ID OFUT1_CAEEL Reviewed; 389 AA. AC Q18014; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 5. DT 27-MAR-2024, entry version 137. DE RecName: Full=GDP-fucose protein O-fucosyltransferase 1 {ECO:0000305}; DE EC=2.4.1.221 {ECO:0000269|PubMed:21966509}; DE AltName: Full=Peptide-O-fucosyltransferase 1 {ECO:0000305}; DE Short=O-FucT-1 {ECO:0000305}; DE AltName: Full=Protein O-fucosyltransferase 1 {ECO:0000312|WormBase:C15C7.7}; DE Flags: Precursor; GN Name=pfut-1 {ECO:0000312|WormBase:C15C7.7}; GN ORFNames=C15C7.7 {ECO:0000312|WormBase:C15C7.7}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] {ECO:0000305} RP HOMOLOGY. RX PubMed=11524432; DOI=10.1074/jbc.m107849200; RA Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., RA Haltiwanger R.S.; RT "Modification of epidermal growth factor-like repeats with O-fucose: RT molecular cloning and expression of a novel GDP-fucose protein O- RT fucosyltransferase."; RL J. Biol. Chem. 276:40338-40345(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 26-383 IN COMPLEX WITH GDP-FUCOSE RP AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, DISULFIDE RP BONDS, AND MUTAGENESIS OF ASN-43 AND ARG-240. RX PubMed=21966509; DOI=10.1371/journal.pone.0025365; RA Lira-Navarrete E., Valero-Gonzalez J., Villanueva R., Martinez-Julvez M., RA Tejero T., Merino P., Panjikar S., Hurtado-Guerrero R.; RT "Structural insights into the mechanism of protein O-fucosylation."; RL PLoS ONE 6:E25365-E25365(2011). 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 (PubMed:21966509). CC Specifically uses GDP-fucose as donor substrate and proper disulfide CC pairing of the substrate EGF domains is required for fucose transfer CC (By similarity). {ECO:0000250|UniProtKB:Q9H488, CC ECO:0000269|PubMed:21966509}. 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:21966509}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645; CC Evidence={ECO:0000269|PubMed:21966509}; 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:21966509}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492; CC Evidence={ECO:0000269|PubMed:21966509}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:21966509}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21966509}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q6EV70}. CC -!- MISCELLANEOUS: Manganese is bound to the substrate GDP-fucose, but is CC not required for enzyme activity. {ECO:0000269|PubMed:21966509}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 65 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284606; CCD64591.1; -; Genomic_DNA. DR RefSeq; NP_741744.2; NM_171649.6. DR PDB; 3ZY2; X-ray; 1.54 A; A=26-383. DR PDB; 3ZY3; X-ray; 1.86 A; A/B=26-383. DR PDB; 3ZY4; X-ray; 1.74 A; A=26-383. DR PDB; 3ZY5; X-ray; 1.96 A; A=26-383. DR PDB; 3ZY6; X-ray; 1.91 A; A=26-383. DR PDBsum; 3ZY2; -. DR PDBsum; 3ZY3; -. DR PDBsum; 3ZY4; -. DR PDBsum; 3ZY5; -. DR PDBsum; 3ZY6; -. DR AlphaFoldDB; Q18014; -. DR SMR; Q18014; -. DR BioGRID; 45548; 1. DR STRING; 6239.C15C7.7.1; -. DR CAZy; GT65; Glycosyltransferase Family 65. DR EPD; Q18014; -. DR PaxDb; 6239-C15C7-7; -. DR PeptideAtlas; Q18014; -. DR EnsemblMetazoa; C15C7.7.1; C15C7.7.1; WBGene00015793. DR GeneID; 180607; -. DR KEGG; cel:CELE_C15C7.7; -. DR UCSC; C15C7.7; c. elegans. DR AGR; WB:WBGene00015793; -. DR WormBase; C15C7.7; CE36786; WBGene00015793; pfut-1. DR eggNOG; KOG3202; Eukaryota. DR eggNOG; KOG3849; Eukaryota. DR GeneTree; ENSGT00390000015634; -. DR HOGENOM; CLU_039551_0_0_1; -. DR InParanoid; Q18014; -. DR OMA; KWQAKYP; -. DR OrthoDB; 5384121at2759; -. DR PhylomeDB; Q18014; -. DR BRENDA; 2.4.1.221; 1045. DR UniPathway; UPA00378; -. DR EvolutionaryTrace; Q18014; -. DR PRO; PR:Q18014; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00015793; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:WormBase. DR GO; GO:0008417; F:fucosyltransferase