Q9W589 (OFUT2_DROME) 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:	O-fut2
ORF Names:	CG14789

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	490 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 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of a number of protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. Ref.5
Catalytic activity	Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.
Enzyme regulation	Does not require divalent metal ions for optimal activity. Ref.5
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum. Golgi apparatus. Note: Mainly located in the endoplasmic reticulum. Ref.5
Sequence similarities	Belongs to the glycosyltransferase 68 family.
Sequence caution	The sequence CAB53644.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism
Cellular component	Endoplasmic reticulum Golgi apparatus
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Inferred from direct assay Ref.5. Source: UniProtKB embryo development Non-traceable author statement PubMed 11698403. Source: UniProtKB fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Non-traceable author statement PubMed 11698403. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from direct assay Ref.5. Source: UniProtKB endoplasmic reticulum Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	peptide-O-fucosyltransferase activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 490	465	GDP-fucose protein O-fucosyltransferase 2		PRO_0000236806
Sites
	Site	443	1	Essential for catalytic activity By similarity
Amino acid modifications
	Glycosylation	29	1	N-linked (GlcNAc...) Potential
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	368	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	442	1	E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-443. Ref.5
	Mutagenesis	443	1	E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-442. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9W589 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 54038E7CDD020768	FASTA	490	56,021
	10 20 30 40 50 60 MRGSWPRLGF PALLLLLHLL TGSDAAVRNG TAKREIGDSR GSSGTCVKGF LQEILPLPAT 70 80 90 100 110 120 CPPEVLGMRG AVYILYDVNI SEGFNLRRDV YIRMAVFVRR LQRRRRFRHV RLVLPPWPRL 130 140 150 160 170 180 YHWHSQGLQQ SGLPWSHFFD LASLRRYAPV LDYEEFLAEQ RLFGNPGAPL VHVGHAFRLQ 190 200 210 220 230 240 HYEVMLEQGI FRDKFERVTD KPCSEGSLSG GPLLQQAELR VGRFHCVRFQ GSAGLLEKLL 250 260 270 280 290 300 REAIDEDTAG PEDVDDMRTY ALLSAETVLH DHWGDEHFWQ ARRSMRFARR LEQVAADFRR 310 320 330 340 350 360 QALDTTDASA GVQRPAMWEL ERPKRNAKGG DYLCAHLRRG DFVRSRDATT PTLKAAAQQV 370 380 390 400 410 420 KQLLRGFNMT TVFLATDATP YELMELKELF YRFRLVHFAP ESNVQRRELK DGGVAVVDQL 430 440 450 460 470 480 VCAYARYFVG TYESTFTYRI YEEREILGFT QASTFNTFCK ALGGSCSRNA VWPIVWADGD 490 SDSEEDSDPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats." Luo Y., Koles K., Vorndam W., Haltiwanger R.S., Panin V.M. J. Biol. Chem. 281:9393-9399(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442 AND GLU-443.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014298 Genomic DNA. Translation: AAF45629.1. AL031027 Genomic DNA. No translation available. AL035632 Genomic DNA. Translation: CAB53644.1. Sequence problems. AY047568 mRNA. Translation: AAK77300.1.
RefSeq	NP_569916.1. NM_130560.3.
UniGene	Dm.4643.
3D structure databases
ProteinModelPortal	Q9W589.
SMR	Q9W589. Positions 73-476.
ModBase	Search...
Protein family/group databases
CAZy	GT68. Glycosyltransferase Family 68.
Proteomic databases
PaxDb	Q9W589.
PRIDE	Q9W589.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070296; FBpp0070283; FBgn0027791.
GeneID	31098.
KEGG	dme:Dmel_CG14789.
Organism-specific databases
CTD	31098.
FlyBase	FBgn0027791. O-fut2.
Phylogenomic databases
eggNOG	NOG77810.
GeneTree	ENSGT00390000007989.
InParanoid	Q9W589.
KO	K03691.
OMA	ICAHARF.
OrthoDB	EOG4SN049.
PhylomeDB	Q9W589.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q9W589.
GermOnline	CG14789. Drosophila melanogaster.
Family and domain databases
InterPro	IPR019378. GDP-Fuc_O-FucTrfase. [Graphical view]
Pfam	PF10250. O-FucT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	31098.
NextBio	771923.

Entry information

Entry name

OFUT2_DROME

Accession

Primary (citable) accession number: Q9W589
Secondary accession number(s): Q7K729, Q9U985

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project