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 24-JAN-2024, entry version 163. 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, CATALYTIC ACTIVITY, AND TISSUE RP 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; RC 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, PATHWAY, SUBCELLULAR LOCATION, AND RP DEVELOPMENTAL 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, FUNCTION, AND CATALYTIC RP ACTIVITY. 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, CATALYTIC ACTIVITY, PATHWAY, 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). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=22645129; DOI=10.1074/jbc.m112.365643; RA Yagi H., Saito T., Yanagisawa M., Yu R.K., Kato K.; RT "Lewis X-carrying N-glycans regulate the proliferation of mouse embryonic RT neural stem cells via the Notch signaling pathway."; RL J. Biol. Chem. 287:24356-24364(2012). 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, beta-D-Gal-(1->4)-beta-D-GlcNAc-) glycan attached CC to glycolipids and N- or O-linked glycoproteins. Fucosylates distal CC type 2 LacNAc and its fucosylated (H-type 2 LacNAc) and sialylated CC (sialyl-type 2 LacNAc) derivatives to form Lewis x (Lex) (CD15) and CC Lewis y (Ley) antigenic epitopes involved in cell adhesion and CC differentiation (PubMed:9756916, PubMed:12626397, PubMed:15121843, CC PubMed:16973732, PubMed:22645129) (By similarity). Generates Lex CC epitopes in the brain, presumably playing a role in the maintenance of CC neuronal stemness and neurite outgrowth in progenitor neural cells CC (PubMed:16973732, PubMed:22645129) (By similarity). Fucosylates the CC internal type 2 LacNAc unit of the polylactosamine chain to form VIM-2 CC antigen that serves as recognition epitope for SELE (By similarity). CC Can also modify milk oligosaccharides in particular type 2 CC tetrasaccharide LNnT (PubMed:9756916) (By similarity). CC {ECO:0000250|UniProtKB:Q9Y231, ECO:0000269|PubMed:12626397, CC ECO:0000269|PubMed:15121843, ECO:0000269|PubMed:16973732, CC ECO:0000269|PubMed:22645129, 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, ECO:0000269|PubMed:15121843, CC ECO:0000269|PubMed:16973732, ECO:0000269|PubMed:22645129, CC ECO:0000269|PubMed:9756916}; 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, ECO:0000269|PubMed:16973732}; 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, ECO:0000269|PubMed:16973732}; 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:Q9Y231}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077; CC Evidence={ECO:0000250|UniProtKB:Q9Y231}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc CC + GDP-beta-L-fucose = beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D- CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP + H(+); CC Xref=Rhea:RHEA:77187, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, CC ChEBI:CHEBI:58189, ChEBI:CHEBI:60239, ChEBI:CHEBI:61352; CC Evidence={ECO:0000250|UniProtKB:Q9Y231}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77188; CC Evidence={ECO:0000250|UniProtKB:Q9Y231}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-beta-D-GlcNAc CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal- CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); CC Xref=Rhea:RHEA:77191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133510, ChEBI:CHEBI:195560; CC Evidence={ECO:0000250|UniProtKB:Q9Y231}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77192; CC Evidence={ECO:0000250|UniProtKB:Q9Y231}; CC -!- ACTIVITY REGULATION: Activated by Mn2+. {ECO:0000250|UniProtKB:Q9Y231}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:22645129}. CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000269|PubMed:12626397, CC ECO:0000269|PubMed:16973732}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y231}. 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 -!- DOMAIN: The donor-binding domain adopts a Rossman-like fold involved in CC GDP-beta-L-fucose sugar donor interactions. CC {ECO:0000250|UniProtKB:Q9Y231}. CC -!- DOMAIN: The acceptor-binding domain adopts a Rossman-like fold CC consisting of six-stranded parallel beta sheets characteristic of the CC Toll/interleukin-1 receptor (TIR) fold family. Interacts with the CC LacNAc unit of type 2 LacNAc and H-type 2 LacNAc structures. It CC contains the catalytic base Glu-137 which deprotonates the hydroxyl CC group of GlcNAc while forming bridging interactions with the donor CC sugar to position the catalytic machinery in the active site. CC {ECO:0000250|UniProtKB:Q9Y231}. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; 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 GlyCosmos; O88819; 3 sites, 1 glycan. DR GlyGen; O88819; 3 sites, 1 N-linked glycan (1 site). DR iPTMnet; O88819; -. DR PhosphoSitePlus; O88819; -. DR jPOST; O88819; -. DR PaxDb; 10090-ENSMUSP00000081826; -. DR ProteomicsDB; 271615; -. DR Antibodypedia; 55123; 64 antibodies from 14 providers. DR DNASU; 14348; -. DR Ensembl; ENSMUST00000084770.5; ENSMUSP00000081826.5; ENSMUSG00000055373.9. DR Ensembl; ENSMUST00000108199.2; ENSMUSP00000103834.2; ENSMUSG00000055373.9. DR GeneID; 14348; -. DR KEGG; mmu:14348; -. DR UCSC; uc008sei.1; mouse. DR AGR; MGI:1330859; -. 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; FRKWDSQ; -. DR OrthoDB; 1331128at2759; -. 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 80 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 122 other cell types or tissues. DR ExpressionAtlas; O88819; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. 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:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB. DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB. DR GO; GO:0106402; P:Lewis x epitope biosynthetic process; IMP:UniProtKB. DR GO; GO:0036071; P:N-glycan fucosylation; IDA:MGI. DR GO; GO:0007399; P:nervous system development; ISO:MGI. DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB. DR GO; GO:0036445; P:neuronal stem cell division; IMP:UniProtKB. DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IMP:MGI. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IMP: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; Glycosyl transferase family 10, C-terminal domain; 1. DR InterPro; IPR031481; Glyco_tran_10_N. DR InterPro; IPR001503; Glyco_trans_10. DR InterPro; IPR038577; GT10-like_C_sf. DR PANTHER; PTHR11929:SF10; 4-GALACTOSYL-N-ACETYLGLUCOSAMINIDE 3-ALPHA-L-FUCOSYLTRANSFERASE 9; 1. DR PANTHER; PTHR11929; ALPHA- 1,3 -FUCOSYLTRANSFERASE; 1. DR Pfam; PF17039; Glyco_tran_10_N; 1. DR Pfam; PF00852; Glyco_transf_10; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR Genevisible; O88819; MM. PE 1: Evidence at protein level; KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; 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 REGION 63..168 FT /note="Acceptor-binding" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT REGION 169..326 FT /note="Donor-binding" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT REGION 327..359 FT /note="Acceptor-binding" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT ACT_SITE 137 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 75 FT /ligand="a beta-D-galactosyl-(1->4)-N-acetyl-beta-D- FT glucosaminyl derivative" FT /ligand_id="ChEBI:CHEBI:133507" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 137 FT /ligand="a beta-D-galactosyl-(1->4)-N-acetyl-beta-D- FT glucosaminyl derivative" FT /ligand_id="ChEBI:CHEBI:133507" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 137 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 168 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 192 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 194 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 195 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 202 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 226 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 241 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 246 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 252 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 255 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT BINDING 256 FT /ligand="GDP-beta-L-fucose" FT /ligand_id="ChEBI:CHEBI:57273" FT /evidence="ECO:0000250|UniProtKB:Q9Y231" 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:0000250|UniProtKB:Q9Y231, ECO:0000255" FT DISULFID 82..335 FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT DISULFID 91..338 FT /evidence="ECO:0000250|UniProtKB:Q9Y231" FT DISULFID 190..238 FT /evidence="ECO:0000250|UniProtKB:Q9Y231" 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 //