activity; ISS:UniProtKB. DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:WormBase. DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0036066; P:protein O-linked fucosylation; IDA:WormBase. DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB. DR CDD; cd11302; O-FucT-1; 1. DR Gene3D; 3.40.50.11340; -; 1. DR Gene3D; 3.40.50.11350; -; 1. DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase. DR InterPro; IPR039922; POFUT1. DR PANTHER; PTHR21420; GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 1; 1. DR PANTHER; PTHR21420:SF10; GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 1; 1. DR Pfam; PF10250; O-FucT; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Disulfide bond; KW Endoplasmic reticulum; Fucose metabolism; Glycoprotein; KW Glycosyltransferase; Manganese; Notch signaling pathway; KW Reference proteome; Signal; Transferase. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..389 FT /note="GDP-fucose protein O-fucosyltransferase 1" FT /id="PRO_0000012152" FT BINDING 40..43 FT /ligand="substrate" FT /evidence="ECO:0007744|PDB:3ZY2, ECO:0007744|PDB:3ZY3, FT ECO:0007744|PDB:3ZY5, ECO:0007744|PDB:3ZY6" FT BINDING 238..240 FT /ligand="substrate" FT /evidence="ECO:0007744|PDB:3ZY2, ECO:0007744|PDB:3ZY3, FT ECO:0007744|PDB:3ZY5, ECO:0007744|PDB:3ZY6" FT BINDING 356..357 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:21966509, FT ECO:0007744|PDB:3ZY2, ECO:0007744|PDB:3ZY3, FT ECO:0007744|PDB:3ZY5, ECO:0007744|PDB:3ZY6" FT CARBOHYD 24 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305" FT DISULFID 35..37 FT /evidence="ECO:0000269|PubMed:21966509" FT DISULFID 119..135 FT /evidence="ECO:0000269|PubMed:21966509" FT DISULFID 249..281 FT /evidence="ECO:0000269|PubMed:21966509" FT DISULFID 266..353 FT /evidence="ECO:0000269|PubMed:21966509" FT MUTAGEN 43 FT /note="N->A: Reduces enzyme activity by over 90%." FT /evidence="ECO:0000269|PubMed:21966509" FT MUTAGEN 240 FT /note="R->A,K: Abolishes enzyme activity." FT /evidence="ECO:0000269|PubMed:21966509" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 41..58 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 86..89 FT /evidence="ECO:0007829|PDB:3ZY2" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 143..149 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:3ZY2" FT TURN 164..167 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:3ZY6" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:3ZY2" FT TURN 184..186 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 188..194 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 216..229 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 232..239 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 243..250 FT /evidence="ECO:0007829|PDB:3ZY2" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:3ZY2" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 264..267 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 278..281 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 285..299 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 302..310 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 314..321 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 336..345 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 346..351 FT /evidence="ECO:0007829|PDB:3ZY2" FT HELIX 356..367 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 368..371 FT /evidence="ECO:0007829|PDB:3ZY2" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:3ZY2" SQ SEQUENCE 389 AA; 44051 MW; 0C84F202AA184554 CRC64; MRVSKVLTLA SFISVCSYSE AKSNETDPNG YIVFCPCMGR FGNQVDQFLG VLAFAKALDR TLVLPNFIEF KHPETKMIPF EFLFQVGTVA KYTRVVTMQE FTKKIMPTVW PPEKRKAFCW TPRQAIYDKS AEPGCHSKEG NPFGPYWDQI DVSFVGDEYF GDIPGGFDLN QMGSRKKWLE KFPSEEYPVL AFSSAPAPFP SKGKVWSIQK YLRWSSRITE QAKKFISANL AKPFVAVHLR NDADWVRVCE HIDTTTNRPL FASEQCLGEG HHLGTLTKEI CSPSKQQILE QIVEKVGSIG AKSVFVASDK DHMIDEINEA LKPYEIEAHR QEPDDMYTSL AIMGRADLFV GNCVSTFSHI VKRERDHAGQ SPRPSAFFGI RAVKRHIDL //