OFUT1_CAEEL
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 03-AUG-2022, entry version 130.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
DE EC=2.4.1.221 {ECO:0000269|PubMed:21966509};
DE AltName: Full=Peptide-O-fucosyltransferase 1;
DE Short=O-FucT-1;
DE Flags: Precursor;
GN ORFNames=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; FO080550; 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; -.
DR CAZy; GT65; Glycosyltransferase Family 65.
DR EPD; Q18014; -.
DR PaxDb; Q18014; -.
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 CTD; 180607; -.
DR WormBase; C15C7.7; CE36786; WBGene00015793; -.
DR eggNOG; KOG3202; Eukaryota.
DR eggNOG; KOG3849; Eukaryota.
DR GeneTree; ENSGT00390000015634; -.
DR HOGENOM; CLU_039551_0_0_1; -.
DR InParanoid; Q18014; -.
DR OMA; YPELCMP; -.
DR OrthoDB; 1127619at2759; -.
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 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 GO; GO:0008593; P:regulation of Notch signaling pathway; IBA:GO_Central.
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 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
