FUT5_HUMAN
ID FUT5_HUMAN Reviewed; 374 AA.
AC Q11128; A8K4X2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5;
DE EC=2.4.1.152 {ECO:0000269|PubMed:7721776};
DE AltName: Full=3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5;
DE EC=2.4.1.65 {ECO:0000269|PubMed:7721776};
DE AltName: Full=Fucosyltransferase 5;
DE AltName: Full=Fucosyltransferase V;
DE Short=Fuc-TV {ECO:0000303|PubMed:1740457};
DE Short=FucT-V;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
GN Name=FUT5 {ECO:0000312|HGNC:HGNC:4016};
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 [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=1740457; DOI=10.1016/s0021-9258(19)50641-x;
RA Weston B.W., Nair R.P., Larsen R.D., Lowe J.B.;
RT "Isolation of a novel human alpha (1,3)fucosyltransferase gene and
RT molecular comparison to the human Lewis blood group alpha
RT (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes
RT encoding enzymes with distinct acceptor substrate specificities.";
RL J. Biol. Chem. 267:4152-4160(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon, Kidney, and Liver;
RX PubMed=7650030; DOI=10.1074/jbc.270.34.20112;
RA Cameron H.S., Szczepaniak D., Weston B.W.;
RT "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in
RT normal tissues. Alternative splicing, polyadenylation, and isoforms.";
RL J. Biol. Chem. 270:20112-20122(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=7721776; DOI=10.1074/jbc.270.15.8712;
RA de Vries T., Srnka C.A., Palcic M.M., Swiedler S.J., van den Eijnden D.H.,
RA Macher B.A.;
RT "Acceptor specificity of different length constructs of human recombinant
RT alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the
RT transmembrane domain of fucosyltransferase V by protein A results in an
RT enzyme with GDP-fucose hydrolyzing activity.";
RL J. Biol. Chem. 270:8712-8722(1995).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASN-86; THR-87; PRO-92;
RP ALA-101; ASN-105; SER-110; SER-111 AND ALA-118, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=9737988; DOI=10.1074/jbc.273.39.25244;
RA Nguyen A.T., Holmes E.H., Whitaker J.M., Ho S., Shetterly S., Macher B.A.;
RT "Human alpha1,3/4-fucosyltransferases. I. Identification of amino acids
RT involved in acceptor substrate binding by site-directed mutagenesis.";
RL J. Biol. Chem. 273:25244-25249(1998).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=9737989; DOI=10.1074/jbc.273.39.25250;
RA Vo L., Lee S., Marcinko M.C., Holmes E.H., Macher B.A.;
RT "Human alpha1,3/4-fucosyltransferases. II. A single amino acid at the COOH
RT terminus of FucT III and V alters their kinetic properties.";
RL J. Biol. Chem. 273:25250-25255(1998).
RN [10]
RP CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TRP-124, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14718375; DOI=10.1093/glycob/cwh053;
RA Dupuy F., Germot A., Julien R., Maftah A.;
RT "Structure/function study of Lewis alpha3- and alpha3/4-
RT fucosyltransferases: the alpha1,4 fucosylation requires an aromatic residue
RT in the acceptor-binding domain.";
RL Glycobiology 14:347-356(2004).
RN [11]
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF THR-87; TRP-124; ASP-125
RP AND ILE-126.
RX PubMed=17604274; DOI=10.1074/jbc.m702395200;
RA Shetterly S., Jost F., Watson S.R., Knegtel R., Macher B.A., Holmes E.H.;
RT "Site-specific fucosylation of sialylated polylactosamines by alpha1,3/4-
RT fucosyltransferases-V and -VI Is defined by amino acids near the N terminus
RT of the catalytic domain.";
RL J. Biol. Chem. 282:24882-24892(2007).
RN [12]
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 preferentially the transfer of L-fucose, from a
CC guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine
CC (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an
CC oligosaccharide, or a glycoprotein- and a glycolipid-linked N-
CC acetyllactosamine unit via an alpha (1,3) linkage and participates in
CC the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X
CC antigens (PubMed:14718375, PubMed:1740457, PubMed:7721776,
CC PubMed:9737988, PubMed:17604274, PubMed:9737989, PubMed:29593094).
