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Q8VHI3 (OFUT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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:
GDP-fucose protein O-fucosyltransferase 2

EC=2.4.1.221
Alternative name(s):
Peptide-O-fucosyltransferase 2
Short name=O-FucT-2
Gene names
Name:Pofut2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombosporin (TSP) and spondin families. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13 By similarity. O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm. Ref.4

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Note: Mainly located in the endoplasmic reticulum By similarity.

Disruption phenotype

Null mice embryos die before E10.5. At the onset of gastrulation at E6.5, embryos are rounder and the embryonic and extra-embryonic ectoderm appears thickened and disorganized. Expression of NODAL and WNT3 is significantly expanded and/or displaced in the primitive streak as is BMP4 in the extra-embryonic ectoderm. By E7.5, embryos are unusually dense and shorter characterized by a dumb-bell appearance. There is unrestricted epithelial to mesenchymal transition (EMT) producing an abundance of mesenchymal cells. SNAIL1 expression is expanded and E-cadherin expression decreased. There is distal expansion of the proximal visceral endoderm. Ref.4

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence caution

The sequence BC018194 differs from that shown. Reason: Frameshift at position 380.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 429408GDP-fucose protein O-fucosyltransferase 2
PRO_0000012155

Regions

Region53 – 564Substrate binding By similarity
Region388 – 3892Substrate binding By similarity

Sites

Active site541Proton donor/acceptor By similarity
Binding site2941Substrate By similarity
Site3961Required for enzyme activity

Amino acid modifications

Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Disulfide bond161 ↔ 192 By similarity
Disulfide bond412 ↔ 419 By similarity

Experimental info

Mutagenesis3961E → A: Abolishes in vitro enzyme activity. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8VHI3 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 0E7AFF5F1CD33560

FASTA42949,429
        10         20         30         40         50         60 
MAALSVVCLL LAAASWRPVS ASGEEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR 

        70         80         90        100        110        120 
DVYIRVASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI 

       130        140        150        160        170        180 
EYEQFIAESG GPFIDQVYVL QGYAEGWKEG TWEEKVDARP CIDPLLYSQD KHEYYRGWFW 

       190        200        210        220        230        240 
GYEETRGLNV SCLSVQGSAS IVAPVLLKNT SARSVMLDRA ENLLHDHYGG REYWDTRRSM 

       250        260        270        280        290        300 
VFAKHLRAVG DEFRSQHLNS TDAADKMAPE EDWTKMKVKL GSALGGPYLG VHLRRKDFIW 

       310        320        330        340        350        360 
GHREDVPSLE GAVKKIRSLM KTHQLDKVFV ATDAIRKEQE ELRKLLPEMV RFEPTWEELE 

       370        380        390        400        410        420 
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE 


QPTHWKIAY 

« Hide

References

« Hide 'large scale' references
[1]"C21orf80, a new gene from the 21q22.3 region: using RNAi to get insight into the function."
Menzel O., Reymond A., Antonarakis S.E., Guipponi M.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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] OF 1-119.
Strain: C57BL/6J.
Tissue: Tongue.
[4]"O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation."
Du J., Takeuchi H., Leonhard-Melief C., Shroyer K.R., Dlugosz M., Haltiwanger R.S., Holdener B.C.
Dev. Biol. 346:25-38(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, MUTAGENESIS OF GLU-396.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF455270 mRNA. Translation: AAL65192.1.
BC018194 mRNA. No translation available.
AK009301 mRNA. Translation: BAB26202.1.
RefSeqNP_084538.2. NM_030262.3.
UniGeneMm.203556.

3D structure databases

ProteinModelPortalQ8VHI3.
SMRQ8VHI3. Positions 41-429.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT68. Glycosyltransferase Family 68.

PTM databases

PhosphoSiteQ8VHI3.

Proteomic databases

PaxDbQ8VHI3.
PRIDEQ8VHI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020493; ENSMUSP00000020493; ENSMUSG00000020260.
GeneID80294.
KEGGmmu:80294.
UCSCuc007fvj.1. mouse.

Organism-specific databases

CTD23275.
MGIMGI:1916863. Pofut2.

Phylogenomic databases

eggNOGNOG77810.
GeneTreeENSGT00390000007989.
HOGENOMHOG000015874.
HOVERGENHBG053367.
InParanoidQ8VHI3.
KOK03691.
OMAICAHARF.
OrthoDBEOG76T9S1.
PhylomeDBQ8VHI3.
TreeFamTF314337.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8VHI3.
BgeeQ8VHI3.
CleanExMM_POFUT2.
GenevestigatorQ8VHI3.

Family and domain databases

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

Other

ChiTaRSPOFUT2. mouse.
NextBio350013.
PROQ8VHI3.
SOURCESearch...

Entry information

Entry nameOFUT2_MOUSE
AccessionPrimary (citable) accession number: Q8VHI3
Secondary accession number(s): Q8VEM2, Q9CV66
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 89 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