Q8WR51 (OFUT2_CAEEL) 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):
Patterning defective protein 2
Peptide-O-fucosyltransferase 2
Short name=O-FucT-2

Gene names

Name:	pad-2
ORF Names:	K10G9.3

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	424 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. Ref.1
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. Note: Mainly located in the endoplasmic reticulum. Ref.1
Tissue specificity	Expressed in the anterior part of embryos, in the hypodermal and neuronal cells of the head. Expressed at different levels in a variety of cell types after hatching, including neuronal, hypodermal, muscle, intestinal, and somatic gonadal cells. Expressed in the nerve ring around the pharynx, in dorsal and ventral nerve cords, intestine, and a variety of hypodermal cells of L1-L3 larvae. Expressed in gonadal sheath cells, spermatheca, and tissues surrounding the vulva of adult hermaphrodites, and in the body wall muscle and hypodermal cells of adults of both sexes. Ref.1
Developmental stage	Expressed starts at morphogenetic embryonic stages and continues throughout development. Ref.1
Sequence similarities	Belongs to the glycosyltransferase 68 family.

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
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 – 20	20	Potential
	Chain	21 – 424	404	GDP-fucose protein O-fucosyltransferase 2		PRO_0000012157
Regions
	Region	51 – 54	4	Substrate binding By similarity
	Region	383 – 384	2	Substrate binding By similarity
Sites
	Active site	52	1	Proton donor/acceptor By similarity
	Binding site	290	1	Substrate By similarity
	Site	391	1	Essential for catalytic activity By similarity
Amino acid modifications
	Glycosylation	205	1	N-linked (GlcNAc...) Ref.3
	Disulfide bond	154 ↔ 187		By similarity
	Disulfide bond	407 ↔ 414		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8WR51 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 2A35F5FC04EF70B3	FASTA	424	50,106
	10 20 30 40 50 60 MHFFPIQLLV LFFAEKIAFA ENSDQTVSRV DSNRYSVAAE KKFLLYDVNF GEGFNLRRDV 70 80 90 100 110 120 YMRVANTVRS LRDSGENYIL VLPPWGRLHH WKRMEVALSW RLFFDLESLN RFIPVIEFED 130 140 150 160 170 180 FLDENRPIDQ VIYLQHYAEG WGTEYVRKFE KRSCLPPAES HYKQVEEFKW KGWFYSYEDV 190 200 210 220 230 240 YSRNFQCVSI QGDSGTLKDL LKHSNFSEST SIMVDRAETI LHEHYGEVDY WKARRSMRYS 250 260 270 280 290 300 NDLVDVADAF RKKYLDSDDK RDKTKLVDDW TKEKPRRTAI GGPYLGIHWR RRDFLYARRA 310 320 330 340 350 360 QLPTIPGTAK ILQDLCKKLD LQKIYLATDA PDQEVDELKA LLNGELEVYR FTDTQKLNDG 370 380 390 400 410 420 QIAIIDQYLC AHAAYFIGSY ESTFTFRIQE DREIIGFPIS TTFNRLCPDT EPTCEQPAKW KIVY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development." Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F., Antonarakis S.E., Guipponi M. Genomics 84:320-330(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205, MASS SPECTROMETRY. Strain: Bristol N2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF455271 mRNA. Translation: AAL65193.1. Z36282 Genomic DNA. Translation: CAD45602.1.
RefSeq	NP_001255070.1. NM_001268141.1.
UniGene	Cel.9168.
3D structure databases
ProteinModelPortal	Q8WR51.
SMR	Q8WR51. Positions 39-424.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.K10G9.3.
Protein family/group databases
CAZy	GT68. Glycosyltransferase Family 68.
Proteomic databases
PaxDb	Q8WR51.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	K10G9.3a; K10G9.3a; K10G9.3.
GeneID	259529.
KEGG	cel:CELE_K10G9.3.
UCSC	K10G9.3. c. elegans.
Organism-specific databases
CTD	259529.
WormBase	K10G9.3; CE31715; WBGene00010757; pad-2.
Phylogenomic databases
eggNOG	NOG77810.
GeneTree	ENSGT00390000007989.
HOGENOM	HOG000015874.
InParanoid	Q8WR51.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR019378. GDP-Fuc_O-FucTrfase. [Graphical view]
Pfam	PF10250. O-FucT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	952052.

Entry information

Entry name

OFUT2_CAEEL

Accession

Primary (citable) accession number: Q8WR51

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2002
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project