FUT9_HUMAN
ID FUT9_HUMAN Reviewed; 359 AA.
AC Q9Y231; Q5T0W4;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9 {ECO:0000305};
DE EC=2.4.1.152 {ECO:0000269|PubMed:10622713, ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078, ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23192350, ECO:0000269|PubMed:23263199};
DE AltName: Full=Fucosyltransferase 9 {ECO:0000303|PubMed:23000574};
DE AltName: Full=Fucosyltransferase IX {ECO:0000303|PubMed:10386598};
DE Short=Fuc-TIX {ECO:0000303|PubMed:10386598};
DE Short=FucT-IX;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FUT9 {ECO:0000303|PubMed:10929005, ECO:0000312|HGNC:HGNC:4020};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP ALA-237.
RC TISSUE=Brain;
RX PubMed=10386598; DOI=10.1016/s0014-5793(99)00640-7;
RA Kaneko M., Kudo T., Iwasaki H., Ikehara Y., Nishihara S., Nakagawa S.,
RA Sasaki K., Shiina T., Inoko H., Saitou N., Narimatsu H.;
RT "Alpha-1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between
RT human and mouse; molecular cloning, characterization and tissue
RT distribution of human Fuc-TIX.";
RL FEBS Lett. 452:237-242(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-237.
RX PubMed=10929005; DOI=10.1093/glycob/10.8.789;
RA Cailleau-Thomas A., Coullin P., Candelier J.J., Balanzino L., Oriol R.,
RA Mollicone R., Mennesson B.;
RT "FUT4 and FUT9 genes are expressed early in human embryogenesis.";
RL Glycobiology 10:789-802(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-237.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10622713; DOI=10.1016/s0014-5793(99)01549-5;
RA Nishihara S., Iwasaki H., Kaneko M., Tawada A., Ito M., Narimatsu H.;
RT "Alpha1,3-fucosyltransferase 9 (FUT9; Fuc-TIX) preferentially fucosylates
RT the distal GlcNAc residue of polylactosamine chain while the other four
RT alpha1,3FUT members preferentially fucosylate the inner GlcNAc residue.";
RL FEBS Lett. 462:289-294(1999).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=11278338; DOI=10.1074/jbc.m007272200;
RA Nakayama F., Nishihara S., Iwasaki H., Kudo T., Okubo R., Kaneko M.,
RA Nakamura M., Karube M., Sasaki K., Narimatsu H.;
RT "CD15 expression in mature granulocytes is determined by alpha 1,3-
RT fucosyltransferase IX, but in promyelocytes and monocytes by alpha 1,3-
RT fucosyltransferase IV.";
RL J. Biol. Chem. 276:16100-16106(2001).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12107078; DOI=10.1093/glycob/12.6.361;
RA Toivonen S., Nishihara S., Narimatsu H., Renkonen O., Renkonen R.;
RT "Fuc-TIX: a versatile alpha1,3-fucosyltransferase with a distinct
RT acceptor- and site-specificity profile.";
RL Glycobiology 12:361-368(2002).
RN [8]
RP FUNCTION.
RX PubMed=16282604; DOI=10.1093/glycob/cwj057;
RA Bogoevska V., Horst A., Klampe B., Lucka L., Wagener C., Nollau P.;
RT "CEACAM1, an adhesion molecule of human granulocytes, is fucosylated by
RT fucosyltransferase IX and interacts with DC-SIGN of dendritic cells via
RT Lewis x residues.";
RL Glycobiology 16:197-209(2006).
RN [9]
RP FUNCTION.
RX PubMed=17335083; DOI=10.1002/jnr.21230;
RA Brito C., Escrevente C., Reis C.A., Lee V.M., Trojanowski J.Q., Costa J.;
RT "Increased levels of fucosyltransferase IX and carbohydrate Lewis(x)
RT adhesion determinant in human NT2N neurons.";
RL J. Neurosci. Res. 85:1260-1270(2007).
RN [10]
RP GLYCOSYLATED, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 2-THR--LEU-9;
RP 2-THR--SER-5; SER-3 AND SER-5, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=18395013; DOI=10.1016/j.biochi.2008.03.002;
RA Brito C., Kandzia S., Graca T., Conradt H.S., Costa J.;
RT "Human fucosyltransferase IX: specificity towards N-linked glycoproteins
RT and relevance of the cytoplasmic domain in intra-Golgi localization.";
RL Biochimie 90:1279-1290(2008).
RN [11]
RP FUNCTION.
RX PubMed=23000574; DOI=10.1016/j.bbagen.2012.09.004;
RA Gouveia R., Schaffer L., Papp S., Grammel N., Kandzia S., Head S.R.,
RA Kleene R., Schachner M., Conradt H.S., Costa J.;
RT "Expression of glycogenes in differentiating human NT2N neurons.
RT Downregulation of fucosyltransferase 9 leads to decreased Lewis(x) levels
RT and impaired neurite outgrowth.";
RL Biochim. Biophys. Acta 1820:2007-2019(2012).
RN [12]
RP MUTAGENESIS OF ASN-62; ASN-101 AND ASN-153, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=23263199; DOI=10.1093/glycob/cws219;
RA Seelhorst K., Stacke C., Ziegelmueller P., Hahn U.;
RT "N-glycosylations of human alpha1,3-fucosyltransferase IX are required for
RT full enzyme activity.";
RL Glycobiology 23:559-567(2013).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23192350; DOI=10.1074/jbc.m112.400929;
RA Buffone A. Jr., Mondal N., Gupta R., McHugh K.P., Lau J.T., Neelamegham S.;
RT "Silencing alpha1,3-fucosyltransferases in human leukocytes reveals a role
RT for FUT9 enzyme during E-selectin-mediated cell adhesion.";
RL J. Biol. Chem. 288:1620-1633(2013).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=29593094; DOI=10.1074/jbc.ra117.000775;
RA Mondal N., Dykstra B., Lee J., Ashline D.J., Reinhold V.N., Rossi D.J.,
RA Sackstein R.;
RT "Distinct human alpha(1,3)-fucosyltransferases drive Lewis-X/sialyl Lewis-X
RT assembly in human cells.";
RL J. Biol. Chem. 293:7300-7314(2018).
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:23263199,
CC PubMed:23192350, PubMed:10386598, PubMed:17335083, PubMed:23000574,
CC PubMed:11278338, PubMed:10622713, PubMed:18395013, PubMed:12107078,
CC PubMed:16282604, PubMed:29593094). Also fucosylates di-, tri- and
CC 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 (PubMed:12107078, PubMed:18395013).
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 (PubMed:18395013, PubMed:23192350).
CC May also fucosylate the internal LacNAc unit of the polylactosamine
CC chain to form VIM-2 antigen that serves as recognition epitope for
CC SELE. {ECO:0000269|PubMed:10386598, ECO:0000269|PubMed:10622713,
CC ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078,
CC ECO:0000269|PubMed:16282604, ECO:0000269|PubMed:17335083,
CC ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23000574,
CC ECO:0000269|PubMed:23192350, ECO:0000269|PubMed:23263199}.
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:10622713,
CC ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078,
CC ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23192350,
CC ECO:0000269|PubMed:23263199, ECO:0000269|PubMed:29593094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000269|PubMed:10622713, ECO:0000269|PubMed:11278338,
CC ECO:0000269|PubMed:12107078, ECO:0000269|PubMed:18395013,
CC ECO:0000269|PubMed:23192350, ECO:0000305|PubMed:29593094};
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:0000269|PubMed:11278338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68045;
CC Evidence={ECO:0000305|PubMed:11278338};
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:0000269|PubMed:18395013}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for N-acetyllactosamine {ECO:0000269|PubMed:23263199};
CC KM=2.6 uM for GDP-fucose {ECO:0000269|PubMed:23263199};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q9Y231; P58418: CLRN1; NbExp=3; IntAct=EBI-3922408, EBI-17274839;
CC Q9Y231; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-3922408, EBI-712073;
CC Q9Y231; O75031: HSF2BP; NbExp=3; IntAct=EBI-3922408, EBI-7116203;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:18395013}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O88819}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in forebrain and stomach, lower
CC expression in spleen and peripheral blood leukocytes, and no expression
CC in small intestine, colon, liver, lung, kidney, adrenal cortex or
CC uterus (PubMed:10386598). Highly expressed in granulocytes. Not
CC expressed in monocytes (PubMed:11278338). {ECO:0000269|PubMed:10386598,
CC ECO:0000269|PubMed:11278338}.
CC -!- PTM: N-glycosylated with complex-type N-glycans.
CC {ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:29593094}.
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_hum_606";
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DR EMBL; AB023021; BAA81685.1; -; mRNA.
DR EMBL; AJ238701; CAB41890.1; -; mRNA.
DR EMBL; AL512406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036101; AAH36101.1; -; mRNA.
DR CCDS; CCDS5033.1; -.
DR RefSeq; NP_006572.2; NM_006581.3.
DR RefSeq; XP_011533685.1; XM_011535383.2.
DR RefSeq; XP_011533687.1; XM_011535385.2.
DR RefSeq; XP_016865677.1; XM_017010188.1.
DR RefSeq; XP_016865679.1; XM_017010190.1.
DR AlphaFoldDB; Q9Y231; -.
DR BioGRID; 115929; 15.
DR IntAct; Q9Y231; 7.
DR STRING; 9606.ENSP00000302599; -.
DR BindingDB; Q9Y231; -.
DR ChEMBL; CHEMBL4985; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q9Y231; 3 sites.
DR iPTMnet; Q9Y231; -.
DR PhosphoSitePlus; Q9Y231; -.
DR BioMuta; FUT9; -.
DR DMDM; 311033382; -.
DR MassIVE; Q9Y231; -.
DR PaxDb; Q9Y231; -.
DR PeptideAtlas; Q9Y231; -.
DR PRIDE; Q9Y231; -.
DR ProteomicsDB; 85620; -.
DR Antibodypedia; 55123; 30 antibodies from 14 providers.
DR DNASU; 10690; -.
DR Ensembl; ENST00000302103.6; ENSP00000302599.4; ENSG00000172461.11.
DR GeneID; 10690; -.
DR KEGG; hsa:10690; -.
DR MANE-Select; ENST00000302103.6; ENSP00000302599.4; NM_006581.4; NP_006572.2.
DR UCSC; uc003pop.5; human.
DR CTD; 10690; -.
DR DisGeNET; 10690; -.
DR GeneCards; FUT9; -.
DR HGNC; HGNC:4020; FUT9.
DR HPA; ENSG00000172461; Group enriched (brain, stomach).
DR MIM; 606865; gene.
DR neXtProt; NX_Q9Y231; -.
DR OpenTargets; ENSG00000172461; -.
DR PharmGKB; PA28436; -.
DR VEuPathDB; HostDB:ENSG00000172461; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000155095; -.
DR HOGENOM; CLU_032075_4_2_1; -.
DR InParanoid; Q9Y231; -.
DR OMA; QTMFNIQ; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q9Y231; -.
DR TreeFam; TF316348; -.
DR BioCyc; MetaCyc:HS10520-MON; -.
DR BRENDA; 2.4.1.152; 2681.
DR PathwayCommons; Q9Y231; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q9Y231; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 10690; 10 hits in 1066 CRISPR screens.
DR ChiTaRS; FUT9; human.
DR GeneWiki; FUT9; -.
DR GenomeRNAi; 10690; -.
DR Pharos; Q9Y231; Tbio.
DR PRO; PR:Q9Y231; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y231; protein.
DR Bgee; ENSG00000172461; Expressed in pylorus and 85 other tissues.
DR Genevisible; Q9Y231; HS.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA: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; IBA:GO_Central.
DR GO; GO:0008417; F:fucosyltransferase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; TAS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:1903037; P:regulation of leukocyte cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:1903236; P:regulation of leukocyte tethering or rolling; IMP: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_0000221118"
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"
FT VARIANT 237
FT /note="T -> A (in dbSNP:rs3811069)"
FT /evidence="ECO:0000269|PubMed:10386598,
FT ECO:0000269|PubMed:10929005, ECO:0000269|PubMed:15489334"
FT /id="VAR_024465"
FT VARIANT 358
FT /note="W -> G (in dbSNP:rs9986564)"
FT /id="VAR_030575"
FT MUTAGEN 2..9
FT /note="Missing: Does not affect glycosylation. Does not
FT affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase activity. Affects subcellular location."
FT /evidence="ECO:0000269|PubMed:18395013"
FT MUTAGEN 2..5
FT /note="Missing: Does not affect glycosylation. Does not
FT affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase activity. Affects subcellular location."
FT /evidence="ECO:0000269|PubMed:18395013"
FT MUTAGEN 3
FT /note="S->A: Does not affect glycosylation; when associated
FT with A-5. Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity;
FT when associated with A-5. Does not affect subcellular
FT location; when associated with A-5."
FT /evidence="ECO:0000269|PubMed:18395013"
FT MUTAGEN 5
FT /note="S->A: Does not affect glycosylation; when associated
FT with A-3. Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity;
FT when associated with A-3. Does not affects subcellular
FT location; when associated with A-3."
FT /evidence="ECO:0000269|PubMed:18395013"
FT MUTAGEN 62
FT /note="N->Q: Weakly decreases alpha 1,3-fucosyltransferase
FT activity. Almost complete loss of alpha 1,3-
FT fucosyltransferase activity; when associated with Q-101.
FT Almost complete loss of alpha 1,3-fucosyltransferase
FT activity; when associated with Q-153. Loss of catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:23263199"
FT MUTAGEN 101
FT /note="N->Q: Significantly decrease alpha 1,3-
FT fucosyltransferase activity. Almost complete loss of alpha
FT 1,3-fucosyltransferase activity; when associated with Q-62.
FT Almost complete loss of alpha 1,3-fucosyltransferase
FT activity; when associated with Q-153. Loss of catalytic
FT efficiency."
FT /evidence="ECO:0000269|PubMed:23263199"
FT MUTAGEN 153
FT /note="N->Q: Almost complete loss of alpha 1,3-
FT fucosyltransferase activity. Almost complete loss of alpha
FT 1,3-fucosyltransferase activity; when associated with Q-62.
FT Almost complete loss of alpha 1,3-fucosyltransferase
FT activity; when associated with Q-101."
FT /evidence="ECO:0000269|PubMed:23263199"
SQ SEQUENCE 359 AA; 42071 MW; D57CFCB039B644D9 CRC64;
MTSTSKGILR PFLIVCIILG CFMACLLIYI KPTNSWIFSP 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 DYNSPSELAK
YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN
