FUT8_HUMAN
ID FUT8_HUMAN Reviewed; 575 AA.
AC Q9BYC5; B4DFS7; G3V5N0; O00235; Q8IUA5; Q9BYC6; Q9P2U5; Q9P2U6;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase;
DE Short=Alpha1-6FucT;
DE EC=2.4.1.68;
DE AltName: Full=Fucosyltransferase 8;
DE AltName: Full=GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase;
DE AltName: Full=GDP-fucose--glycoprotein fucosyltransferase;
DE AltName: Full=Glycoprotein 6-alpha-L-fucosyltransferase;
GN Name=FUT8;
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), AND FUNCTION.
RX PubMed=9133635; DOI=10.1093/oxfordjournals.jbchem.a021631;
RA Yanagidani S., Uozumi N., Ihara Y., Miyoshi E., Yamaguchi N., Taniguchi N.;
RT "Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-
RT glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human
RT gastric cancer MKN45 cells.";
RL J. Biochem. 121:626-632(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RA Cailleau A., Balanzino L., Candelier J.J., Oriol R., Mollicone R.;
RT "Differential splice variants of human FUT8 embryonic cDNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10814706; DOI=10.1093/glycob/10.6.637;
RA Yamaguchi Y., Ikeda Y., Takahashi T., Ihara H., Tanaka T., Sasho C.,
RA Uozumi N., Yanagidani S., Inoue S., Fujii J., Taniguchi N.;
RT "Genomic structure and promoter analysis of the human alpha1,6-
RT fucosyltransferase gene (FUT8).";
RL Glycobiology 10:637-643(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING.
RC TISSUE=Embryo;
RX PubMed=14514715; DOI=10.1093/glycob/cwh006;
RA Martinez-Duncker I., Michalski J.C., Bauvy C., Candelier J.J.,
RA Mennesson B., Codogno P., Oriol R., Mollicone R.;
RT "Activity and tissue distribution of splice variants of alpha6-
RT fucosyltransferase in human embryogenesis.";
RL Glycobiology 14:13-25(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lung;
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 DONOR SUBSTRATE-BINDING, AND MUTAGENESIS OF ARG-365 AND ARG-366.
RX PubMed=10764839; DOI=10.1093/glycob/10.5.503;
RA Takahashi T., Ikeda Y., Tateishi A., Yamaguchi Y., Ishikawa M.,
RA Taniguchi N.;
RT "A sequence motif involved in the donor substrate binding by alpha1,6-
RT fucosyltransferase: the role of the conserved arginine residues.";
RL Glycobiology 10:503-510(2000).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M.,
RA Dixon J.E., Yeo C.Y., Whitman M.;
RT "A secreted tyrosine kinase acts in the extracellular environment.";
RL Cell 158:1033-1044(2014).
RN [10]
RP INVOLVEMENT IN CDGF1, VARIANTS CDGF1 239-ARG--LYS-575 DEL; 315-ARG--LYS-557
RP DEL AND GLY-337, FUNCTION, AND CHARACTERIZATION OF VARIANTS CDGF1
RP 239-ARG--LYS-575 DEL; 315-ARG--LYS-557? DEL AND GLY-337.
RX PubMed=29304374; DOI=10.1016/j.ajhg.2017.12.009;
RA Ng B.G., Xu G., Chandy N., Steyermark J., Shinde D.N., Radtke K.,
RA Raymond K., Lebrilla C.B., AlAsmari A., Suchy S.F., Powis Z., Faqeih E.A.,
RA Berry S.A., Kronn D.F., Freeze H.H.;
RT "Biallelic Mutations in FUT8 Cause a Congenital Disorder of Glycosylation
RT with Defective Fucosylation.";
RL Am. J. Hum. Genet. 102:188-195(2018).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 68-575, FUNCTION, CATALYTIC
RP ACTIVITY, DISULFIDE BOND, AND MUTAGENESIS OF ARG-365; ASP-368; LYS-369;
RP GLU-373; TYR-382; ASP-409; ASP-410; ASP-453 AND SER-469.
RX PubMed=17172260; DOI=10.1093/glycob/cwl079;
RA Ihara H., Ikeda Y., Toma S., Wang X., Suzuki T., Gu J., Miyoshi E.,
RA Tsukihara T., Honke K., Matsumoto A., Nakagawa A., Taniguchi N.;
RT "Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8.";
RL Glycobiology 17:455-466(2007).
RN [12]
RP VARIANT CDGF1 315-ARG--LYS-575 DEL.
RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT "Autozygome and high throughput confirmation of disease genes candidacy.";
RL Genet. Med. 21:736-742(2019).
