FUT6_GORGO
ID FUT6_GORGO Reviewed; 359 AA.
AC Q8HYJ6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6 {ECO:0000250|UniProtKB:P51993};
DE EC=2.4.1.152 {ECO:0000250|UniProtKB:P51993};
DE AltName: Full=Fucosyltransferase 6;
DE AltName: Full=Fucosyltransferase VI;
DE Short=Fuc-TVI;
DE Short=FucT-VI;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FUT6 {ECO:0000250|UniProtKB:P51993};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14718375; DOI=10.1093/glycob/cwh053;
RA Dupuy F., Germot A., Julien R., Maftah A.;
RT "Structure/function study of Lewis alpha3- and alpha3/4-
RT fucosyltransferases: the alpha1,4 fucosylation requires an aromatic residue
RT in the acceptor-binding domain.";
RL Glycobiology 14:347-356(2004).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a
CC distal alpha2,3 sialylated lactosamine unit of a glycoprotein- or
CC glycolipid-linked sialopolylactosamines chain or of a distal or
CC internal lactosamine unit of a neutral glycoprotein- or glycolipid-
CC linked polylactosamines chain through an alpha-1,3 glycosidic linkage
CC and participates in surface expression of the sialyl Lewis X (sLe(x)),
CC Lewis X (Le(x)) and non sialylated VIM2 determinants. Moreover
CC transfers fucose to H-type 2 (Fucalpha1-2Galbeta1-4GlcNAc) chain
CC acceptor substrates and participates in difucosylated sialyl Lewis x
CC determinants. Also fucosylates a polylactosamine substrate having a 6
CC sulfate modification at the GlcNAc moiety and gives rise to sialyl and
CC non-sialyl 6-sulfo lewis X. Does not have activity towards type 1
CC ((Galbeta1-3GlcNAc)) and H-type 1 chain (Fucalpha1-2Galbeta1-3GlcNAc)
CC acceptors substrates. {ECO:0000250|UniProtKB:P51993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941;
CC EC=2.4.1.152; Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-
CC L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-
CC (1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145342, ChEBI:CHEBI:145343;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90357, ChEBI:CHEBI:90360;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48369;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90357, ChEBI:CHEBI:90358;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48365;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90336, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48357;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62824, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60152,
CC ChEBI:CHEBI:62287; Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62825;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosamine = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosamine; Xref=Rhea:RHEA:62836,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145937, ChEBI:CHEBI:145938;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62837;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + lactose = beta-D-galactosyl-(1->4)-[alpha-
CC L-fucosyl-(1->3)]-D-glucose + GDP + H(+); Xref=Rhea:RHEA:62888,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90065;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62889;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose
CC = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-Glc +
CC GDP + H(+); Xref=Rhea:RHEA:64016, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:147155,
CC ChEBI:CHEBI:149659; Evidence={ECO:0000250|UniProtKB:P51993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64017;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-6-sulfooxy-
CC glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-
CC (1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-6-sulfooxy-
CC glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:64032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:149663, ChEBI:CHEBI:149664;
CC Evidence={ECO:0000250|UniProtKB:P51993};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P51993}.
CC -!- SUBUNIT: Homodimer and monomer. Monomer (secreted form).
CC {ECO:0000250|UniProtKB:P51993}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P51993}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P51993}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P51993}. Secreted
CC {ECO:0000250|UniProtKB:P51993}. Note=Membrane-bound form in trans
CC cisternae of Golgi. {ECO:0000250|UniProtKB:P51993}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P51993}.
CC -!- PTM: Proteolytic cleavage releases a secreted glycoform of 43 kDa.
CC {ECO:0000250|UniProtKB:P51993}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 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; AF515437; AAO15993.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8HYJ6; -.
DR STRING; 9593.ENSGGOP00000006122; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q8HYJ6; -.
DR BRENDA; 2.4.1.65; 2496.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036071; P:N-glycan fucosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase FUT6"
FT /id="PRO_0000221109"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..359
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 73..112
FT /note="determines site-specific fucosylation"
FT /evidence="ECO:0000250|UniProtKB:P51993"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 41688 MW; 17AB6435C22B616C CRC64;
MDPLGPAKPQ WSCRCCLTTL LFQLLVAVCF FSYLRVSRDD PTVYPNGSRF PDSTGTPARS
IPLILLWTWP FNKPTALPRC SEMLPGTADC NITADRKVYP QADAVIVHHR EVMYNPSAQL
PRSPRRQGQR WIWFSMESPS HCWQLKAMDG YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH
PPLNLSAKTE LVAWAVSGWG PNSARVRYYQ SLQAHLKVDV YGRSHKSLPQ GTMMETLSRY
KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD
LARYLQELDK DHARYLSYFG WRETLRPRSF SWALAFCKAC WKLQEESRYQ TRSITAWFT
