., Mollicone R. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1). Tissue: Embryo.
[3]	"Genomic structure and promoter analysis of the human alpha1,6-fucosyltransferase gene (FUT8)." Yamaguchi Y., Ikeda Y., Takahashi T., Ihara H., Tanaka T., Sasho C., Uozumi N., Yanagidani S., Inoue S., Fujii J., Taniguchi N. Glycobiology 10:637-643(2000) [PubMed: 10814706] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
[4]	"A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues." Takahashi T., Ikeda Y., Tateishi A., Yamaguchi Y., Ishikawa M., Taniguchi N. Glycobiology 10:503-510(2000) [PubMed: 10764839] [Abstract] Cited for: DONOR SUBSTRATE-BINDING, MUTAGENESIS OF ARG-365 AND ARG-366.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Fucosyltransferase 8

Cross-references

Sequence databases

EMBLGenBankDDBJ

D89289 mRNA. Translation: BAA19764.1.
AF038281, AF038280 Genomic DNA. Translation: AAB92372.2.
Y17979 mRNA. Translation: CAA76988.1.
Y17976 mRNA. Translation: CAA76985.1.
Y17977 mRNA. Translation: CAA76986.1.
Y17978 mRNA. Translation: CAA76987.1.
AB049828 Genomic DNA. Translation: BAB40975.1.
AB049740 mRNA. Translation: BAB40929.2.
AB032573 Genomic DNA. Translation: BAA92859.2.
AB032573 Genomic DNA. Translation: BAA92858.1.

IPI

IPI00004668.
IPI00215828.

PIR

JC5432.

RefSeq

NP_835367.1.
NP_835368.1.
NP_835369.1.

UniGene

Hs.654961

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DE0	X-ray	2.61	X	68-575	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT23. Glycosyltransferase Family 23.

Proteomic databases

PRIDE

Q9BYC5.

Genome annotation databases

Ensembl

ENSG00000033170. Homo sapiens. [Contig view]

GeneID

2530.

Organism-specific databases

GeneCards

GC14P064947.

H-InvDB

HIX0026626.

HGNC

HGNC:4019. FUT8.

HPA

CAB017129.

MIM

602589. gene.

PharmGKB

PA28435.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BYC5.

HOVERGEN

Q9BYC5.

OMA

Q9BYC5. LILESHN.

Enzyme and pathway databases

BRENDA

2.4.1.68. 247.

Gene expression databases

ArrayExpress

Q9BYC5.

Bgee

Q9BYC5.

CleanEx

HS_FUT8.

GermOnline

ENSG00000033170. Homo sapiens.

Family and domain databases

InterPro

IPR015827. Alpha1_6FUT_euk.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00018. SH3_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000472. Alpha1_6FUT_euk. 1 hit.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS50002. SH3. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

9971.

SOURCE

Search...

Entry information

Entry name

FUT8_HUMAN

Accession

Primary (citable) accession number: Q9BYC5
Secondary accession number(s): O00235 , Q9BYC6, Q9P2U5, Q9P2U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	March 5, 2002
Last modified:	June 16, 2009
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)