CC -!- FUNCTION: Catalyzes the addition of fucose in alpha 1-6 linkage to the
CC first GlcNAc residue, next to the peptide chains in N-glycans.
CC {ECO:0000269|PubMed:17172260, ECO:0000269|PubMed:29304374,
CC ECO:0000269|PubMed:9133635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = GDP +
CC H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-
CC [alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein];
CC Xref=Rhea:RHEA:12985, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:13532,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:60651, ChEBI:CHEBI:137207; EC=2.4.1.68;
CC Evidence={ECO:0000269|PubMed:17172260};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q9BYC5; Q96DT7-3: ZBTB10; NbExp=3; IntAct=EBI-2869363, EBI-12017160;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BYC5-1; Sequence=Displayed;
CC Name=2; Synonyms=Retinal;
CC IsoId=Q9BYC5-2; Sequence=VSP_001807, VSP_001808;
CC Name=3;
CC IsoId=Q9BYC5-3; Sequence=VSP_046837;
CC Name=4; Synonyms=Retina-1, Retina-2;
CC IsoId=Q9BYC5-4; Sequence=VSP_053361, VSP_053362;
CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000269|PubMed:25171405}.
CC -!- DISEASE: Congenital disorder of glycosylation with defective
CC fucosylation 1 (CDGF1) [MIM:618005]: A form of congenital disorder of
CC glycosylation, a genetically heterogeneous group of multisystem
CC disorders caused by a defect in glycoprotein biosynthesis and
CC characterized by under-glycosylated serum glycoproteins. Congenital
CC disorders of glycosylation result in a wide variety of clinical
CC features, such as defects in the nervous system development,
CC psychomotor retardation, dysmorphic features, hypotonia, coagulation
CC disorders, and immunodeficiency. The broad spectrum of features
CC reflects the critical role of N-glycoproteins during embryonic
CC development, differentiation, and maintenance of cell functions. CDGF1
CC is an autosomal recessive disorder, apparent from birth, characterized
CC by poor growth, failure to thrive, hypotonia, skeletal anomalies, and
CC delayed psychomotor development with intellectual disability.
CC {ECO:0000269|PubMed:29304374, ECO:0000269|PubMed:30237576}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 4]: Seems to be only expressed in retina,
CC inactive as a fucosyltransferase. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00992}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 8;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_605";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FUT8ID40649ch14q23.html";
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DR EMBL; D89289; BAA19764.1; -; mRNA.
DR EMBL; AH005745; AAB92372.2; -; Genomic_DNA.
DR EMBL; Y17979; CAA76988.1; -; mRNA.
DR EMBL; Y17976; CAA76985.1; -; mRNA.
DR EMBL; Y17977; CAA76986.1; -; mRNA.
DR EMBL; Y17978; CAA76987.1; -; mRNA.
DR EMBL; AB049828; BAB40975.1; -; Genomic_DNA.
DR EMBL; AB049740; BAB40929.2; -; mRNA.
DR EMBL; AB032573; BAA92859.2; -; Genomic_DNA.
DR EMBL; AB032573; BAA92858.1; -; Genomic_DNA.
DR EMBL; AJ514324; CAD55804.1; -; mRNA.
DR EMBL; AJ514325; CAD55805.1; -; mRNA.
DR EMBL; AK294242; BAG57538.1; -; mRNA.
DR EMBL; AL109847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093889; AAH93889.1; -; mRNA.
DR EMBL; BC101816; AAI01817.1; -; mRNA.
DR CCDS; CCDS9775.1; -. [Q9BYC5-1]
DR CCDS; CCDS9776.2; -. [Q9BYC5-3]
DR PIR; JC5432; JC5432.
DR RefSeq; NP_004471.4; NM_004480.4. [Q9BYC5-3]
DR RefSeq; NP_835368.1; NM_178155.2. [Q9BYC5-1]
DR RefSeq; NP_835369.1; NM_178156.2. [Q9BYC5-1]
DR PDB; 2DE0; X-ray; 2.61 A; X=68-575.
DR PDB; 6VLD; X-ray; 2.28 A; A/B/G/H=105-575.
DR PDB; 6VLE; X-ray; 2.28 A; A/B=105-575.
DR PDB; 6X5H; X-ray; 2.25 A; A/B/C/D=41-575.
DR PDB; 6X5R; X-ray; 2.40 A; A/B=41-575.
DR PDB; 6X5S; X-ray; 3.30 A; A/B=108-573.
DR PDB; 6X5T; X-ray; 2.47 A; A/B/C/D/E/F/G/H=41-575.
