FUT4_BOVIN
ID FUT4_BOVIN Reviewed; 398 AA.
AC Q8HZR3;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 4;
DE AltName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase;
DE EC=2.4.1.152 {ECO:0000250|UniProtKB:P22083, ECO:0000250|UniProtKB:Q11127};
DE AltName: Full=Fucosyltransferase 4;
DE AltName: Full=Fucosyltransferase IV;
DE Short=Fuc-TIV;
DE Short=FucT-IV;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FUT4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Javaud C., Julien R.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes alpha(1->3) linkage of fucosyl moiety transferred
CC from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2
CC lactosamine (LacNAc, Gal-beta(1->4)GlcNAc) glycan attached to N- or O-
CC linked glycoproteins. Robustly fucosylates nonsialylated distal LacNAc
CC unit of the polylactosamine chain to form Lewis X antigen (CD15), a
CC glycan determinant known to mediate important cellular functions in
CC development and immunity. Fucosylates with lower efficiency sialylated
CC LacNAc acceptors to form sialyl Lewis X and 6-sulfo sialyl Lewis X
CC determinants that serve as recognition epitopes for C-type lectins.
CC Together with FUT7 contributes to SELE, SELL and SELP selectin ligand
CC biosynthesis and selectin-dependent lymphocyte homing, leukocyte
CC migration and blood leukocyte homeostasis (By similarity). In a cell
CC type specific manner, may also fucosylate the internal LacNAc unit of
CC the polylactosamine chain to form VIM-2 antigen that serves as
CC recognition epitope for SELE (By similarity).
CC {ECO:0000250|UniProtKB:P22083, ECO:0000250|UniProtKB:Q11127}.
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:Q11127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
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:Q11127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
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)-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP +
CC H(+); Xref=Rhea:RHEA:68044, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145343, ChEBI:CHEBI:176900;
CC Evidence={ECO:0000250|UniProtKB:P22083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68045;
CC Evidence={ECO:0000250|UniProtKB:P22083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S
CC derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000250|UniProtKB:Q11127};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q11127}.
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; AF531092; AAN63882.1; -; mRNA.
DR RefSeq; NP_777161.1; NM_174736.2.
DR AlphaFoldDB; Q8HZR3; -.
DR STRING; 9913.ENSBTAP00000048467; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; Q8HZR3; -.
DR PRIDE; Q8HZR3; -.
DR GeneID; 282854; -.
DR KEGG; bta:282854; -.
DR CTD; 2526; -.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q8HZR3; -.
DR OrthoDB; 551308at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; 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:0005802; C:trans-Golgi network; 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; ISS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; ISS:UniProtKB.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; 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 GO; GO:1903037; P:regulation of leukocyte cell-cell adhesion; 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 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Inflammatory response;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..398
FT /note="Alpha-(1,3)-fucosyltransferase 4"
FT /id="PRO_0000221099"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 45194 MW; FAE2DA1E638706F4 CRC64;
MRARWGRRGA RRGGPGLPGT HLALLAASLL SSSVAIYVCW KQLPPLPWAS PSPPRPVNVL
LWWEPFRGRH NPRRPPPDCQ RRFNISGCVL HTDRAAYEEA QAVLFHHRDL VKGPPDWPPP
WGVQMPPVEE REGLVMDDEG QEAEAETSAA LGPRPAGQRW VWMNFESPSH SPGLQGLAGN
IFNWTLSYRA DSDIFVPYGY LYPRTHPSEQ PPGLVPPLAR KQGLVAWVVS NWDERQARVR
YYRQLSQYVT VDVFGKGGPG QPLPDAELVH TVARYKFYLA FENSQHLDYI TEKLWRNAFL
AGAVPVVLGP NRTNYERFVP SNAFIHVDDF PSASSLAAHL QFLDRNPTVY RGYFRWRRSH
AVHVTSFWDE PWCLACQAVQ KAGNQRKSVP NLAGWFQQ
