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Q9VYV5 (FUT8_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-(1,6)-fucosyltransferase

Short name=Alpha1-6FucT
EC=2.4.1.68
Alternative name(s):
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
GDP-fucose--glycoprotein fucosyltransferase
Glycoprotein 6-alpha-L-fucosyltransferase
Gene names
Name:FucT6
ORF Names:CG2448
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. UniProtKB Q9BYC5

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 apparatusGolgi 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 GT23 domain.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG3916Q9VGB81EBI-172309,EBI-147840
Ipk2Q9VPR61EBI-172309,EBI-83394

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Alpha-(1,6)-fucosyltransferase
PRO_0000080530

Regions

Topological domain1 – 1717Cytoplasmic Potential
Transmembrane18 – 3821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain39 – 619581Lumenal Potential
Domain255 – 539285GT23
Domain548 – 60962SH3 UniProtKB Q9BYC5
Region411 – 4122Important for donor substrate binding By similarity
Motif345 – 3517SH3-binding Potential UniProtKB Q9BYC5

Amino acid modifications

Disulfide bond253 ↔ 315 By similarity
Disulfide bond261 ↔ 279 By similarity
Disulfide bond267 ↔ 271 By similarity
Disulfide bond511 ↔ 518 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VYV5 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 691BFD9B5C6557DE

FASTA61970,206
        10         20         30         40         50         60 
MLLVRQLFGA SANSWARALI IFVLAWIGLV YVFVVKLTNT QGQQAAGESE LNARRISQAL 

        70         80         90        100        110        120 
QMLEHTRQRN EELKQLIDEL MSDQLDKQSA MKLVQRLEND ALNPKLAPEV AGPEPESMFE 

       130        140        150        160        170        180 
SAPADLRGWN NVAEGAPNDL EAGVPDHGEF EPSLEYEFTR RRIQTNIGEI WNFFSSELGK 

       190        200        210        220        230        240 
VRKAVAAGHA SADLEESINQ VLLQGAEHKR SLLSDMERMR QSDGYEAWRH KEARDLSDLV 

       250        260        270        280        290        300 
QRRLHHLQNP SDCQNARKLV CKLNKGCGYG CQLHHVVYCF IVAYATERTL ILKSRGWRYH 

       310        320        330        340        350        360 
KGGWEEVFQP VSNSCHDAGT ANTYNWPGKP NTQVLVLPII DSLMPRPPYL PLAVPEDLAP 

       370        380        390        400        410        420 
RLKRLHGDPI VWWVGQFLKY LLRPQPTTRD FLTSGMRNLG WERPIVGVHV RRTDKVGTEA 

       430        440        450        460        470        480 
ACHSVEEYMT YVEDYYRTLE VNGSTVARRI FLASDDAQVI EEARRKYPQY QIIGDPEVAR 

       490        500        510        520        530        540 
MASVSTRYTD TALNGIILDI HLLSMSDHLV CTFSSQVCRV AYEIMQTMYP DAAHRFKSLD 

       550        560        570        580        590        600 
DIYYYGGQNA HNRRVVIAHK PRTHEDLQLR VGDLVSVAGN HWDGNSKGKN TRTNQGGLFP 

       610 
SFKVEEKVDT AKLPLYAGI 

« Hide

References

« Hide 'large scale' references
[1]"Core a3- and a6-fucosyltransferases in Drosophila: characterization and origin of diversity."
Petit D., Picaud F., Dupuy F., Germot A., Julien R., Maftah A.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.
[5]"Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism."
Roos C., Kolmer M., Mattila P., Renkonen R.
J. Biol. Chem. 277:3168-3175(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF441264 mRNA. Translation: AAN63649.1.
AE014298 Genomic DNA. Translation: AAF48079.1.
AY051451 mRNA. Translation: AAK92875.1.
RefSeqNP_572740.1. NM_132512.4.
UniGeneDm.4605.

3D structure databases

ProteinModelPortalQ9VYV5.
SMRQ9VYV5. Positions 155-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58529. 3 interactions.
DIPDIP-21409N.
IntActQ9VYV5. 2 interactions.
MINTMINT-900962.
STRING7227.FBpp0073457.

Protein family/group databases

CAZyGT23. Glycosyltransferase Family 23.

Proteomic databases

PaxDbQ9VYV5.
PRIDEQ9VYV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073620; FBpp0073457; FBgn0030327.
GeneID32122.
KEGGdme:Dmel_CG2448.

Organism-specific databases

CTD32122.
FlyBaseFBgn0030327. FucT6.

Phylogenomic databases

eggNOGNOG251249.
GeneTreeENSGT00530000063737.
InParanoidQ9VYV5.
KOK00717.
OMADPIVWWV.
OrthoDBEOG7N37C3.
PhylomeDBQ9VYV5.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ9VYV5.

Family and domain databases

InterProIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PIRSFPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51659. GT23. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFucT6. drosophila.
GenomeRNAi32122.
NextBio776952.
PROQ9VYV5.

Entry information

Entry nameFUT8_DROME
AccessionPrimary (citable) accession number: Q9VYV5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase