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P83337

- OFUT1_CRIGR

UniProt

P83337 - OFUT1_CRIGR

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Protein
GDP-fucose protein O-fucosyltransferase 1
Gene
POFUT1
Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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 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. 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 DELTA1 or JAGGED1 By similarity. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) By similarity.3 Publications

Catalytic activityi

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.3 Publications

Enzyme regulationi

Activated by manganese and, to a lesser extent, by other divalent metals such as cobalt and calcium. Inhibited by copper, ferric and zinc ions.1 Publication

Kineticsi

  1. KM=11 µM for His(6)-F7-EGF-11 Publication
  2. KM=15 µM for F7-EGF-1

Vmax=2.5 µmol/min/mg enzyme

Vmax=2.4 µmol/min/mg enzyme

pH dependencei

Optimum pH is 5.5-8.0.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei339 – 3391Substrate By similarity

GO - Molecular functioni

  1. peptide-O-fucosyltransferase activity Source: UniProtKB
  2. transferase activity Source: UniProtKB
  3. transferase activity, transferring glycosyl groups Source: UniProtKB
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: GOC
  4. protein glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Enzyme and pathway databases

UniPathwayiUPA00378.

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:POFUT1
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus
ProteomesiUP000001075: Unassembled WGS sequence

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392GDP-fucose protein O-fucosyltransferase 1
PRO_0000220935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 44 By similarity
Glycosylationi66 – 661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi130 ↔ 144 By similarity
Glycosylationi164 – 1641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi253 ↔ 287 By similarity
Disulfide bondi271 ↔ 358 By similarity

Post-translational modificationi

N-glycosylated. Contains high mannose-type carbohydrates.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 503Substrate binding By similarity
Regioni242 – 2443Substrate binding By similarity
Regioni360 – 3612Substrate binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi389 – 3924Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Phylogenomic databases

KOiK03691.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83337-1 [UniParc]FASTAAdd to Basket

« Hide

MGAAAWAPPH LLLRVSLLLL LLLPLRGRLA GSWDLAGYLL YCPCMGRFGN    50
QADHFLGSLA FAKLLNRTLA VPPWIEYQHH KPPFTNLHVS YQKYFKLEPL 100
QAYHRVISLE EFMEKLAPIH WPPEKRVAYC FEVAAQRSPD KKTCPMKEGN 150
PFGPFWDQFH VSFNKSELFT GISFSASYKE QWIQRFPPEE HPVLALPGAP 200
AQFPVLEEHR ALQKYMVWSD EMVKTGEAQI STHLIRPYVG IHLRIGSDWK 250
NACAMLKDGT AGSHFMASPQ CVGYSRSTAT PLTMTMCLPD LNEIQRAVKL 300
WVRALNARSI YIATDSESYV PEIQQLFKEK VKVVSLKPEV AQVDLYILGQ 350
ADHFIGNCVS SFTAFVKRER DLHGRQSSFF GMDRPSQPRD EF 392
Length:392
Mass (Da):44,669
Last modified:January 9, 2013 - v2
Checksum:i45E1421CBA0880C4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661N → V AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JH000311 Genomic DNA. Translation: EGW00282.1.
RefSeqiXP_003502364.1. XM_003502316.2.

Genome annotation databases

GeneIDi100753417.
KEGGicge:100753417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
JH000311 Genomic DNA. Translation: EGW00282.1 .
RefSeqi XP_003502364.1. XM_003502316.2.

3D structure databases

ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100753417.
KEGGi cge:100753417.

Organism-specific databases

CTDi 23509.

Phylogenomic databases

KOi K03691.

Enzyme and pathway databases

UniPathwayi UPA00378 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: PROTEIN SEQUENCE OF 28-88.
  3. "O-linked fucose and other post-translational modifications unique to EGF modules."
    Harris R.J., Spellman M.W.
    Glycobiology 3:219-224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY.
  4. "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: FUNCTION.
  5. "Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells."
    Wang Y., Spellman M.W.
    J. Biol. Chem. 273:8112-8118(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES.

Entry informationi

Entry nameiOFUT1_CRIGR
AccessioniPrimary (citable) accession number: P83337
Secondary accession number(s): G3HE95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 9, 2013
Last modified: September 3, 2014
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

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

External Data

Dasty 3

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