Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O88819 (FUT9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-(1,3)-fucosyltransferase 9

EC=2.4.1.-
Alternative name(s):
Fucosyltransferase 9
Fucosyltransferase IX
Short name=Fuc-TIX
Short name=FucT-IX
Galactoside 3-L-fucosyltransferase
Gene names
Name:Fut9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
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. Ref.1

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.

Tissue specificity

Mainly detected in brain and kidney. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Alpha-(1,3)-fucosyltransferase 9
PRO_0000221119

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Signal-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
O88819 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 96A2394547F2A44E

FASTA35942,041
        10         20         30         40         50         60 
MTSTSKGILR PFLIVCIILG 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 AFGEYVNDKN LIPTISTCKF 

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

       310        320        330        340        350 
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning and characterization of a novel murine alpha1, 3-fucosyltransferase, mFuc-TIX, that synthesizes the Lewis x (CD15) epitope in brain and kidney."
Kudo T., Ikehara Y., Togayachi A., Kaneko M., Hiraga T., Sasaki K., Narimatsu H.
J. Biol. Chem. 273:26729-26738(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Corpus striatum and Olfactory bulb.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015426 mRNA. Translation: BAA33522.1.
AK032177 mRNA. Translation: BAC27746.1.
AK036183 mRNA. Translation: BAC29338.1.
AK043410 mRNA. Translation: BAC31540.1.
AK047650 mRNA. Translation: BAC33112.1.
AK049122 mRNA. Translation: BAC33555.1.
AK163871 mRNA. Translation: BAE37522.1.
RefSeqNP_034373.1. NM_010243.3.
UniGeneMm.39101.

3D structure databases

ProteinModelPortalO88819.
SMRO88819. Positions 100-325.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT10. Glycosyltransferase Family 10.

PTM databases

PhosphoSiteO88819.

Proteomic databases

PaxDbO88819.
PRIDEO88819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084770; ENSMUSP00000081826; ENSMUSG00000055373.
ENSMUST00000108199; ENSMUSP00000103834; ENSMUSG00000055373.
GeneID14348.
KEGGmmu:14348.
UCSCuc008sei.1. mouse.

Organism-specific databases

CTD10690.
MGIMGI:1330859. Fut9.

Phylogenomic databases

eggNOGNOG19459.
HOGENOMHOG000045583.
HOVERGENHBG000274.
InParanoidO88819.
KOK03663.
OMALIWVWPF.
OrthoDBEOG7Z69C9.
PhylomeDBO88819.
TreeFamTF316348.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeO88819.
CleanExMM_FUT9.
GenevestigatorO88819.

Family and domain databases

InterProIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERPTHR11929. PTHR11929. 1 hit.
PfamPF00852. Glyco_transf_10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285799.
PROO88819.
SOURCESearch...

Entry information

Entry nameFUT9_MOUSE
AccessionPrimary (citable) accession number: O88819
Secondary accession number(s): Q3TQ63
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot