FUT5_GORGO
ID FUT5_GORGO Reviewed; 374 AA.
AC Q8HYJ7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5 {ECO:0000250|UniProtKB:Q11128};
DE EC=2.4.1.152 {ECO:0000250|UniProtKB:Q11128};
DE AltName: Full=3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5 {ECO:0000250|UniProtKB:Q11128};
DE EC=2.4.1.65 {ECO:0000250|UniProtKB:Q11128};
DE AltName: Full=Fucosyltransferase 5;
DE AltName: Full=Fucosyltransferase V;
DE Short=Fuc-TV {ECO:0000250|UniProtKB:Q11128};
DE Short=FucT-V;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FUT5 {ECO:0000250|UniProtKB:Q11128};
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 preferentially the transfer of L-fucose, from a
CC guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine
CC (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an
CC oligosaccharide, or a glycoprotein- and a glycolipid-linked N-
CC acetyllactosamine unit via an alpha (1,3) linkage and participates in
CC the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X
CC antigens. Preferentially transfers fucose to the GlcNAc of an internal
CC N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor
CC substrate. Also catalyzes to a lesser extend the transfer of L-fucose
CC to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-
CC GlcNAc) chain oligosaccharide via an alpha (1,4) linkage.
CC Preferentially catalyzes sialylated type 2 oligosaccharide acceptors
CC over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-
CC D-GlcNAc) oligosaccharide acceptors. Lactose-based structures are also
CC acceptor substrates. {ECO:0000250|UniProtKB:Q11128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-
CC fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304;
CC EC=2.4.1.65; Evidence={ECO:0000250|UniProtKB:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23629;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside
CC III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48376,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90376, ChEBI:CHEBI:90379;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48365;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc6Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside III(3)-alpha-Fuc-nLc6Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:61610, ChEBI:CHEBI:90307;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48337;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside III(3)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48332, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:77240;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48333;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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)-N-acetyl-
CC beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-
CC (1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-
CC beta-D-glucosyl-(1<->1')-ceramide; Xref=Rhea:RHEA:48352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90335, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48353;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62825;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
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:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62837;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc + GDP-beta-L-
CC fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-
CC GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62900, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62263,
CC ChEBI:CHEBI:62507; Evidence={ECO:0000250|UniProtKB:Q11128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-
CC L-Fuc-(1->4)]-beta-D-GlcNAc derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62904, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:146021, ChEBI:CHEBI:146022;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62905;
CC Evidence={ECO:0000250|UniProtKB:Q11128};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q11128}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AF515436; AAO15992.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8HYJ7; -.
DR STRING; 9593.ENSGGOP00000006125; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q8HYJ7; -.
DR BRENDA; 2.4.1.65; 2496.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001519; Unplaced.
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:0017060; F:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
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:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; 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; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..374
FT /note="4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase FUT5"
FT /id="PRO_0000221104"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 374 AA; 43122 MW; 6507EC4629EDD75C CRC64;
MDPLGPAKPQ WLWRRCLAGL LFQLLVAVCF FSYLRVSQDH ATGSPRPGLM VVEPVTRAPN
GSRCQDSAAT PAHPTLLILL WTWPFNTPVA LPRCSEMVPG AADCNITANS NVYPQADAVI
VHHWDIMYNP SANLLPPTRP QGQRWIWFSM ESPSNCRHLE ALDGYFNLTM SYRSDSDIFT
PYGWLEPWSG QPAHPPLNLS AKTELVAWAV SNWKPDSARV RYYQSLKAHL KVDVYGHSHK
PLPKGTMMET LSRYKFYLAF ENSLHLDYIT EKLWRNALEA WAVPVVLGPS RGNYERFLPP
DAFIHVDDFQ SPKDLARYLQ ELDKDHARYL SYFRWRETLR PRSFSWALDF CKACWKLQQE
SRYQTVRSIA AWFT
