OFUT1_HUMAN
ID OFUT1_HUMAN Reviewed; 388 AA.
AC Q9H488; A8K4R8; E1P5M4; Q14685; Q5W185; Q9BW76;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 1;
DE EC=2.4.1.221 {ECO:0000269|PubMed:11524432};
DE AltName: Full=Peptide-O-fucosyltransferase 1;
DE Short=O-FucT-1;
DE Flags: Precursor;
GN Name=POFUT1; Synonyms=FUT12, KIAA0180;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
RX PubMed=8358148; DOI=10.1093/glycob/3.3.219;
RA Harris R.J., Spellman M.W.;
RT "O-linked fucose and other post-translational modifications unique to EGF
RT modules.";
RL Glycobiology 3:219-224(1993).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INVOLVEMENT IN DDD2.
RX PubMed=23684010; DOI=10.1016/j.ajhg.2013.04.022;
RA Li M., Cheng R., Liang J., Yan H., Zhang H., Yang L., Li C., Jiao Q.,
RA Lu Z., He J., Ji J., Shen Z., Li C., Hao F., Yu H., Yao Z.;
RT "Mutations in POFUT1, encoding protein O-fucosyltransferase 1, cause
RT generalized Dowling-Degos disease.";
RL Am. J. Hum. Genet. 92:895-903(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13] {ECO:0007744|PDB:5UX6, ECO:0007744|PDB:5UXH}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 24-384 IN COMPLEX WITH
RP GDP-FUCOSE, FUNCTION IN NOTCH SIGNALING, GLYCOSYLATION AT ASN-62, DISULFIDE
RP BONDS, AND MUTAGENESIS OF ARG-240; MET-262; SER-356 AND ARG-366.
RX PubMed=28334865; DOI=10.1093/glycob/cwx020;
RA McMillan B.J., Zimmerman B., Egan E.D., Lofgren M., Xu X., Hesser A.,
RA Blacklow S.C.;
RT "Structure of human POFUT1, its requirement in ligand-independent oncogenic
RT Notch signaling, and functional effects of Dowling-Degos mutations.";
RL Glycobiology 2017:1-10(2017).
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:0000269|PubMed:11524432, ECO:0000269|PubMed:28334865,
CC ECO:0000269|PubMed:8358148}.
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:11524432};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:11524432};
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:11524432};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:11524432};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for F7 EGF domain {ECO:0000269|PubMed:11524432};
CC KM=4 uM for GDP-fucose {ECO:0000269|PubMed:11524432};
CC Vmax=3 umol/min/mg enzyme {ECO:0000269|PubMed:11524432};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11524432}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q6EV70}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H488-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H488-2; Sequence=VSP_001809;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, placenta, lung,
CC liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:11524432}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19159218}.
CC -!- DISEASE: Dowling-Degos disease 2 (DDD2) [MIM:615327]: An autosomal
CC dominant genodermatosis. Affected individuals develop a postpubertal
CC reticulate hyperpigmentation that is progressive and disfiguring, and
CC small hyperkeratotic dark brown papules that affect mainly the flexures
CC and great skin folds. Patients usually show no abnormalities of the
CC hair or nails. {ECO:0000269|PubMed:23684010}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 65 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Peptide-
CC O-fucosyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_609";
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DR EMBL; AF375884; AAL09576.1; -; mRNA.
DR EMBL; D80002; BAA11497.2; -; mRNA.
DR EMBL; AL121897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK291033; BAF83722.1; -; mRNA.
DR EMBL; CH471077; EAW76383.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76384.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76385.1; -; Genomic_DNA.
DR EMBL; BC000582; AAH00582.1; -; mRNA.
DR CCDS; CCDS13198.1; -. [Q9H488-1]
DR CCDS; CCDS13199.1; -. [Q9H488-2]
DR RefSeq; NP_056167.1; NM_015352.1. [Q9H488-1]
DR RefSeq; NP_758436.1; NM_172236.1. [Q9H488-2]
DR PDB; 5UX6; X-ray; 2.09 A; A/B=24-384.
DR PDB; 5UXH; X-ray; 2.41 A; A/B=24-384.
DR PDBsum; 5UX6; -.
DR PDBsum; 5UXH; -.
DR AlphaFoldDB; Q9H488; -.
DR SMR; Q9H488; -.
DR BioGRID; 117056; 45.
DR IntAct; Q9H488; 7.
DR STRING; 9606.ENSP00000364902; -.
DR CAZy; GT65; Glycosyltransferase Family 65.
DR GlyConnect; 1266; 1 N-Linked glycan (1 site).
DR GlyGen; Q9H488; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9H488; -.
DR MetOSite; Q9H488; -.
DR PhosphoSitePlus; Q9H488; -.
DR SwissPalm; Q9H488; -.
DR BioMuta; POFUT1; -.
DR DMDM; 23396787; -.
DR CPTAC; CPTAC-1506; -.
DR EPD; Q9H488; -.
DR jPOST; Q9H488; -.
DR MassIVE; Q9H488; -.
DR MaxQB; Q9H488; -.
