FUT6_PONPY
ID FUT6_PONPY Reviewed; 359 AA.
AC Q9GKU6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11404338; DOI=10.1093/genetics/158.2.747;
RA Koda Y., Tachida H., Pang H., Liu Y., Soejima M., Ghaderi A.A.,
RA Takenaka O., Kimura H.;
RT "Contrasting patterns of polymorphisms at the ABO-secretor gene (FUT2) and
RT plasma alpha(1,3)fucosyltransferase gene (FUT6) in human populations.";
RL Genetics 158:747-756(2001).
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}.
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DR EMBL; AB051859; BAB18672.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GKU6; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR UniPathway; UPA00378; -.
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: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; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..359
FT /note="4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase FUT6"
FT /id="PRO_0000221112"
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 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; 41848 MW; 87598D528A45F86C CRC64;
MDPLGPAKTQ WSWRCCLTAL LFQLLVAVCF FSYLRVSRDD PTVYPNGSPF PDSTGTPAHS
IPLILLWTWP FNKPIALPRC SEMVPGTADC NITADRKVYP QADAVIVHHR EVMYNPSAQL
PRSPRRQGQR WIWFNLESPS HCWHLKAMDG YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH
PPLNLSAKTE LVAWAVSNWR PNSARVRYYQ SLQAHLKVDV YGRSHKPLPQ GTMMETLSRY
KFYLAFENSV HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD
LAQYLQELDK DHARYLSYFR WRETLQPRSC SWALDFCKAC WKLQEESRYQ TRSIAAWFT
