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Q6EV70

- OFUT1_RAT

UniProt

Q6EV70 - OFUT1_RAT

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Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

Pofut1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) (By similarity). Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1.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.By similarity1 Publication

Enzyme regulationi

Activated by manganese and, to a lesser extent, by calcium.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei342 – 3421SubstrateBy similarity

GO - Molecular functioni

  1. fucosyltransferase activity Source: UniProtKB
  2. peptide-O-fucosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. fucose metabolic process Source: UniProtKB-KW
  3. heart development Source: Ensembl
  4. nervous system development Source: Ensembl
  5. Notch signaling pathway Source: UniProtKB-KW
  6. protein O-linked glycosylation Source: UniProtKB
  7. somitogenesis Source: Ensembl
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

ReactomeiREACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.
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
Name:Pofut1Imported
Synonyms:Fut12
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi1303001. Pofut1.

Subcellular locationi

Endoplasmic reticulum 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: RGD
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 395363GDP-fucose protein O-fucosyltransferase 1Sequence AnalysisPRO_0000012151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 47By similarity
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi133 ↔ 147By similarity
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi256 ↔ 290By similarity
Disulfide bondi274 ↔ 361By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6EV70.
PRIDEiQ6EV70.

Expressioni

Gene expression databases

GenevestigatoriQ6EV70.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013730.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 533Substrate bindingBy similarity
Regioni245 – 2473Substrate bindingBy similarity
Regioni363 – 3642Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi392 – 3954Prevents secretion from ER

Sequence similaritiesi

Belongs to the glycosyltransferase 68 family.Sequence Analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
HOVERGENiHBG059976.
InParanoidiQ6EV70.
KOiK03691.
OMAiSEHPVLA.
OrthoDBiEOG7ZD1VC.
PhylomeDBiQ6EV70.
TreeFamiTF314805.

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.

Q6EV70-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAAAWAPSH LLLRASFLLL LLLLPLPLRG RAGGSWDLAG YLLYCPCMGR
60 70 80 90 100
FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL
110 120 130 140 150
EPLQAYHRVI SLEDFMEKLA PFHWPPEKRV AYCFEVAAQR SPDKKTCPMK
160 170 180 190 200
EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YKEQWIQRFP PKEHPVLALP
210 220 230 240 250
GAPAQFPVLE EHRELQKYMV WSDEMVRTGE AQISTHLVRP YVGIHLRIGS
260 270 280 290 300
DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TATPLTTTMC LPDLKEIQRA
310 320 330 340 350
VKLWVRALDA RSVYIATDSE SYVSEIQQLF KEKVKVVSLK PEVAQIDLYI
360 370 380 390
LGQADHFIGN CVSSFTAFVK RERDLHGRPS SFFGMDRPSQ LRDEF
Length:395
Mass (Da):44,983
Last modified:August 16, 2004 - v1
Checksum:i2A85521E22F38920
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ781499 mRNA. Translation: CAH03711.1.
RefSeqiNP_001002278.1. NM_001002278.1.
UniGeneiRn.214685.

Genome annotation databases

EnsembliENSRNOT00000013730; ENSRNOP00000013730; ENSRNOG00000010104.
GeneIDi311551.
KEGGirno:311551.
UCSCiRGD:1303001. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ781499 mRNA. Translation: CAH03711.1 .
RefSeqi NP_001002278.1. NM_001002278.1.
UniGenei Rn.214685.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000013730.

Protein family/group databases

CAZyi GT65. Glycosyltransferase Family 65.

Proteomic databases

PaxDbi Q6EV70.
PRIDEi Q6EV70.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000013730 ; ENSRNOP00000013730 ; ENSRNOG00000010104 .
GeneIDi 311551.
KEGGi rno:311551.
UCSCi RGD:1303001. rat.

Organism-specific databases

CTDi 23509.
RGDi 1303001. Pofut1.

Phylogenomic databases

eggNOGi NOG250895.
GeneTreei ENSGT00390000015634.
HOGENOMi HOG000231651.
HOVERGENi HBG059976.
InParanoidi Q6EV70.
KOi K03691.
OMAi SEHPVLA.
OrthoDBi EOG7ZD1VC.
PhylomeDBi Q6EV70.
TreeFami TF314805.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.

Miscellaneous databases

NextBioi 663802.
PROi Q6EV70.

Gene expression databases

Genevestigatori Q6EV70.

Family and domain databases

InterProi IPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view ]
Pfami PF10250. O-FucT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs."
    Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.
    Glycobiology 13:1C-5C(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: WistarImported.
  2. "Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains."
    Wang Y., Lee G.F., Kelley R.F., Spellman M.W.
    Glycobiology 6:837-842(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
  3. "O-fucosylation of notch occurs in the endoplasmic reticulum."
    Luo Y., Haltiwanger R.S.
    J. Biol. Chem. 280:11289-11294(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiOFUT1_RAT
AccessioniPrimary (citable) accession number: Q6EV70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3