DR PDB; 6X5U; X-ray; 3.20 A; A/B/C/D/E/F/G/H=41-575.
DR PDBsum; 2DE0; -.
DR PDBsum; 6VLD; -.
DR PDBsum; 6VLE; -.
DR PDBsum; 6X5H; -.
DR PDBsum; 6X5R; -.
DR PDBsum; 6X5S; -.
DR PDBsum; 6X5T; -.
DR PDBsum; 6X5U; -.
DR AlphaFoldDB; Q9BYC5; -.
DR SMR; Q9BYC5; -.
DR BioGRID; 108806; 173.
DR IntAct; Q9BYC5; 32.
DR MINT; Q9BYC5; -.
DR STRING; 9606.ENSP00000353910; -.
DR ChEMBL; CHEMBL3596087; -.
DR CAZy; GT23; Glycosyltransferase Family 23.
DR iPTMnet; Q9BYC5; -.
DR PhosphoSitePlus; Q9BYC5; -.
DR BioMuta; FUT8; -.
DR DMDM; 20138326; -.
DR EPD; Q9BYC5; -.
DR jPOST; Q9BYC5; -.
DR MassIVE; Q9BYC5; -.
DR MaxQB; Q9BYC5; -.
DR PaxDb; Q9BYC5; -.
DR PeptideAtlas; Q9BYC5; -.
DR PRIDE; Q9BYC5; -.
DR ProteomicsDB; 33572; -.
DR ProteomicsDB; 70528; -.
DR ProteomicsDB; 79611; -. [Q9BYC5-1]
DR ProteomicsDB; 79612; -. [Q9BYC5-2]
DR Antibodypedia; 24748; 251 antibodies from 28 providers.
DR DNASU; 2530; -.
DR Ensembl; ENST00000342677.10; ENSP00000345865.6; ENSG00000033170.17. [Q9BYC5-2]
DR Ensembl; ENST00000360689.9; ENSP00000353910.5; ENSG00000033170.17. [Q9BYC5-1]
DR Ensembl; ENST00000394586.6; ENSP00000378087.2; ENSG00000033170.17. [Q9BYC5-1]
DR Ensembl; ENST00000557164.5; ENSP00000452433.1; ENSG00000033170.17. [Q9BYC5-3]
DR Ensembl; ENST00000673929.1; ENSP00000501213.1; ENSG00000033170.17. [Q9BYC5-1]
DR GeneID; 2530; -.
DR KEGG; hsa:2530; -.
DR MANE-Select; ENST00000673929.1; ENSP00000501213.1; NM_001371533.1; NP_001358462.1.
DR UCSC; uc001xin.3; human. [Q9BYC5-1]
DR CTD; 2530; -.
DR DisGeNET; 2530; -.
DR GeneCards; FUT8; -.
DR HGNC; HGNC:4019; FUT8.
DR HPA; ENSG00000033170; Tissue enhanced (brain).
DR MalaCards; FUT8; -.
DR MIM; 602589; gene.
DR MIM; 618005; phenotype.
DR neXtProt; NX_Q9BYC5; -.
DR OpenTargets; ENSG00000033170; -.
DR PharmGKB; PA28435; -.
DR VEuPathDB; HostDB:ENSG00000033170; -.
DR eggNOG; KOG3705; Eukaryota.
DR GeneTree; ENSGT00530000063737; -.
DR HOGENOM; CLU_021940_1_0_1; -.
DR InParanoid; Q9BYC5; -.
DR OMA; GGQNPHN; -.
DR PhylomeDB; Q9BYC5; -.
DR TreeFam; TF106108; -.
DR BioCyc; MetaCyc:HS00491-MON; -.
DR BRENDA; 2.4.1.68; 2681.
DR PathwayCommons; Q9BYC5; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR SignaLink; Q9BYC5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2530; 29 hits in 1076 CRISPR screens.
DR ChiTaRS; FUT8; human.
DR EvolutionaryTrace; Q9BYC5; -.
DR GeneWiki; FUT8; -.
DR GenomeRNAi; 2530; -.
DR Pharos; Q9BYC5; Tbio.
DR PRO; PR:Q9BYC5; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BYC5; protein.
DR Bgee; ENSG00000033170; Expressed in corpus callosum and 204 other tissues.
DR ExpressionAtlas; Q9BYC5; baseline and differential.
DR Genevisible; Q9BYC5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; NAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0046921; F:alpha-(1->6)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0046368; P:GDP-L-fucose metabolic process; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0036071; P:N-glycan fucosylation; IBA:GO_Central.
