Q8VHI3 (OFUT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Pofut2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Cellular component	Endoplasmic reticulum Golgi apparatus
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW mesoderm formation Inferred from mutant phenotype Ref.4. Source: MGI regulation of epithelial to mesenchymal transition Inferred from mutant phenotype Ref.4. Source: MGI regulation of gene expression Inferred from mutant phenotype Ref.4. Source: MGI regulation of secretion Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptide-O-fucosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 429	408	GDP-fucose protein O-fucosyltransferase 2		PRO_0000012155
Regions
	Region	53 – 56	4	Substrate binding By similarity
	Region	388 – 389	2	Substrate binding By similarity
Sites
	Active site	54	1	Proton donor/acceptor By similarity
	Binding site	294	1	Substrate By similarity
	Site	396	1	Required for enzyme activity
Amino acid modifications
	Glycosylation	189	1	N-linked (GlcNAc...) Potential
	Glycosylation	209	1	N-linked (GlcNAc...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Potential
	Disulfide bond	161 ↔ 192		By similarity
	Disulfide bond	412 ↔ 419		By similarity
Experimental info
	Mutagenesis	396	1	E → A: Abolishes in vitro enzyme activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8VHI3 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 0E7AFF5F1CD33560	FASTA	429	49,429
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00128336.
RefSeq	NP_084538.2. NM_030262.3.
UniGene	Mm.203556.
3D structure databases
ProteinModelPortal	Q8VHI3.
SMR	Q8VHI3. Positions 41-429.
ModBase	Search...
Protein family/group databases
CAZy	GT68. Glycosyltransferase Family 68.
PTM databases
PhosphoSite	Q8VHI3.
Proteomic databases
PaxDb	Q8VHI3.
PRIDE	Q8VHI3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020493; ENSMUSP00000020493; ENSMUSG00000020260.
GeneID	80294.
KEGG	mmu:80294.
Organism-specific databases
CTD	23275.
MGI	MGI:1916863. Pofut2.
Phylogenomic databases
eggNOG	NOG77810.
GeneTree	ENSGT00390000007989.
HOGENOM	HOG000015874.
HOVERGEN	HBG053367.
InParanoid	Q8VHI3.
KO	K03691.
OMA	ICAHARF.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q8VHI3.
Bgee	Q8VHI3.
CleanEx	MM_POFUT2.
Genevestigator	Q8VHI3.
GermOnline	ENSMUSG00000020260. Mus musculus.
Family and domain databases
InterPro	IPR019378. GDP-Fuc_O-FucTrfase. [Graphical view]
Pfam	PF10250. O-FucT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POFUT2. mouse.
NextBio	350013.
SOURCE	Search...

Entry information

Entry name

OFUT2_MOUSE

Accession

Primary (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 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program