FUT9_MOUSE
ID FUT9_MOUSE Reviewed; 359 AA.
AC O88819; Q3TQ63;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 {ECO:0000305};
DE EC=2.4.1.152 {ECO:0000269|PubMed:12626397};
DE AltName: Full=Fucosyltransferase 9;
DE AltName: Full=Fucosyltransferase IX {ECO:0000303|PubMed:12626397};
DE Short=Fuc-TIX {ECO:0000303|PubMed:9756916};
DE Short=FucT-IX;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=Fut9 {ECO:0000312|MGI:MGI:1330859};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9756916; DOI=10.1074/jbc.273.41.26729;
RA Kudo T., Ikehara Y., Togayachi A., Kaneko M., Hiraga T., Sasaki K.,
RA Narimatsu H.;
RT "Expression cloning and characterization of a novel murine alpha1, 3-
RT fucosyltransferase, mFuc-TIX, that synthesizes the Lewis x (CD15) epitope
RT in brain and kidney.";
RL J. Biol. Chem. 273:26729-26738(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpus striatum, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12626397; DOI=10.1093/glycob/cwg048;
RA Nishihara S., Iwasaki H., Nakajima K., Togayachi A., Ikehara Y., Kudo T.,
RA Kushi Y., Furuya A., Shitara K., Narimatsu H.;
RT "Alpha1,3-fucosyltransferase IX (Fut9) determines Lewis X expression in
RT brain.";
RL Glycobiology 13:445-455(2003).
RN [4]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15121843; DOI=10.1128/mcb.24.10.4221-4228.2004;
RA Kudo T., Kaneko M., Iwasaki H., Togayachi A., Nishihara S., Abe K.,
RA Narimatsu H.;
RT "Normal embryonic and germ cell development in mice lacking alpha 1,3-
RT fucosyltransferase IX (Fut9) which show disappearance of stage-specific
RT embryonic antigen 1.";
RL Mol. Cell. Biol. 24:4221-4228(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16973732; DOI=10.1093/glycob/cwl047;
RA Kudo T., Fujii T., Ikegami S., Inokuchi K., Takayama Y., Ikehara Y.,
RA Nishihara S., Togayachi A., Takahashi S., Tachibana K., Yuasa S.,
RA Narimatsu H.;
RT "Mice lacking alpha1,3-fucosyltransferase IX demonstrate disappearance of
RT Lewis x structure in brain and increased anxiety-like behaviors.";
RL Glycobiology 17:1-9(2007).
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:12626397,
CC PubMed:9756916, PubMed:15121843, PubMed:16973732). Also fucosylates
CC di-, tri- and tetraantennary N-glycans linked to glycoproteins and the
CC inner lactosamine unit of the alpha2,3-sialylated polylactosamine
CC resulting in sLex (CD15s) epitope synthesis (By similarity).
CC Furthermore, it is capable of synthesizing Lewis a (Lea), although to a
CC lesser extent than Lex and Lewis y (Ley) and to confer SELE-dependent,
CC but not SELL- and SELP-selectin-dependent, cell rolling and adhesion by
CC enhancing Lex and sLex synthesis (By similarity). May also fucosylate
CC the internal LacNAc unit of the polylactosamine chain to form VIM-2
CC antigen that serves as recognition epitope for SELE.
CC {ECO:0000250|UniProtKB:Q9Y231, ECO:0000269|PubMed:12626397,
CC ECO:0000269|PubMed:15121843, ECO:0000269|PubMed:16973732,
CC ECO:0000269|PubMed:9756916}.
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:12626397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000269|PubMed:12626397};
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:0000269|PubMed:12626397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48389;
CC Evidence={ECO:0000269|PubMed:12626397};
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:0000269|PubMed:12626397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48381;
CC Evidence={ECO:0000269|PubMed:12626397};
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:12626397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377;
CC Evidence={ECO:0000269|PubMed:12626397};
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:0000269|PubMed:12626397}.
CC -!- TISSUE SPECIFICITY: Mainly detected in brain and kidney.
