FUT9_CANLF
ID FUT9_CANLF Reviewed; 359 AA.
AC Q659L1;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 {ECO:0000250|UniProtKB:Q9Y231};
DE EC=2.4.1.152 {ECO:0000250|UniProtKB:Q9Y231};
DE AltName: Full=Fucosyltransferase 9 {ECO:0000303|Ref.1};
DE AltName: Full=Fucosyltransferase IX {ECO:0000250|UniProtKB:Q9Y231};
DE Short=Fuc-TIX {ECO:0000250|UniProtKB:Q9Y231};
DE Short=FucT-IX;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FUT9 {ECO:0000250|UniProtKB:Q9Y231};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Martinez-Duncker I., Oriol R., Mollicone R.;
RT "Phylogeny of fucosyltransferases.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 lactosamine unit of a glycoprotein or a glycolipid-linked
CC polylactosamine chains through an alpha-1,3 glycosidic linkage and
CC participates in particular to the Lewis x (Lex)/CD15 epitope
CC biosynthesis in neurons which allows cell differentiation, cell
CC adhesion, and initiation of neurite outgrowth. Also fucosylates di-,
CC tri- and tetraantennary N-glycans linked to glycoproteins and the inner
CC lactosamine unit of the alpha2,3-sialylated polylactosamine resulting
CC in sLex (CD15s) epitope synthesis. Furthermore, it is capable to
CC synthesizes Lewis a (Lea), although to a lesser extent than Lex and
CC Lewis y (Ley) and to confer SELE-dependent, but not SELL- and SELP-
CC selectin-dependent, cell rolling and adhesion by enhancing Lex and sLex
CC synthesis. May also fucosylate the internal LacNAc unit of the
CC polylactosamine chain to form VIM-2 antigen that serves as recognition
CC epitope for SELE. {ECO:0000250|UniProtKB:Q9Y231}.
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:Q9Y231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:Q9Y231};
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:Q9Y231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68045;
CC Evidence={ECO:0000250|UniProtKB:Q9Y231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-N-glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC glucosyl-(1<->1')-ceramide + GDP-beta-L-fucose = alpha-N-
CC glycoloylneuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-
CC 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 + GDP + H(+); Xref=Rhea:RHEA:48388,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90383, ChEBI:CHEBI:90384;
CC Evidence={ECO:0000250|UniProtKB:O88819};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48389;
CC Evidence={ECO:0000250|UniProtKB:O88819};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-
CC beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + GDP-beta-L-fucose = a neolactoside IV(3)-alpha-
CC Gal,III(3)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48380,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90380, ChEBI:CHEBI:90381;
CC Evidence={ECO:0000250|UniProtKB:O88819};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48381;
CC Evidence={ECO:0000250|UniProtKB:O88819};
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:O88819};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377;
CC Evidence={ECO:0000250|UniProtKB:O88819};
CC -!- ACTIVITY REGULATION: Activated by Mn2+. {ECO:0000250|UniProtKB:Q9Y231}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9Y231}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O88819}.
CC -!- PTM: N-glycosylated with complex-type N-glycans.
CC {ECO:0000250|UniProtKB:Q9Y231}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; AJ831838; CAH41981.1; -; mRNA.
DR RefSeq; NP_001005380.1; NM_001005380.1.
DR RefSeq; XP_005627091.1; XM_005627034.1.
DR RefSeq; XP_005627092.1; XM_005627035.1.
DR RefSeq; XP_005627094.1; XM_005627037.1.
DR RefSeq; XP_005627096.1; XM_005627039.1.
DR RefSeq; XP_013973502.1; XM_014118027.1.
DR RefSeq; XP_013973503.1; XM_014118028.1.
DR AlphaFoldDB; Q659L1; -.
DR STRING; 9612.ENSCAFP00000005103; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; Q659L1; -.
DR Ensembl; ENSCAFT00030009125; ENSCAFP00030008007; ENSCAFG00030004971.
DR Ensembl; ENSCAFT00040008492; ENSCAFP00040007373; ENSCAFG00040004479.
DR Ensembl; ENSCAFT00845014928; ENSCAFP00845011571; ENSCAFG00845008503.
DR GeneID; 449027; -.
DR KEGG; cfa:449027; -.
DR CTD; 10690; -.
DR VEuPathDB; HostDB:ENSCAFG00845008503; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000155095; -.
DR InParanoid; Q659L1; -.
DR OrthoDB; 551308at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000003421; Expressed in prefrontal cortex and 10 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi 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:0032588; C:trans-Golgi network membrane; 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:AgBase.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; ISS:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:AgBase.
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 GO; GO:1903236; P:regulation of leukocyte tethering or rolling; 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; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..359
FT /note="4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase 9"
FT /id="PRO_0000221116"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..359
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 359 AA; 42055 MW; BD07DF768B367864 CRC64;
MTSASKGILR PFLIVCIILG CFMACLLIYI KPTNSWIFSP MESASSVLKM KNFFSTKTDY
FNETTILIWV WPFGQTFDLT SCQAMFNIQG CHLTTDRSLY NKSHAVLIHH RDISWDLTNL
PQQARPPFQK WIWMNLESPT HTPQKSGIEH LFNLTLTYRR DSDIQVPYGF LTVSTNPFVF
EVPSKEKLVC WVVSNWNPEH ARVKYYNELS KSIEIHTYGQ AFGEYVNDKN LIPTISTCKF
YLSFENSIHK DYITEKLYNA FLAGSVPVVL GPSRENYENY IPADSFIHVE DYNSPSELAK
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN
