FUT9_RAT
ID FUT9_RAT Reviewed; 359 AA.
AC Q99JB3;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 {ECO:0000305};
DE EC=2.4.1.152 {ECO:0000269|PubMed:11020213, ECO:0000269|PubMed:11675393};
DE AltName: Full=Fucosyltransferase 9;
DE AltName: Full=Fucosyltransferase IX {ECO:0000303|PubMed:11020213, ECO:0000303|PubMed:11675393};
DE Short=Fuc-TIX {ECO:0000303|PubMed:11020213};
DE Short=FucT-IX;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=Fut9 {ECO:0000312|RGD:619955};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11675393; DOI=10.1074/jbc.m108495200;
RA Shimoda Y., Tajima Y., Osanai T., Katsume A., Kohara M., Kudo T.,
RA Narimatsu H., Takashima N., Ishii Y., Nakamura S., Osumi N., Sanai Y.;
RT "Pax6 controls the expression of Lewis x epitope in the embryonic forebrain
RT by regulating alpha 1,3-fucosyltransferase IX expression.";
RL J. Biol. Chem. 277:2033-2039(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11020213;
RX DOI=10.1002/1097-4547(20001015)62:2<206::aid-jnr5>3.0.co;2-e;
RA Baboval T., Henion T., Kinnally E., Smith F.I.;
RT "Molecular cloning of rat alpha1,3-fucosyltransferase IX (Fuc-TIX) and
RT comparison of the expression of Fuc-TIV and Fuc-TIX genes during rat
RT postnatal cerebellum development.";
RL J. Neurosci. Res. 62:206-215(2000).
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 (PubMed:11020213,
CC PubMed:11675393). Also fucosylates di-, tri- and tetraantennary N-
CC glycans linked to glycoproteins and the inner lactosamine unit of the
CC alpha2,3-sialylated polylactosamine resulting in sLex (CD15s) epitope
CC synthesis. Furthermore, it is capable of synthesizing Lewis a (Lea),
CC although to a lesser extent than Lex and Lewis y (Ley) and to confer
CC SELE-dependent, but not SELL- and SELP-selectin-dependent, cell rolling
CC and adhesion by enhancing Lex and sLex synthesis (By similarity). May
CC also fucosylate the internal LacNAc unit of the polylactosamine chain
CC to form VIM-2 antigen that serves as recognition epitope for SELE.
CC {ECO:0000250|UniProtKB:Q9Y231, ECO:0000269|PubMed:11020213,
CC ECO:0000269|PubMed:11675393}.
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:0000269|PubMed:11020213,
CC ECO:0000269|PubMed:11675393};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000269|PubMed:11020213, ECO:0000269|PubMed:11675393};
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:0000269|PubMed:11020213, ECO:0000269|PubMed:11675393};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377;
CC Evidence={ECO:0000269|PubMed:11020213, ECO:0000269|PubMed:11675393};
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; AB049819; BAB40953.1; -; mRNA.
DR EMBL; AF345993; AAK16591.1; -; mRNA.
DR RefSeq; NP_445917.1; NM_053465.1.
DR AlphaFoldDB; Q99JB3; -.
DR STRING; 10116.ENSRNOP00000011393; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q99JB3; 3 sites.
DR PaxDb; Q99JB3; -.
DR PRIDE; Q99JB3; -.
DR Ensembl; ENSRNOT00000113229; ENSRNOP00000087361; ENSRNOG00000070149.
DR GeneID; 84597; -.
DR KEGG; rno:84597; -.
DR UCSC; RGD:619955; rat.
DR CTD; 10690; -.
DR RGD; 619955; Fut9.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000155095; -.
DR HOGENOM; CLU_032075_4_2_1; -.
DR InParanoid; Q99JB3; -.
DR OMA; QTMFNIQ; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q99JB3; -.
DR TreeFam; TF316348; -.
DR Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q99JB3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008475; Expressed in frontal cortex and 4 other tissues.
DR Genevisible; Q99JB3; RN.
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; ISO:RGD.
DR GO; GO:0008417; F:fucosyltransferase activity; NAS:RGD.
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:0007399; P:nervous system development; IDA:RGD.
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; ISO:RGD.
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 1: Evidence at protein 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_0000221121"
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; 42037 MW; 369B4A7BD0C6CC80 CRC64;
MTSTSKGILR PFLIVCIILG CFVACLLIYI KPTNSWVFSP MESASSVLKM KNFFSRKTDY
FNETTILVWV WPFGQTFDLT SCQAMFNIQG CHLTTDRSLY NKSHAVLIHH RDISWDLTNL
PQQARPPFQK WIWMNLESPT HTPQKSGIEH LFNLTLTYRR DSDIQVPYGF LTVSTSPFVF
EVPSKEKLVC WVVSNWNPEH ARVKYYNELS KSIEIHTYGQ AFGEYVNDKN LIPTISTCKF
YLSFENSIHK DYITEKLYNA FLAGSVPVVL GPSRENYENY IPADSFIHVE DFNSPSELAK
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN
