Reviewed, UniProtKB/Swiss-Prot Q8VHI3 (OFUT2_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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 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 thrombospondin type 1 repeats By similarity.
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.
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
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide-O-fucosyltransferase activity Inferred from electronic annotation. Source: EC
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
Amino acid modifications
	Glycosylation	189	1	N-linked (GlcNAc...) Potential
	Glycosylation	209	1	N-linked (GlcNAc...) Potential
	Glycosylation	259	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8VHI3-1 [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: 15489334] [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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-119. Strain: C57BL/6J. Tissue: Tongue.
+	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.
UniGene	Mm.203556
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8VHI3.
Protein family/group databases
CAZy	GT68. Glycosyltransferase Family 68.
Proteomic databases
PRIDE	Q8VHI3.
Genome annotation databases
Ensembl	ENSMUST00000020493; ENSMUSP00000020493; ENSMUSG00000020260; Mus musculus. [Genome view]
GeneID	80294.
KEGG	mmu:80294.
UCSC	uc007fvj.1. mouse.
Organism-specific databases
CTD	80294.
MGI	MGI:1916863. Pofut2.
Phylogenomic databases
HOGENOM	HBG314645.
HOVERGEN	Q8VHI3.
InParanoid	Q8VHI3.
OMA	HARFFIG.
PhylomeDB	Q8VHI3.
Enzyme and pathway databases
BRENDA	2.4.1.221. 244.
Gene expression databases
ArrayExpress	Q8VHI3.
Bgee	Q8VHI3.
CleanEx	MM_POFUT2.
Genevestigator	Q8VHI3.
GermOnline	ENSMUSG00000020260. Mus musculus.
Family and domain databases
InterPro	IPR019378. GDP-Fuc_prot_O-FucTrfase. [Graphical view]
Pfam	PF10250. O-FucT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)