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Q18014

- OFUT1_CAEEL

UniProt

Q18014 - OFUT1_CAEEL

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Protein
GDP-fucose protein O-fucosyltransferase 1
Gene
C15C7.7
Organism
Caenorhabditis elegans
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 EGF domains.By similarity1 Publication

Catalytic activityi

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei334 – 3341Substrate

GO - Molecular functioni

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

GO - Biological processi

  1. Notch signaling pathway Source: UniProtKB-KW
  2. fucose metabolic process Source: UniProtKB-KW
  3. protein O-linked fucosylation Source: WormBase
  4. protein O-linked glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Keywords - Ligandi

Manganese

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT65. Glycosyltransferase Family 65.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-fucose protein O-fucosyltransferase 1 (EC:2.4.1.221)
Alternative name(s):
Peptide-O-fucosyltransferase 1
Short name:
O-FucT-1
Gene namesi
ORF Names:C15C7.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome X

Organism-specific databases

WormBaseiC15C7.7; CE36786; WBGene00015793.

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431N → A: Reduces enzyme activity by over 90%. 1 Publication
Mutagenesisi240 – 2401R → A or K: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 389368GDP-fucose protein O-fucosyltransferase 1
PRO_0000012152Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi35 ↔ 371 Publication
Disulfide bondi119 ↔ 1351 Publication
Disulfide bondi249 ↔ 2811 Publication
Disulfide bondi266 ↔ 3531 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ18014.
PRIDEiQ18014.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 344
Beta strandi38 – 403
Helixi41 – 5818
Beta strandi61 – 633
Beta strandi67 – 693
Beta strandi71 – 744
Beta strandi76 – 783
Helixi80 – 834
Helixi86 – 894
Turni90 – 923
Helixi98 – 1047
Helixi106 – 1094
Helixi112 – 1143
Beta strandi116 – 1216
Helixi143 – 1497
Beta strandi156 – 1594
Turni164 – 1674
Beta strandi170 – 1723
Helixi178 – 1814
Turni184 – 1863
Beta strandi188 – 1947
Helixi203 – 2119
Helixi216 – 22914
Beta strandi232 – 2398
Helixi243 – 2508
Turni254 – 2563
Turni261 – 2633
Helixi264 – 2674
Helixi269 – 2713
Helixi278 – 2814
Helixi285 – 29915
Beta strandi302 – 3109
Helixi314 – 3218
Helixi322 – 3243
Helixi336 – 34510
Beta strandi346 – 3516
Helixi356 – 36712
Beta strandi368 – 3714
Beta strandi375 – 3773

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZY2X-ray1.54A26-383[»]
3ZY3X-ray1.86A/B26-383[»]
3ZY4X-ray1.74A26-383[»]
3ZY5X-ray1.96A26-383[»]
3ZY6X-ray1.91A26-383[»]
ProteinModelPortaliQ18014.
SMRiQ18014. Positions 26-381.

Miscellaneous databases

EvolutionaryTraceiQ18014.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 433Substrate binding
Regioni238 – 2403Substrate binding
Regioni355 – 3562Substrate binding

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
InParanoidiQ18014.
KOiK03691.
OMAiSEHPVLA.
OrthoDBiEOG7ZD1VC.
PhylomeDBiQ18014.

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.

Q18014-1 [UniParc]FASTAAdd to Basket

« Hide

MRVSKVLTLA SFISVCSYSE AKSNETDPNG YIVFCPCMGR FGNQVDQFLG    50
VLAFAKALDR TLVLPNFIEF KHPETKMIPF EFLFQVGTVA KYTRVVTMQE 100
FTKKIMPTVW PPEKRKAFCW TPRQAIYDKS AEPGCHSKEG NPFGPYWDQI 150
DVSFVGDEYF GDIPGGFDLN QMGSRKKWLE KFPSEEYPVL AFSSAPAPFP 200
SKGKVWSIQK YLRWSSRITE QAKKFISANL AKPFVAVHLR NDADWVRVCE 250
HIDTTTNRPL FASEQCLGEG HHLGTLTKEI CSPSKQQILE QIVEKVGSIG 300
AKSVFVASDK DHMIDEINEA LKPYEIEAHR QEPDDMYTSL AIMGRADLFV 350
GNCVSTFSHI VKRERDHAGQ SPRPSAFFGI RAVKRHIDL 389
Length:389
Mass (Da):44,051
Last modified:February 1, 2005 - v5
Checksum:i0C84F202AA184554
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FO080550 Genomic DNA. Translation: CCD64591.1.
RefSeqiNP_741744.2. NM_171649.6.
UniGeneiCel.30602.

Genome annotation databases

EnsemblMetazoaiC15C7.7; C15C7.7; WBGene00015793.
GeneIDi180607.
KEGGicel:CELE_C15C7.7.
UCSCiC15C7.7. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FO080550 Genomic DNA. Translation: CCD64591.1 .
RefSeqi NP_741744.2. NM_171649.6.
UniGenei Cel.30602.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ZY2 X-ray 1.54 A 26-383 [» ]
3ZY3 X-ray 1.86 A/B 26-383 [» ]
3ZY4 X-ray 1.74 A 26-383 [» ]
3ZY5 X-ray 1.96 A 26-383 [» ]
3ZY6 X-ray 1.91 A 26-383 [» ]
ProteinModelPortali Q18014.
SMRi Q18014. Positions 26-381.
ModBasei Search...

Protein family/group databases

CAZyi GT65. Glycosyltransferase Family 65.

Proteomic databases

PaxDbi Q18014.
PRIDEi Q18014.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai C15C7.7 ; C15C7.7 ; WBGene00015793 .
GeneIDi 180607.
KEGGi cel:CELE_C15C7.7.
UCSCi C15C7.7. c. elegans.

Organism-specific databases

CTDi 180607.
WormBasei C15C7.7 ; CE36786 ; WBGene00015793 .

Phylogenomic databases

eggNOGi NOG250895.
GeneTreei ENSGT00390000015634.
HOGENOMi HOG000231651.
InParanoidi Q18014.
KOi K03691.
OMAi SEHPVLA.
OrthoDBi EOG7ZD1VC.
PhylomeDBi Q18014.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

EvolutionaryTracei Q18014.
NextBioi 910082.
PROi Q18014.

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. "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.
  2. "Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase."
    Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S.
    J. Biol. Chem. 276:40338-40345(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMOLOGY.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 26-383 IN COMPLEX WITH GDP-FUCOSE AND MANGANESE, ABSENCE OF COFACTOR REQUIREMENT, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF ASN-43 AND ARG-240.

Entry informationi

Entry nameiOFUT1_CAEEL
AccessioniPrimary (citable) accession number: Q18014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 90 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

Manganese is bound to the substrate GDP-fucose, but is not required for enzyme activity.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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