DR PaxDb; Q9H488; -.
DR PeptideAtlas; Q9H488; -.
DR PRIDE; Q9H488; -.
DR ProteomicsDB; 80793; -. [Q9H488-1]
DR ProteomicsDB; 80794; -. [Q9H488-2]
DR Antibodypedia; 25350; 229 antibodies from 31 providers.
DR DNASU; 23509; -.
DR Ensembl; ENST00000375730.3; ENSP00000364882.3; ENSG00000101346.14. [Q9H488-2]
DR Ensembl; ENST00000375749.8; ENSP00000364902.3; ENSG00000101346.14. [Q9H488-1]
DR GeneID; 23509; -.
DR KEGG; hsa:23509; -.
DR MANE-Select; ENST00000375749.8; ENSP00000364902.3; NM_015352.2; NP_056167.1.
DR UCSC; uc002wxo.3; human. [Q9H488-1]
DR CTD; 23509; -.
DR DisGeNET; 23509; -.
DR GeneCards; POFUT1; -.
DR HGNC; HGNC:14988; POFUT1.
DR HPA; ENSG00000101346; Low tissue specificity.
DR MalaCards; POFUT1; -.
DR MIM; 607491; gene.
DR MIM; 615327; phenotype.
DR neXtProt; NX_Q9H488; -.
DR OpenTargets; ENSG00000101346; -.
DR Orphanet; 79145; Dowling-Degos disease.
DR PharmGKB; PA33495; -.
DR VEuPathDB; HostDB:ENSG00000101346; -.
DR eggNOG; KOG3849; Eukaryota.
DR GeneTree; ENSGT00390000015634; -.
DR HOGENOM; CLU_039551_0_0_1; -.
DR InParanoid; Q9H488; -.
DR OMA; YPELCMP; -.
DR OrthoDB; 1127619at2759; -.
DR PhylomeDB; Q9H488; -.
DR TreeFam; TF314805; -.
DR BRENDA; 2.4.1.221; 2681.
DR PathwayCommons; Q9H488; -.
DR Reactome; R-HSA-1912399; Pre-NOTCH Processing in the Endoplasmic Reticulum.
DR SignaLink; Q9H488; -.
DR SIGNOR; Q9H488; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 23509; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; POFUT1; human.
DR GenomeRNAi; 23509; -.
DR Pharos; Q9H488; Tbio.
DR PRO; PR:Q9H488; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H488; protein.
DR Bgee; ENSG00000101346; Expressed in stromal cell of endometrium and 96 other tissues.
DR Genevisible; Q9H488; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
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; NAS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:UniProtKB.
DR GO; GO:0036066; P:protein O-linked fucosylation; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS: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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism;
KW Disulfide bond; Endoplasmic reticulum; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Manganese; Notch signaling pathway;
KW 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_0000012148"
FT MOTIF 385..388
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT BINDING 43..46
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UXH"
FT BINDING 238..240
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UXH"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UXH"
FT BINDING 357..358
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UXH"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UX6"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 38..40
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UX6, ECO:0007744|PDB:5UXH"
FT DISULFID 126..140
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UX6, ECO:0007744|PDB:5UXH"
FT DISULFID 249..283
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UX6, ECO:0007744|PDB:5UXH"
FT DISULFID 267..354
FT /evidence="ECO:0000269|PubMed:28334865,
FT ECO:0007744|PDB:5UX6, ECO:0007744|PDB:5UXH"
FT VAR_SEQ 182..388
FT /note="FSPKEHPVLALPGAPAQFPVLEEHRPLQKYMVWSDEMVKTGEAQIHAHLVRP
FT YVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTAAPLTMTMCLPDLKEIQR
FT AVKLWVRSLDAQSVYVATDSESYVPELQQLFKGKVKVVSLKPEVAQVDLYILGQADHFI
FT GNCVSSFTAFVKRERDLQGRPSSFFGMDRPPKLRDEF -> RENHSCVTLLFPR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001809"
FT VARIANT 322
FT /note="L -> F (in dbSNP:rs17268666)"
FT /id="VAR_049231"
FT VARIANT 348
FT /note="D -> N (in dbSNP:rs35259534)"
FT /id="VAR_049232"
FT MUTAGEN 240
FT /note="R->A,C: Strongly impaired ability to activate NOTCH
FT signaling."
FT /evidence="ECO:0000269|PubMed:28334865"
FT MUTAGEN 262
FT /note="M->T: No effect on ability to activate NOTCH
FT signaling."
FT /evidence="ECO:0000269|PubMed:28334865"
FT MUTAGEN 356
FT /note="S->F: Abolishes ability to activate NOTCH
FT signaling."
FT /evidence="ECO:0000269|PubMed:28334865"
FT MUTAGEN 366
FT /note="R->W: Strongly impaired ability to activate NOTCH
FT signaling."
FT /evidence="ECO:0000269|PubMed:28334865"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5UXH"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5UX6"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:5UX6"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:5UX6"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:5UX6"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:5UX6"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5UX6"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5UX6"
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
