OFUT1_PANTR
ID OFUT1_PANTR Reviewed; 388 AA.
AC Q6EV69;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
DE EC=2.4.1.221 {ECO:0000250|UniProtKB:Q9H488};
DE AltName: Full=Peptide-O-fucosyltransferase 1;
DE Short=O-FucT-1;
DE Flags: Precursor;
GN Name=POFUT1; Synonyms=FUT12;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12966037; DOI=10.1093/glycob/cwg113;
RA Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.;
RT "A new superfamily of protein-O-fucosyltransferases, alpha2-
RT fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and
RT identification of conserved peptide motifs.";
RL Glycobiology 13:1C-5C(2003).
CC -!- FUNCTION: Catalyzes the reaction that attaches fucose through an O-
CC glycosidic linkage to a conserved serine or threonine residue found in
CC the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and
CC C3 are the second and third conserved cysteines. Specifically uses GDP-
CC fucose as donor substrate and proper disulfide pairing of the substrate
CC EGF domains is required for fucose transfer. Plays a crucial role in
CC NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a
CC substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can
CC then extend the fucosylation on the NOTCH EGF repeats. This extended
CC fucosylation is required for optimal ligand binding and canonical NOTCH
CC signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines
CC its ability to cluster acetylcholine receptors (AChRs).
CC {ECO:0000250|UniProtKB:Q9H488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-
CC L-seryl-[protein] + GDP + H(+); Xref=Rhea:RHEA:63644, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:17914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189632; EC=2.4.1.221;
CC Evidence={ECO:0000250|UniProtKB:Q9H488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000250|UniProtKB:Q9H488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-
CC fucosyl)-L-threonyl-[protein] + GDP + H(+); Xref=Rhea:RHEA:70491,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:17915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189631; EC=2.4.1.221;
CC Evidence={ECO:0000250|UniProtKB:Q9H488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000250|UniProtKB:Q9H488};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9H488}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q6EV70}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P83337}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 65 family.
CC {ECO:0000305}.
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DR EMBL; AJ781500; CAH03712.1; -; mRNA.
DR RefSeq; NP_001008982.1; NM_001008982.1.
DR AlphaFoldDB; Q6EV69; -.
DR SMR; Q6EV69; -.
DR STRING; 9598.ENSPTRP00000022931; -.
DR CAZy; GT65; Glycosyltransferase Family 65.
DR PaxDb; Q6EV69; -.
DR Ensembl; ENSPTRT00000024842; ENSPTRP00000022931; ENSPTRG00000013375.
DR GeneID; 449504; -.
DR KEGG; ptr:449504; -.
DR CTD; 23509; -.
DR VGNC; VGNC:14278; POFUT1.
DR eggNOG; KOG3849; Eukaryota.
DR GeneTree; ENSGT00390000015634; -.
DR HOGENOM; CLU_039551_0_0_1; -.
DR InParanoid; Q6EV69; -.
DR OMA; YPELCMP; -.
DR OrthoDB; 1127619at2759; -.
DR TreeFam; TF314805; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 20.
DR Bgee; ENSPTRG00000013375; Expressed in fibroblast and 22 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0036066; P:protein O-linked fucosylation; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR CDD; cd11302; O-FucT-1; 1.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR039922; POFUT1.
DR PANTHER; PTHR21420; PTHR21420; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Disulfide bond; Endoplasmic reticulum;
KW Fucose metabolism; Glycoprotein; Glycosyltransferase; Manganese;
KW Notch signaling pathway; Reference proteome; Signal; Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..388
FT /note="GDP-fucose protein O-fucosyltransferase 1"
FT /id="PRO_0000012150"
FT MOTIF 385..388
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT BINDING 43..46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 238..240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 357..358
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..40
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT DISULFID 126..140
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT DISULFID 249..283
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT DISULFID 267..354
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
SQ SEQUENCE 388 AA; 43956 MW; 3FACCCA434D02415 CRC64;
MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH FLGSLAFAKL
LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH RVISLEDFME KLAPTHWPPE
KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP FWDQFHVSFN KSELFTGISF SASYREQWSQ
RFSPKEHPVL ALPGAPAQFP VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR
IGSDWKNACA MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS
LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF IGNCVSSFTA
FVKRERDLQG RPSSFFGMDR PPKLRDEF
