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Reviewed, UniProtKB/Swiss-Prot Q91ZW2 (OFUT1_MOUSE)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GDP-fucose protein O-fucosyltransferase 1
    EC=2.4.1.221
Alternative name(s):
    Peptide-O-fucosyltransferase 1
      Short name=O-FucT-1
Gene names
Name: Pofut1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains. Plays a crucial role in Notch signaling By similarity.

Catalytic activity

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 393363GDP-fucose protein O-fucosyltransferase 1
PRO_0000012149

Regions

Motif390 – 3934Prevents secretion from ER Potential

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2331A → S in BAC32009. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q91ZW2-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D982104E95E5CF3B

FASTA39344,688
        10         20         30         40         50         60 
MGAAAWAPPH LLLRASFLLL LLLLPLRGRS AGSWDLAGYL LYCPCMGRFG NQADHFLGSL 

        70         80         90        100        110        120 
AFAKLLNRTL AVPPWIEYQH HKPPFTNLHV SYQKYFKLEP LQAYHRVVSL EDFMENLAPS 

       130        140        150        160        170        180 
HWPPEKRVAY CFEVAAQRSP DKKTCPMKEG NPFGPFWDQF HVSFNKSELF TGISFSASYK 

       190        200        210        220        230        240 
EQWTQRFPAK EHPVLALPGA PAQFPVLEEH RELQKYMVWS DEMVRTGEAL ISAHLVRPYV 

       250        260        270        280        290        300 
GIHLRIGSDW KNACAMLKDG TAGSHFMASP QCVGYSRSTA TPLTMTMCLP DLKEIQRAVT 

       310        320        330        340        350        360 
LWVRALNARS VYIATDSESY VSEIQQLFKD KVRVVSLKPE VAQIDLYILG QADHFIGNCV 

       370        380        390 
SSFTAFVKRE RDLHGRQSSF FGMDRPSQLR DEF 

« Hide

References

« Hide 'large scale' references
[1]"Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase."
Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S.
J. Biol. Chem. 276:40338-40345(2001) [PubMed: 11524432] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvJ.
Tissue: Liver.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary gland.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 1

Cross-references

Sequence databases

AF375885 mRNA. Translation: AAL09577.1.
AK044629 mRNA. Translation: BAC32009.1.
AK132301 mRNA. Translation: BAE21090.1.
BC046295 mRNA. Translation: AAH46295.1.
IPIIPI00131488.
RefSeqNP_001034144.1.
NP_536711.3.
UniGeneMm.293761

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

PTM databases

PhosphoSiteQ91ZW2.

Proteomic databases

PRIDEQ91ZW2.

Genome annotation databases

EnsemblENSMUSG00000046020. Mus musculus. [Contig view]
GeneID140484.
KEGGmmu:140484.

Organism-specific databases

MGIMGI:2153207. Pofut1.

Phylogenomic databases

HOGENOMQ91ZW2.
HOVERGENQ91ZW2.
OMAQ91ZW2. QSVYIAT.

Enzyme and pathway databases

BRENDA2.4.1.221. 244.

Gene expression databases

ArrayExpressQ91ZW2.
BgeeQ91ZW2.
CleanExMM_POFUT1.
GermOnlineENSMUSG00000046020. Mus musculus.

Family and domain databases

InterProIPR019378. GDP-Fuc_prot_O-FucTrfase.
[Graphical view]
PfamPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio369790.
SOURCESearch...

Entry information

Entry nameOFUT1_MOUSE
AccessionPrimary (citable) accession number: Q91ZW2
Secondary accession number(s): Q3V1R0, Q8C8R4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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

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