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   27-MAR-2024, entry version 188.
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;
CC       Note=Peptide-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; 52.
DR   IntAct; Q9H488; 7.
DR   STRING; 9606.ENSP00000364902; -.
DR   CAZy; GT65; Glycosyltransferase Family 65.
DR   GlyConnect; 1266; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q9H488; 2 sites, 1 glycan.
DR   GlyGen; Q9H488; 3 sites, 1 N-linked glycan (1 site), 1 O-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; 9606-ENSP00000364902; -.
DR   PeptideAtlas; Q9H488; -.
DR   ProteomicsDB; 80793; -. [Q9H488-1]
DR   ProteomicsDB; 80794; -. [Q9H488-2]
DR   Pumba; Q9H488; -.
DR   Antibodypedia; 25350; 254 antibodies from 31 providers.
DR   DNASU; 23509; -.
DR   Ensembl; ENST00000375730.3; ENSP00000364882.3; ENSG00000101346.15. [Q9H488-2]
DR   Ensembl; ENST00000375749.8; ENSP00000364902.3; ENSG00000101346.15. [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   AGR; HGNC:14988; -.
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; KWQAKYP; -.
DR   OrthoDB; 5384121at2759; -.
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; 21 hits in 1159 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 98 other cell types or tissues.
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:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:UniProtKB.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
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:SF3; GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 1; 1.
DR   Pfam; PF10250; O-FucT; 1.
DR   Genevisible; Q9H488; HS.
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
//