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Q9JL27 (FUT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:
Galactoside 2-alpha-L-fucosyltransferase 2
EC=2.4.1.69
Alternative name(s):
Alpha(1,2)FT 2
Fucosyltransferase 2
GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2
Secretory blood group protein 2
Gene names
Name:Fut2
Synonyms:Sec2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway.

Catalytic activity

GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Miscellaneous

In mouse, there are three genes (Fut1, Fut2 and Sec1) which encode galactoside 2-L-fucosyltransferase.

Sequence similarities

Belongs to the glycosyltransferase 11 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Galactoside 2-alpha-L-fucosyltransferase 2
PRO_0000149109

Regions

Topological domain1 – 55Cytoplasmic Potential
Transmembrane6 – 2621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 347321Lumenal Potential

Amino acid modifications

Glycosylation1921N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9JL27 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DD5F441046CC8E79

FASTA34739,243
        10         20         30         40         50         60 
MASAQVPFSF PLAHFLIFVF VTSTIIHLQQ RIVKLQTLSE KELQAVQMSS PNAARTDMQQ 

        70         80         90        100        110        120 
SAKLQGIFTI NSIGRLGNQM GEYATLFALA RMNGRLAFIP ESMHNALAPI FRISLPVLHS 

       130        140        150        160        170        180 
DTARRIPWQN YHLNDWMEER YRHIPGQYVR FTGYPCSWTF YHHLRPEILK EFTLHDHVRE 

       190        200        210        220        230        240 
EAQAFLRGLR VNGSQPSTFV GVHVRRGDYV HVMPKVWKGV VADRGYLEKA LDRFRARYSS 

       250        260        270        280        290        300 
PVFVVTSNGM AWCRENINTS LGDVVFAGNG IEGSPAKDFA LLTQCNHTIM TIGTFGIWAA 

       310        320        330        340 
YLAGGDTIYL ANYTLPDSPF LKIFKPAAAF LPEWMGIPAD LSPLLKH

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, genomic mapping, and expression of two secretor blood group alpha (1,2)fucosyltransferase genes differentially regulated in mouse uterine epithelium and gastrointestinal tract."
Domino S.E., Zhang L., Lowe J.B.
J. Biol. Chem. 276:23748-23756(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Ola.
[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: Colon.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Fucosyltransferase 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF214656 Genomic DNA. Translation: AAF45146.1.
AK033520 mRNA. Translation: BAC28338.1.
IPIIPI00311608.
RefSeqNP_001258922.1. NM_001271993.1.
NP_061364.2. NM_018876.4.
UniGeneMm.290046.

3D structure databases

ProteinModelPortalQ9JL27.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000063719.

Protein family/group databases

CAZyGT11. Glycosyltransferase Family 11.

PTM databases

PhosphoSiteQ9JL27.

Proteomic databases

PRIDEQ9JL27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069800; ENSMUSP00000063719; ENSMUSG00000055978.
GeneID14344.
KEGGmmu:14344.

Organism-specific databases

CTD2524.
MGIMGI:109374. Fut2.

Phylogenomic databases

eggNOGNOG17447.
GeneTreeENSGT00390000001450.
HOGENOMHOG000261621.
HOVERGENHBG004338.
InParanoidQ9JL27.
KOK00718.
OMAFSFPMAH.
OrthoDBEOG4BK545.

Enzyme and pathway databases

BRENDA2.4.1.69. 3474.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9JL27.
BgeeQ9JL27.
CleanExMM_FUT2.
GenevestigatorQ9JL27.
GermOnlineENSMUSG00000055978. Mus musculus.

Family and domain databases

InterProIPR002516. Glyco_trans_11.
[Graphical view]
PANTHERPTHR11927. PTHR11927. 1 hit.
PfamPF01531. Glyco_transf_11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285785.
SOURCESearch...

Entry information

Entry nameFUT2_MOUSE
AccessionPrimary (citable) accession number: Q9JL27
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: October 1, 2000
Last modified: April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents