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Protein

Alpha-(1,3)-fucosyltransferase 9

Gene

Fut9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Pathwayi

GO - Molecular functioni

  • alpha-(1->3)-fucosyltransferase activity Source: MGI

GO - Biological processi

  • fucosylation Source: GOC
  • nervous system development Source: Ensembl
  • protein glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT10. Glycosyltransferase Family 10.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Fut9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1330859. Fut9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3221Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini33 – 359327LumenalSequence 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 – 359359Alpha-(1,3)-fucosyltransferase 9PRO_0000221119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO88819.
PaxDbiO88819.
PRIDEiO88819.

PTM databases

PhosphoSiteiO88819.

Expressioni

Tissue specificityi

Mainly detected in brain and kidney.1 Publication

Gene expression databases

BgeeiO88819.
CleanExiMM_FUT9.
ExpressionAtlasiO88819. baseline and differential.
GenevestigatoriO88819.

Structurei

3D structure databases

ProteinModelPortaliO88819.
SMRiO88819. Positions 183-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 10 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG19459.
HOGENOMiHOG000045583.
HOVERGENiHBG000274.
InParanoidiO88819.
KOiK03663.
OMAiLYNRSHA.
OrthoDBiEOG7Z69C9.
PhylomeDBiO88819.
TreeFamiTF316348.

Family and domain databases

InterProiIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERiPTHR11929. PTHR11929. 1 hit.
PfamiPF00852. Glyco_transf_10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88819-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSTSKGILR PFLIVCIILG CFMACLLIYI KPTNSWVFSP MESASSVLKM
60 70 80 90 100
KNFFSTKTDY FNETTILVWV WPFGQTFDLT SCQAMFNIQG CHLTTDRSLY
110 120 130 140 150
NKSHAVLIHH RDISWDLTNL PQQARPPFQK WIWMNLESPT HTPQKSGIEH
160 170 180 190 200
LFNLTLTYRR DSDIQVPYGF LTVSTNPFVF EVPSKEKLVC WVVSNWNPEH
210 220 230 240 250
ARVKYYNELS KSIEIHTYGQ AFGEYVNDKN LIPTISTCKF YLSFENSIHK
260 270 280 290 300
DYITEKLYNA FLAGSVPVVL GPSRENYENY IPADSFIHVE DFNSPSELAK
310 320 330 340 350
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV

GNLEKWFWN
Length:359
Mass (Da):42,041
Last modified:November 1, 1998 - v1
Checksum:i96A2394547F2A44E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18011.1.
RefSeqiNP_034373.1. NM_010243.3.
UniGeneiMm.39101.

Genome annotation databases

EnsembliENSMUST00000084770; ENSMUSP00000081826; ENSMUSG00000055373.
ENSMUST00000108199; ENSMUSP00000103834; ENSMUSG00000055373.
GeneIDi14348.
KEGGimmu:14348.
UCSCiuc008sei.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Fucosyltransferase 9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18011.1.
RefSeqiNP_034373.1. NM_010243.3.
UniGeneiMm.39101.

3D structure databases

ProteinModelPortaliO88819.
SMRiO88819. Positions 183-313.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT10. Glycosyltransferase Family 10.

PTM databases

PhosphoSiteiO88819.

Proteomic databases

MaxQBiO88819.
PaxDbiO88819.
PRIDEiO88819.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084770; ENSMUSP00000081826; ENSMUSG00000055373.
ENSMUST00000108199; ENSMUSP00000103834; ENSMUSG00000055373.
GeneIDi14348.
KEGGimmu:14348.
UCSCiuc008sei.1. mouse.

Organism-specific databases

CTDi10690.
MGIiMGI:1330859. Fut9.

Phylogenomic databases

eggNOGiNOG19459.
HOGENOMiHOG000045583.
HOVERGENiHBG000274.
InParanoidiO88819.
KOiK03663.
OMAiLYNRSHA.
OrthoDBiEOG7Z69C9.
PhylomeDBiO88819.
TreeFamiTF316348.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi285799.
PROiO88819.
SOURCEiSearch...

Gene expression databases

BgeeiO88819.
CleanExiMM_FUT9.
ExpressionAtlasiO88819. baseline and differential.
GenevestigatoriO88819.

Family and domain databases

InterProiIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERiPTHR11929. PTHR11929. 1 hit.
PfamiPF00852. Glyco_transf_10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiFUT9_MOUSE
AccessioniPrimary (citable) accession number: O88819
Secondary accession number(s): Q3TQ63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 1, 1998
Last modified: May 27, 2015
This is version 117 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.