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Protein

Alpha-(1,6)-fucosyltransferase

Gene

Fut8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

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:Fut8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1303096. Fut8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence analysis
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini31 – 575545LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Alpha-(1,6)-fucosyltransferasePRO_0000357042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi204 ↔ 266By similarity
Disulfide bondi212 ↔ 230By similarity
Disulfide bondi218 ↔ 222By similarity
Modified residuei278 – 2781PhosphoserineBy similarity
Disulfide bondi465 ↔ 472By similarity

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ6EV76.
PRIDEiQ6EV76.

PTM databases

PhosphoSiteiQ6EV76.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011220.

Structurei

3D structure databases

ProteinModelPortaliQ6EV76.
SMRiQ6EV76. Positions 108-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 493288GT23PROSITE-ProRule annotationAdd
BLAST
Domaini502 – 56362SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni365 – 3662Important for donor substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi299 – 3057SH3-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, SH3-binding, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3705. Eukaryota.
ENOG410YHM8. LUCA.
HOGENOMiHOG000007175.
HOVERGENiHBG028260.
InParanoidiQ6EV76.
KOiK00717.
PhylomeDBiQ6EV76.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 1 hit.
[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.

Q6EV76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL
60 70 80 90 100
ERLKQQNEDL RRMAESLRIP EGPIDQGTAT GRVRVLEEQL VKAKEQIENY
110 120 130 140 150
KKQARNGLGK DHELLRRRIE NGAKELWFFL QSELKKLKHL EGNELQRHAD
160 170 180 190 200
EILLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN
210 220 230 240 250
PKDCSKARKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY
260 270 280 290 300
ATGGWETVFR PVSETCTDRS GLSTGHWSGE VNDKNIQVVE LPIVDSLHPR
310 320 330 340 350
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT
360 370 380 390 400
KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD
410 420 430 440 450
KKRVYLATDD PALLKEAKTK YSNYEFISDN SISWSAGLHN RYTENSLRGV
460 470 480 490 500
ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG
510 520 530 540 550
GQNAHNQIAV YPHKPRTDEE IPMEPGDIIG VAGNHWDGYS KGVNRKLGKT
560 570
GLYPSYKVRE KIETVKYPTY PEAEK
Length:575
Mass (Da):66,485
Last modified:August 16, 2004 - v1
Checksum:i731EFB6D850B76CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ781406 mRNA. Translation: CAH03674.1.
RefSeqiNP_001002289.1. NM_001002289.1.
UniGeneiRn.228620.

Genome annotation databases

GeneIDi432392.
KEGGirno:432392.
UCSCiRGD:1303096. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ781406 mRNA. Translation: CAH03674.1.
RefSeqiNP_001002289.1. NM_001002289.1.
UniGeneiRn.228620.

3D structure databases

ProteinModelPortaliQ6EV76.
SMRiQ6EV76. Positions 108-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011220.

Protein family/group databases

CAZyiGT23. Glycosyltransferase Family 23.

PTM databases

PhosphoSiteiQ6EV76.

Proteomic databases

PaxDbiQ6EV76.
PRIDEiQ6EV76.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi432392.
KEGGirno:432392.
UCSCiRGD:1303096. rat.

Organism-specific databases

CTDi2530.
RGDi1303096. Fut8.

Phylogenomic databases

eggNOGiKOG3705. Eukaryota.
ENOG410YHM8. LUCA.
HOGENOMiHOG000007175.
HOVERGENiHBG028260.
InParanoidiQ6EV76.
KOiK00717.
PhylomeDBiQ6EV76.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi696858.
PROiQ6EV76.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51659. GT23. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Phylogeny of fucosyltransferases."
    Martinez-Duncker I., Oriol R., Mollicone R.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.

Entry informationi

Entry nameiFUT8_RAT
AccessioniPrimary (citable) accession number: Q6EV76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: August 16, 2004
Last modified: May 11, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.