FUT8_CAEEL
ID FUT8_CAEEL Reviewed; 559 AA.
AC G5EFE7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Alpha-(1,6)-fucosyltransferase {ECO:0000255|PIRNR:PIRNR000472};
DE Short=Alpha1-6FucT {ECO:0000250|UniProtKB:Q9BYC5};
DE EC=2.4.1.68 {ECO:0000255|PIRNR:PIRNR000472, ECO:0000269|PubMed:15604090};
DE AltName: Full=Fucosyltransferase 8 {ECO:0000312|WormBase:C10F3.6};
DE AltName: Full=GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase {ECO:0000250|UniProtKB:Q9BYC5};
DE AltName: Full=GDP-fucose--glycoprotein fucosyltransferase {ECO:0000250|UniProtKB:Q9BYC5};
DE AltName: Full=Glycoprotein 6-alpha-L-fucosyltransferase {ECO:0000250|UniProtKB:Q9BYC5};
GN Name=fut-8 {ECO:0000312|WormBase:C10F3.6};
GN ORFNames=C10F3.6 {ECO:0000312|WormBase:C10F3.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:CAD54736.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Balanzino L., Oriol R., Michalski J.C., Candelier J.J.,
RA Martinez-Duncker I., Mollicone R.;
RT "Cloning, expression and genomic organization of two core
RT fucosyltransferases (CeE and CeD) from Caenorhabditis elegans.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15604090; DOI=10.1093/glycob/cwi028;
RA Paschinger K., Staudacher E., Stemmer U., Fabini G., Wilson I.B.;
RT "Fucosyltransferase substrate specificity and the order of fucosylation in
RT invertebrates.";
RL Glycobiology 15:463-474(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
RA Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K., Noebauer K.,
RA Guo X., Seeberger P.H., Wilson I.B., Aebi M., Hengartner M.O., Kuenzler M.;
RT "Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity
RT towards nematotoxic fungal galectin CGL2.";
RL PLoS Pathog. 6:E1000717-E1000717(2010).
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 (PubMed:15604090). The addition is prevented if the GlcNAc residue is
CC already fucosylated (PubMed:15604090). Involved in susceptibility to
CC the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the
CC synthesis of core alpha-1,6-fucosylated N-glycans to which Cgl2 binds
CC (PubMed:20062796). {ECO:0000255|PIRNR:PIRNR000472,
CC ECO:0000269|PubMed:15604090, ECO:0000269|PubMed:20062796}.
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:0000255|PIRNR:PIRNR000472,
CC ECO:0000269|PubMed:15604090};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15604090};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15604090};
CC Note=May also use Ca(2+). The enzyme has substantial activity without
CC divalent cations. {ECO:0000269|PubMed:15604090};
CC -!- ACTIVITY REGULATION: Inhibited by Fe(3+), Ni(2+) and Cu(2+).
CC {ECO:0000269|PubMed:15604090}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7.5. {ECO:0000269|PubMed:15604090};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|PIRNR:PIRNR000472}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000255|PIRNR:PIRNR000472}; Single-pass type II membrane protein
CC {ECO:0000305}. Note=Membrane-bound form in trans cisternae of Golgi.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC {ECO:0000255|PIRNR:PIRNR000472}.
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DR EMBL; AJ512486; CAD54736.1; -; mRNA.
DR EMBL; BX284605; CCD64126.1; -; Genomic_DNA.
DR RefSeq; NP_504555.2; NM_072154.5.
DR AlphaFoldDB; G5EFE7; -.
DR SMR; G5EFE7; -.
DR IntAct; G5EFE7; 3.
DR STRING; 6239.C10F3.6; -.
DR EPD; G5EFE7; -.
DR PaxDb; G5EFE7; -.
DR PeptideAtlas; G5EFE7; -.
DR EnsemblMetazoa; C10F3.6.1; C10F3.6.1; WBGene00001508.
DR EnsemblMetazoa; C10F3.6.2; C10F3.6.2; WBGene00001508.
DR GeneID; 178985; -.
DR KEGG; cel:CELE_C10F3.6; -.
DR CTD; 178985; -.
DR WormBase; C10F3.6; CE32580; WBGene00001508; fut-8.
DR eggNOG; KOG3705; Eukaryota.
DR GeneTree; ENSGT00530000063737; -.
DR HOGENOM; CLU_021940_1_0_1; -.
DR InParanoid; G5EFE7; -.
DR OMA; TYCAITA; -.
DR OrthoDB; 1290594at2759; -.
DR PhylomeDB; G5EFE7; -.
DR Reactome; R-CEL-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR PRO; PR:G5EFE7; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001508; Expressed in larva and 3 other tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046921; F:alpha-(1->6)-fucosyltransferase activity; IDA:WormBase.
DR GO; GO:0008417; F:fucosyltransferase activity; IGI:UniProtKB.
DR GO; GO:0046702; F:galactoside 6-L-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008424; F:glycoprotein 6-alpha-L-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0036071; P:N-glycan fucosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:WormBase.
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 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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW SH3 domain; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="Alpha-(1,6)-fucosyltransferase"
FT /id="PRO_0000438179"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..559
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 190..480
FT /note="GT23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT DOMAIN 489..550
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 63..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..352
FT /note="Important for donor substrate binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00992"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 188..251
FT /evidence="ECO:0000250|UniProtKB:Q9BYC5"
FT DISULFID 196..214
FT /evidence="ECO:0000250|UniProtKB:Q9BYC5"
FT DISULFID 202..206
FT /evidence="ECO:0000250|UniProtKB:Q9BYC5"
FT DISULFID 452..459
FT /evidence="ECO:0000250|UniProtKB:Q9BYC5"
SQ SEQUENCE 559 AA; 63649 MW; BBF6F1944A9BEF9F CRC64;
MLKCIAAVGT VVWMTMFLFL YSQLSNNQSG GDSIRAWRQT KEAIDKLQEQ NEDLKSILEK
ERQERNDQHK KIMEQSHQLP PNPENPSLPK PEPVKEIISK PSILGPVQQE VQKRMLDDRI
REMFYLLHSQ TIENSTKILL ETQMISLMGL SAQLEKLEGS EEERFKQRTA ITQRIFKSIE
KLQNPKACSE AKTLVCNLDK ECGFGCQLHH VTYCAITAFA TQRMMVLKRD GSSWKYSSHG
WTSVFKKLSK CSFDEAVGNT EAKPFAEPSP ARVVSLGIVD SLITKPTFLP QAVPEQLLES
LTSLHSHPPA FFVGTFISYL MRFNSATQEK LDKALKSIPL DKGPIVGLQI RRTDKVGTEA
AFHALKEYME WTEIWFKVEE KRQGKPLERR IFIASDDPTV VPEAKNDYPN YEVYGSTEIA
KTAQLNNRYT DASLMGVITD IYILSKVNYL VCTFSSQVCR MGYELRQPSG ADDGSKFHSL
DDIYYFGGQQ AHEVIVIEDH IAQNNKEIDL KVGDKVGIAG NHWNGYSKGT NRQTYKEGVF
PSYKVVNDWR KFKFEALLD
