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Reviewed, UniProtKB/Swiss-Prot Q9JIG1 (FUT9_CRIGR)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-(1,3)-fucosyltransferase
    EC=2.4.1.-
Alternative name(s):
    Galactoside 3-L-fucosyltransferase
    Fucosyltransferase 9
    Fucosyltransferase IX
      Short name=FucT-IX
      Short name=Fuc-TIX
Gene names
Name: FUT9
OrganismCricetulus griseus (Chinese hamster)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Transfers a fucose to lacto-N-neotetraose but not to either alpha2,3-sialyl lacto-N-neotetraose or lacto-N-tetraose. Can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides By similarity.

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 10 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processprotein amino acid glycosylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionfucosyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Alpha-(1,3)-fucosyltransferase
PRO_0000221117

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Signal-anchor for type II membrane protein Potential
Topological domain33 – 359327Lumenal Potential

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9JIG1-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9D5CD8BFF07EA902

FASTA35942,071
        10         20         30         40         50         60 
MTSTSKGILR PFLIVCVILA CFMACLLIYI KPTNSWVFSP MESASSVLKM KNFFSTKTDY 

        70         80         90        100        110        120 
FNETTILVWV WPFGQTFDLT SCQAMFNIQG CHLTTDRSLY NKSHAVLIHH RDISWDLTNL 

       130        140        150        160        170        180 
PQQARPPFQK WIWMNLESPT HTPQKSGIEH LFNLTLTYRR DSDIQVPYGF LTVSTNPFVF 

       190        200        210        220        230        240 
EVPSKEKLVC WVVSNWNPEH ARVKYYNELS KSIEIHTYGQ AFGEYVNEKN LIPTISTCKF 

       250        260        270        280        290        300 
YLSFENSIHK DYITEKLYNA FLAGSVPVVL GPSRENYENY IPADSFIHVE DYNSPSELAK 

       310        320        330        340        350 
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN 

« Hide

References

[1]"Alpha(1,3)fucosyltransferases expressed by the gain-of-function Chinese hamster ovary glycosylation mutants LEC12, LEC29, and LEC30."
Patnaik S.K., Zhang A., Shi S., Stanley P.
Arch. Biochem. Biophys. 375:322-332(2000) [PubMed: 10700388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Patnaik S.K., Potvin B., Stanley P.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AF230460 mRNA. Translation: AAF82412.1.
AY628212 mRNA. Translation: AAT47342.1.
AY628213 mRNA. Translation: AAT47343.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT10. Glycosyltransferase Family 10.

Phylogenomic databases

HOVERGENQ9JIG1.

Family and domain databases

InterProIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERPTHR11929. Glyco_trans_10. 1 hit.
PfamPF00852. Glyco_transf_10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUT9_CRIGR
AccessionPrimary (citable) accession number: Q9JIG1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents