Reviewed, UniProtKB/Swiss-Prot Q9VYV5 (FUT8_DROME)

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

Gene names

Name:	FucT6
ORF Names:	CG2448

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	619 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 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 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
Domain	SH3 domain Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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	glycoprotein 6-alpha-L-fucosyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VGB8	1	EBI-172309,EBI-147840
Ipk2	Q9VPR6	1	EBI-172309,EBI-83394

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 619	619	Alpha-(1,6)-fucosyltransferase		PRO_0000080530
Regions
	Topological domain	1 – 17	17	Cytoplasmic Potential
	Transmembrane	18 – 38	21	Signal-anchor for type II membrane protein Potential
	Topological domain	39 – 619	581	Lumenal Potential
	Domain	548 – 609	62	SH3 UniProtKB Q9BYC5
	Region	411 – 412	2	Important for donor substrate binding By similarity
	Motif	345 – 351	7	SH3-binding Potential UniProtKB Q9BYC5

Sequences

	Sequence		Length	Mass (Da)
	Q9VYV5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 691BFD9B5C6557DE	FASTA	619	70,206
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [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: 11698403] [Abstract] Cited for: HOMOLOGY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF441264 mRNA. Translation: AAN63649.1. AE014298 Genomic DNA. Translation: AAF48079.1. AY051451 mRNA. Translation: AAK92875.1.
RefSeq	NP_572740.1.
UniGene	Dm.4605
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:21409N.
IntAct	Q9VYV5. 3 interactions.
Protein family/group databases
CAZy	GT23. Glycosyltransferase Family 23.
Proteomic databases
PRIDE	Q9VYV5.
Genome annotation databases
Ensembl	FBgn0030327. Drosophila melanogaster. [Contig view]
GeneID	32122.
KEGG	dme:Dmel_CG2448.
NMPDR	fig|7227.3.peg.17473.
Organism-specific databases
FlyBase	FBgn0030327. FucT6.
Phylogenomic databases
HOGENOM	Q9VYV5.
OMA	Q9VYV5. LILESHN.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001531-MON.
BRENDA	2.4.1.68. 48.
Gene expression databases
ArrayExpress	Q9VYV5.
GermOnline	CG2448. Drosophila melanogaster.
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	776952.

Entry information

Entry name

FUT8_DROME

Accession

Primary (citable) accession number: Q9VYV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project