DR GO; GO:0006491; P:N-glycan processing; TAS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:ProtInc.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR GO; GO:0043112; P:receptor metabolic process; IEA:Ensembl.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR CDD; cd11792; SH3_Fut8; 1.
DR InterPro; IPR015827; Fut8.
DR InterPro; IPR045573; Fut8_N_cat.
DR InterPro; IPR035653; Fut8_SH3.
DR InterPro; IPR027350; GT23_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF19745; FUT8_N_cat; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF000472; Alpha1_6FUT_euk; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51659; GT23; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Congenital disorder of glycosylation;
KW Disease variant; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain; SH3-binding;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..575
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000080526"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..575
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 206..493
FT /note="GT23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT DOMAIN 502..563
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 365..366
FT /note="Important for donor substrate binding"
FT MOTIF 299..305
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTS2"
FT DISULFID 204..266
FT /evidence="ECO:0000269|PubMed:17172260"
FT DISULFID 212..230
FT /evidence="ECO:0000269|PubMed:17172260"
FT DISULFID 218..222
FT /evidence="ECO:0000269|PubMed:17172260"
FT DISULFID 465..472
FT /evidence="ECO:0000269|PubMed:17172260"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046837"
FT VAR_SEQ 1..14
FT /note="MRPWTGSWRWIMLI -> MHRQIWHLHWTLVR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14514715,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_053361"
FT VAR_SEQ 15..420
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14514715,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_053362"
FT VAR_SEQ 280..329
FT /note="EVKDKNVQVVELPIVDSLHPRPPYLPLAVPEDLADRLVRVHGDPAVWWVS
FT -> TPIMNLLVITLFPGQLDCTIDTQKIHFVE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10814706"
FT /id="VSP_001807"
FT VAR_SEQ 330..575
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10814706"
FT /id="VSP_001808"
FT VARIANT 101
FT /note="K -> Q (in dbSNP:rs2229678)"
FT /id="VAR_054038"
FT VARIANT 239..575
FT /note="Missing (in CDGF1; drastic decrease of protein level
FT in patient's fibroblasts and complete loss of total core
FT fucosylated N-glycans in serum and fibroblasts compared to
FT controls)"
FT /evidence="ECO:0000269|PubMed:29304374"
FT /id="VAR_080978"
FT VARIANT 267
FT /note="T -> K (in dbSNP:rs35949016)"
FT /id="VAR_033537"
FT VARIANT 315..575
FT /note="Missing (in CDGF1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30237576"
FT /id="VAR_082143"
FT VARIANT 315..557
FT /note="Missing (in CDGF1; complete loss of total core
FT fucosylated N-glycans in patient's serum and fibroblasts
FT compared to controls)"
FT /evidence="ECO:0000269|PubMed:29304374"
FT /id="VAR_080979"
FT VARIANT 337
FT /note="R -> G (in CDGF1; drastic decrease of protein level
FT in patient's fibroblasts and complete loss of total core
FT fucosylated N-glycans in serum and fibroblasts compared to
FT controls)"
FT /evidence="ECO:0000269|PubMed:29304374"
FT /id="VAR_080980"
FT MUTAGEN 365
FT /note="R->A,K: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10764839,
FT ECO:0000269|PubMed:17172260"
FT MUTAGEN 366
FT /note="R->A,K: Decreases activity to 3%."
FT /evidence="ECO:0000269|PubMed:10764839"
FT MUTAGEN 368
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 369
FT /note="K->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 373
FT /note="E->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 382
FT /note="Y->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 409
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 410
FT /note="D->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 453
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT MUTAGEN 469
FT /note="S->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17172260"
FT CONFLICT 214
FT /note="I -> T (in Ref. 5; BAG57538)"
FT /evidence="ECO:0000305"
FT HELIX 110..137
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 142..172
FT /evidence="ECO:0007829|PDB:6X5H"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 176..199
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6X5H"
FT TURN 280..285
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:6X5H"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 379..396
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 400..409
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 413..420
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 430..435
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 444..459
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 536..544
FT /evidence="ECO:0007829|PDB:6X5H"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 549..554
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:6X5H"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6X5H"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:6X5H"
SQ SEQUENCE 575 AA; 66516 MW; 5AE24A93881E18D0 CRC64;
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL
RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY KKQTRNGLGK DHEILRRRIE
NGAKELWFFL QSELKKLKNL EGNELQRHAD EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR
EKEAKDLTEL VQRRITYLQN PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT
LILESQNWRY ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI
GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PSLLKEAKTK
YPNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ
TLHPDASANF HSLDDIYYFG GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS
KGVNRKLGRT GLYPSYKVRE KIETVKYPTY PEAEK