CC {ECO:0000269|PubMed:9756916}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 1-cell embryos and then decreased
CC dramatically in 2- and 4-cell embryos. It increases transiently in 8-
CC cell embryos and then vanishes completely at the morula stage
CC (PubMed:15121843). Predominantly expressed at all stages both in
CC cerebrum and in cerebellum containing mesencephalon. Expression
CC increases during the embryonic stage with the highest expression at P0
CC and decreases. Expression increases from the embryo to P7 stage, with
CC the highest expression at P7, and decreases in adult brain. At P7
CC expressed in the neurons in layers II-IV and those in layers V and VI
CC of the cerebral cortex. At P7 expressed in cerebellum, granule neurons
CC in the internal granule cell layer (PubMed:12626397).
CC {ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:15121843}.
CC -!- PTM: N-glycosylated with complex-type N-glycans.
CC {ECO:0000250|UniProtKB:Q9Y231}.
CC -!- DISRUPTION PHENOTYPE: Homozygous Fut9 knockout mice develop normally,
CC with no gross phenotypic abnormalities, and are fertile.
CC {ECO:0000269|PubMed:15121843, ECO:0000269|PubMed:16973732}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 9;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_616";
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DR EMBL; AB015426; BAA33522.1; -; mRNA.
DR EMBL; AK032177; BAC27746.1; -; mRNA.
DR EMBL; AK036183; BAC29338.1; -; mRNA.
DR EMBL; AK043410; BAC31540.1; -; mRNA.
DR EMBL; AK047650; BAC33112.1; -; mRNA.
DR EMBL; AK049122; BAC33555.1; -; mRNA.
DR EMBL; AK163871; BAE37522.1; -; mRNA.
DR CCDS; CCDS18011.1; -.
DR RefSeq; NP_034373.1; NM_010243.3.
DR AlphaFoldDB; O88819; -.
DR STRING; 10090.ENSMUSP00000081826; -.
DR SwissLipids; SLP:000001437; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyConnect; 2119; 1 N-Linked glycan (1 site).
DR GlyGen; O88819; 3 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; O88819; -.
DR jPOST; O88819; -.
DR PaxDb; O88819; -.
DR PRIDE; O88819; -.
DR ProteomicsDB; 271615; -.
DR Antibodypedia; 55123; 30 antibodies from 14 providers.
DR DNASU; 14348; -.
DR Ensembl; ENSMUST00000084770; ENSMUSP00000081826; ENSMUSG00000055373.
DR Ensembl; ENSMUST00000108199; ENSMUSP00000103834; ENSMUSG00000055373.
DR GeneID; 14348; -.
DR KEGG; mmu:14348; -.
DR UCSC; uc008sei.1; mouse.
DR CTD; 10690; -.
DR MGI; MGI:1330859; Fut9.
DR VEuPathDB; HostDB:ENSMUSG00000055373; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000155095; -.
DR HOGENOM; CLU_032075_4_2_1; -.
DR InParanoid; O88819; -.
DR OMA; QTMFNIQ; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; O88819; -.
DR TreeFam; TF316348; -.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14348; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Fut9; mouse.
DR PRO; PR:O88819; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O88819; protein.
DR Bgee; ENSMUSG00000055373; Expressed in retrosplenial region and 121 other tissues.
DR ExpressionAtlas; O88819; baseline and differential.
DR Genevisible; O88819; MM.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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; IDA:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:MGI.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
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; IDA:MGI.
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_0000221119"
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; 42041 MW; 96A2394547F2A44E CRC64;
MTSTSKGILR PFLIVCIILG CFMACLLIYI KPTNSWVFSP MESASSVLKM KNFFSTKTDY
FNETTILVWV WPFGQTFDLT SCQAMFNIQG CHLTTDRSLY NKSHAVLIHH RDISWDLTNL
PQQARPPFQK WIWMNLESPT HTPQKSGIEH LFNLTLTYRR DSDIQVPYGF LTVSTNPFVF
EVPSKEKLVC WVVSNWNPEH ARVKYYNELS KSIEIHTYGQ AFGEYVNDKN LIPTISTCKF
YLSFENSIHK DYITEKLYNA FLAGSVPVVL GPSRENYENY IPADSFIHVE DFNSPSELAK
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN
