OFUT1_RAT
ID OFUT1_RAT Reviewed; 395 AA.
AC Q6EV70;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
DE EC=2.4.1.221 {ECO:0000269|PubMed:9023546};
DE AltName: Full=Peptide-O-fucosyltransferase 1;
DE Short=O-FucT-1;
DE Flags: Precursor;
GN Name=Pofut1 {ECO:0000312|RGD:1303001}; Synonyms=Fut12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:CAH03711.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar {ECO:0000312|EMBL:CAH03711.1};
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).
RN [2]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY, AND
RP PATHWAY.
RX PubMed=9023546; DOI=10.1093/glycob/6.8.837;
RA Wang Y., Lee G.F., Kelley R.F., Spellman M.W.;
RT "Identification of a GDP-L-fucose:polypeptide fucosyltransferase and
RT enzymatic addition of O-linked fucose to EGF domains.";
RL Glycobiology 6:837-842(1996).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=15653671; DOI=10.1074/jbc.m414574200;
RA Luo Y., Haltiwanger R.S.;
RT "O-fucosylation of notch occurs in the endoplasmic reticulum.";
RL J. Biol. Chem. 280:11289-11294(2005).
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. Fucosylates AGRN and
CC determines its ability to cluster acetylcholine receptors (AChRs) (By
CC similarity). Plays a crucial role in NOTCH signaling. Initial
CC fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG,
CC an acetylglucosaminyltransferase that can then extend the fucosylation
CC on the NOTCH EGF repeats. This extended fucosylation is required for
CC optimal ligand binding and canonical NOTCH signaling induced by DLL1 or
CC JAGGED1. {ECO:0000250, ECO:0000269|PubMed:15653671,
CC ECO:0000269|PubMed:9023546}.
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:0000269|PubMed:9023546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:9023546};
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:0000269|PubMed:9023546};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:9023546};
CC -!- ACTIVITY REGULATION: Activated by manganese and, to a lesser extent, by
CC calcium. {ECO:0000269|PubMed:9023546}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:15653671, ECO:0000269|PubMed:9023546}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:15653671}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P83337}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 65 family.
CC {ECO:0000255}.
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DR EMBL; AJ781499; CAH03711.1; -; mRNA.
DR RefSeq; NP_001002278.1; NM_001002278.1.
DR AlphaFoldDB; Q6EV70; -.
DR SMR; Q6EV70; -.
DR STRING; 10116.ENSRNOP00000013730; -.
DR CAZy; GT65; Glycosyltransferase Family 65.
DR GlyGen; Q6EV70; 2 sites.
DR jPOST; Q6EV70; -.
DR PaxDb; Q6EV70; -.
DR PRIDE; Q6EV70; -.
DR Ensembl; ENSRNOT00000013730; ENSRNOP00000013730; ENSRNOG00000010104.
DR GeneID; 311551; -.
DR KEGG; rno:311551; -.
DR UCSC; RGD:1303001; rat.
DR CTD; 23509; -.
DR RGD; 1303001; Pofut1.
DR eggNOG; KOG3849; Eukaryota.
DR GeneTree; ENSGT00390000015634; -.
DR HOGENOM; CLU_039551_0_0_1; -.
DR InParanoid; Q6EV70; -.
DR OMA; QRFPPKE; -.
DR OrthoDB; 1127619at2759; -.
DR PhylomeDB; Q6EV70; -.
DR TreeFam; TF314805; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6EV70; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000010104; Expressed in liver and 19 other tissues.
DR Genevisible; Q6EV70; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0036066; P:protein O-linked fucosylation; ISO:RGD.
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; ISO:RGD.
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 1: Evidence at protein 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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..395
FT /note="GDP-fucose protein O-fucosyltransferase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012151"
FT MOTIF 392..395
FT /note="Prevents secretion from ER"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 245..247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT BINDING 364..365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..47
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT DISULFID 133..147
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT DISULFID 256..290
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
FT DISULFID 274..361
FT /evidence="ECO:0000250|UniProtKB:Q9H488"
SQ SEQUENCE 395 AA; 44983 MW; 2A85521E22F38920 CRC64;
MGAAAWAPSH LLLRASFLLL LLLLPLPLRG RAGGSWDLAG YLLYCPCMGR FGNQADHFLG
SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA
PFHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS
YKEQWIQRFP PKEHPVLALP GAPAQFPVLE EHRELQKYMV WSDEMVRTGE AQISTHLVRP
YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TATPLTTTMC LPDLKEIQRA
VKLWVRALDA RSVYIATDSE SYVSEIQQLF KEKVKVVSLK PEVAQIDLYI LGQADHFIGN
CVSSFTAFVK RERDLHGRPS SFFGMDRPSQ LRDEF
