Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9VYV5

- FUT8_DROME

UniProt

Q9VYV5 - FUT8_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-(1,6)-fucosyltransferase

Gene

FucT6

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  1. alpha-(1->6)-fucosyltransferase activity Source: FlyBase
  2. glycoprotein 6-alpha-L-fucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. fucosylation Source: GOC
  2. GDP-L-fucose metabolic process Source: UniProtKB
  3. N-glycan fucosylation Source: GOC
  4. protein glycosylation in Golgi Source: InterPro
  5. protein N-linked glycosylation via asparagine Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_180687. Reactions specific to the complex N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT23. Glycosyltransferase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-(1,6)-fucosyltransferase (EC:2.4.1.68)
Short name:
Alpha1-6FucT
Alternative name(s):
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
GDP-fucose--glycoprotein fucosyltransferase
Glycoprotein 6-alpha-L-fucosyltransferase
Gene namesi
Name:FucT6
ORF Names:CG2448
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0030327. FucT6.

Subcellular locationi

Golgi apparatusGolgi stack membrane By similarity; Single-pass type II membrane protein By similarity
Note: Membrane-bound form in trans cisternae of Golgi.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei18 – 3821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini39 – 619581LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: InterPro
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Alpha-(1,6)-fucosyltransferasePRO_0000080530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi253 ↔ 315By similarity
Disulfide bondi261 ↔ 279By similarity
Disulfide bondi267 ↔ 271By similarity
Disulfide bondi511 ↔ 518By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9VYV5.
PRIDEiQ9VYV5.

Expressioni

Gene expression databases

BgeeiQ9VYV5.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CG3916Q9VGB81EBI-172309,EBI-147840
Ipk2Q9VPR61EBI-172309,EBI-83394

Protein-protein interaction databases

BioGridi58529. 3 interactions.
DIPiDIP-21409N.
IntActiQ9VYV5. 2 interactions.
MINTiMINT-900962.
STRINGi7227.FBpp0073457.

Structurei

3D structure databases

ProteinModelPortaliQ9VYV5.
SMRiQ9VYV5. Positions 155-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 539285GT23PROSITE-ProRule annotationAdd
BLAST
Domaini548 – 60962SH3By similarityAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 4122Important for donor substrate bindingPROSITE-ProRule annotation

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi345 – 3517SH3-bindingSequence Analysis

Sequence similaritiesi

Belongs to the glycosyltransferase 23 family.PROSITE-ProRule annotation
Contains 1 GT23 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG251249.
GeneTreeiENSGT00530000063737.
InParanoidiQ9VYV5.
KOiK00717.
OMAiDPIVWWV.
OrthoDBiEOG7N37C3.
PhylomeDBiQ9VYV5.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51659. GT23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VYV5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLVRQLFGA SANSWARALI IFVLAWIGLV YVFVVKLTNT QGQQAAGESE
60 70 80 90 100
LNARRISQAL QMLEHTRQRN EELKQLIDEL MSDQLDKQSA MKLVQRLEND
110 120 130 140 150
ALNPKLAPEV AGPEPESMFE SAPADLRGWN NVAEGAPNDL EAGVPDHGEF
160 170 180 190 200
EPSLEYEFTR RRIQTNIGEI WNFFSSELGK VRKAVAAGHA SADLEESINQ
210 220 230 240 250
VLLQGAEHKR SLLSDMERMR QSDGYEAWRH KEARDLSDLV QRRLHHLQNP
260 270 280 290 300
SDCQNARKLV CKLNKGCGYG CQLHHVVYCF IVAYATERTL ILKSRGWRYH
310 320 330 340 350
KGGWEEVFQP VSNSCHDAGT ANTYNWPGKP NTQVLVLPII DSLMPRPPYL
360 370 380 390 400
PLAVPEDLAP RLKRLHGDPI VWWVGQFLKY LLRPQPTTRD FLTSGMRNLG
410 420 430 440 450
WERPIVGVHV RRTDKVGTEA ACHSVEEYMT YVEDYYRTLE VNGSTVARRI
460 470 480 490 500
FLASDDAQVI EEARRKYPQY QIIGDPEVAR MASVSTRYTD TALNGIILDI
510 520 530 540 550
HLLSMSDHLV CTFSSQVCRV AYEIMQTMYP DAAHRFKSLD DIYYYGGQNA
560 570 580 590 600
HNRRVVIAHK PRTHEDLQLR VGDLVSVAGN HWDGNSKGKN TRTNQGGLFP
610
SFKVEEKVDT AKLPLYAGI
Length:619
Mass (Da):70,206
Last modified:May 1, 2000 - v1
Checksum:i691BFD9B5C6557DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF441264 mRNA. Translation: AAN63649.1.
AE014298 Genomic DNA. Translation: AAF48079.1.
AY051451 mRNA. Translation: AAK92875.1.
RefSeqiNP_572740.1. NM_132512.4.
UniGeneiDm.4605.

Genome annotation databases

EnsemblMetazoaiFBtr0073620; FBpp0073457; FBgn0030327.
GeneIDi32122.
KEGGidme:Dmel_CG2448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF441264 mRNA. Translation: AAN63649.1 .
AE014298 Genomic DNA. Translation: AAF48079.1 .
AY051451 mRNA. Translation: AAK92875.1 .
RefSeqi NP_572740.1. NM_132512.4.
UniGenei Dm.4605.

3D structure databases

ProteinModelPortali Q9VYV5.
SMRi Q9VYV5. Positions 155-616.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58529. 3 interactions.
DIPi DIP-21409N.
IntActi Q9VYV5. 2 interactions.
MINTi MINT-900962.
STRINGi 7227.FBpp0073457.

Protein family/group databases

CAZyi GT23. Glycosyltransferase Family 23.

Proteomic databases

PaxDbi Q9VYV5.
PRIDEi Q9VYV5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0073620 ; FBpp0073457 ; FBgn0030327 .
GeneIDi 32122.
KEGGi dme:Dmel_CG2448.

Organism-specific databases

CTDi 32122.
FlyBasei FBgn0030327. FucT6.

Phylogenomic databases

eggNOGi NOG251249.
GeneTreei ENSGT00530000063737.
InParanoidi Q9VYV5.
KOi K00717.
OMAi DPIVWWV.
OrthoDBi EOG7N37C3.
PhylomeDBi Q9VYV5.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_180687. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

ChiTaRSi FucT6. fly.
GenomeRNAii 32122.
NextBioi 776952.
PROi Q9VYV5.

Gene expression databases

Bgeei Q9VYV5.

Family and domain databases

InterProi IPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view ]
PIRSFi PIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51659. GT23. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiFUT8_DROME
AccessioniPrimary (citable) accession number: Q9VYV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3