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Q8VHI3

- OFUT2_MOUSE

UniProt

Q8VHI3 - OFUT2_MOUSE

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Protein
GDP-fucose protein O-fucosyltransferase 2
Gene
Pofut2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541Proton donor/acceptor By similarity
Binding sitei294 – 2941Substrate By similarity
Sitei396 – 3961Required for enzyme activity

GO - Molecular functioni

  1. fucosyltransferase activity Source: MGI
  2. peptide-O-fucosyltransferase activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. fucose metabolic process Source: UniProtKB-KW
  2. fucosylation Source: MGI
  3. mesoderm formation Source: MGI
  4. protein O-linked fucosylation Source: UniProtKB
  5. regulation of epithelial to mesenchymal transition Source: MGI
  6. regulation of gene expression Source: MGI
  7. regulation of secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Enzyme and pathway databases

ReactomeiREACT_211817. O-glycosylation of TSR domain-containing proteins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT68. Glycosyltransferase Family 68.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pofut2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1916863. Pofut2.

Subcellular locationi

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

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi396 – 3961E → A: Abolishes in vitro enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 429408GDP-fucose protein O-fucosyltransferase 2
PRO_0000012155Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi161 ↔ 192 By similarity
Glycosylationi189 – 1891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi209 – 2091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi259 – 2591N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi412 ↔ 419 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8VHI3.
PaxDbiQ8VHI3.
PRIDEiQ8VHI3.

PTM databases

PhosphoSiteiQ8VHI3.

Expressioni

Gene expression databases

ArrayExpressiQ8VHI3.
BgeeiQ8VHI3.
CleanExiMM_POFUT2.
GenevestigatoriQ8VHI3.

Structurei

3D structure databases

ProteinModelPortaliQ8VHI3.
SMRiQ8VHI3. Positions 41-429.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 564Substrate binding By similarity
Regioni388 – 3892Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77810.
GeneTreeiENSGT00390000007989.
HOGENOMiHOG000015874.
HOVERGENiHBG053367.
InParanoidiQ8VHI3.
KOiK03691.
OMAiICAHARF.
OrthoDBiEOG76T9S1.
PhylomeDBiQ8VHI3.
TreeFamiTF314337.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8VHI3-1 [UniParc]FASTAAdd to Basket

« Hide

MAALSVVCLL LAAASWRPVS ASGEEFWPGQ SAADILSGAA SRRRYLLYDV    50
NPPEGFNLRR DVYIRVASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV 100
RIPWSEFFDL PSLNKNIPVI EYEQFIAESG GPFIDQVYVL QGYAEGWKEG 150
TWEEKVDARP CIDPLLYSQD KHEYYRGWFW GYEETRGLNV SCLSVQGSAS 200
IVAPVLLKNT SARSVMLDRA ENLLHDHYGG REYWDTRRSM VFAKHLRAVG 250
DEFRSQHLNS TDAADKMAPE EDWTKMKVKL GSALGGPYLG VHLRRKDFIW 300
GHREDVPSLE GAVKKIRSLM KTHQLDKVFV ATDAIRKEQE ELRKLLPEMV 350
RFEPTWEELE LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL 400
GLDPKTTYNR FCGDQEKACE QPTHWKIAY 429
Length:429
Mass (Da):49,429
Last modified:March 1, 2002 - v1
Checksum:i0E7AFF5F1CD33560
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF455270 mRNA. Translation: AAL65192.1.
BC018194 mRNA. No translation available.
AK009301 mRNA. Translation: BAB26202.1.
CCDSiCCDS23954.1.
RefSeqiNP_084538.2. NM_030262.3.
UniGeneiMm.203556.

Genome annotation databases

EnsembliENSMUST00000020493; ENSMUSP00000020493; ENSMUSG00000020260.
GeneIDi80294.
KEGGimmu:80294.
UCSCiuc007fvj.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 2

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF455270 mRNA. Translation: AAL65192.1 .
BC018194 mRNA. No translation available.
AK009301 mRNA. Translation: BAB26202.1 .
CCDSi CCDS23954.1.
RefSeqi NP_084538.2. NM_030262.3.
UniGenei Mm.203556.

3D structure databases

ProteinModelPortali Q8VHI3.
SMRi Q8VHI3. Positions 41-429.
ModBasei Search...

Protein family/group databases

CAZyi GT68. Glycosyltransferase Family 68.

PTM databases

PhosphoSitei Q8VHI3.

Proteomic databases

MaxQBi Q8VHI3.
PaxDbi Q8VHI3.
PRIDEi Q8VHI3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020493 ; ENSMUSP00000020493 ; ENSMUSG00000020260 .
GeneIDi 80294.
KEGGi mmu:80294.
UCSCi uc007fvj.1. mouse.

Organism-specific databases

CTDi 23275.
MGIi MGI:1916863. Pofut2.

Phylogenomic databases

eggNOGi NOG77810.
GeneTreei ENSGT00390000007989.
HOGENOMi HOG000015874.
HOVERGENi HBG053367.
InParanoidi Q8VHI3.
KOi K03691.
OMAi ICAHARF.
OrthoDBi EOG76T9S1.
PhylomeDBi Q8VHI3.
TreeFami TF314337.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_211817. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

ChiTaRSi POFUT2. mouse.
NextBioi 350013.
PROi Q8VHI3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8VHI3.
Bgeei Q8VHI3.
CleanExi MM_POFUT2.
Genevestigatori Q8VHI3.

Family and domain databases

InterProi IPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view ]
Pfami PF10250. O-FucT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiOFUT2_MOUSE
AccessioniPrimary (citable) accession number: Q8VHI3
Secondary accession number(s): Q8VEM2, Q9CV66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 92 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

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