CC Preferentially transfers fucose to the GlcNAc of an internal N-
CC acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor
CC substrate (PubMed:7721776, PubMed:17604274). Also catalyzes to a lesser
CC extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-
CC galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-
CC Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosaccharide via an
CC alpha (1,4) linkage (PubMed:14718375, PubMed:1740457, PubMed:7721776,
CC PubMed:9737988, PubMed:17604274). Preferentially catalyzes sialylated
CC type 2 oligosaccharide acceptors over neutral type 2 or H type 2
CC (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosaccharide
CC acceptors (PubMed:1740457, PubMed:9737989). Lactose-based structures
CC are also acceptor substrates (PubMed:1740457, PubMed:7721776).
CC {ECO:0000269|PubMed:14718375, ECO:0000269|PubMed:1740457,
CC ECO:0000269|PubMed:17604274, ECO:0000269|PubMed:7721776,
CC ECO:0000269|PubMed:9737988, ECO:0000269|PubMed:9737989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-
CC fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304;
CC EC=2.4.1.65; Evidence={ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23629;
CC Evidence={ECO:0000305|PubMed:7721776};
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:0000269|PubMed:29593094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={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)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-
CC L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-
CC (1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145342, ChEBI:CHEBI:145343;
CC Evidence={ECO:0000269|PubMed:29593094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000305|PubMed:29593094};
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:29593094,
CC ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000305|PubMed:29593094, ECO:0000305|PubMed:7721776};
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:7721776, ECO:0000269|PubMed:9737988};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48377;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-ceramide + GDP + H(+); Xref=Rhea:RHEA:48364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90357, ChEBI:CHEBI:90358;
CC Evidence={ECO:0000269|PubMed:17604274, ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48365;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc6Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside III(3)-alpha-Fuc-nLc6Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48336, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:61610, ChEBI:CHEBI:90307;
CC Evidence={ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48337;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside III(3)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48332, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:77240;
CC Evidence={ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48333;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-
CC beta-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; Xref=Rhea:RHEA:48352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90335, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000269|PubMed:17604274, ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48353;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62824, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60152,
CC ChEBI:CHEBI:62287; Evidence={ECO:0000269|PubMed:1740457,
CC ECO:0000269|PubMed:7721776, ECO:0000269|PubMed:9737988,
CC ECO:0000269|PubMed:9737989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62825;
CC Evidence={ECO:0000305|PubMed:7721776, ECO:0000305|PubMed:9737989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosamine = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosamine; Xref=Rhea:RHEA:62836,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145937, ChEBI:CHEBI:145938;
CC Evidence={ECO:0000269|PubMed:1740457, ECO:0000269|PubMed:7721776,
CC ECO:0000269|PubMed:9737989};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62837;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc + GDP-beta-L-
CC fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-
CC GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62900, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62263,
CC ChEBI:CHEBI:62507; Evidence={ECO:0000269|PubMed:9737989};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-
CC L-Fuc-(1->4)]-beta-D-GlcNAc derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62904, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:146021, ChEBI:CHEBI:146022;
CC Evidence={ECO:0000269|PubMed:7721776};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62905;
CC Evidence={ECO:0000305|PubMed:7721776};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38 uM for GDP-fucose {ECO:0000269|PubMed:14718375};
CC KM=1.1 uM for alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc-sp-biotin
CC {ECO:0000269|PubMed:14718375};
CC KM=18.8 uM for GDP-fucose {ECO:0000269|PubMed:9737989};
CC KM=60 mM for beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
CC {ECO:0000269|PubMed:9737988};
CC KM=3.4 mM for beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
CC {ECO:0000269|PubMed:9737988};
CC Vmax=1 nmol/h/mg enzyme toward GDP-fucose
CC {ECO:0000269|PubMed:14718375};
CC Vmax=38 nmol/h/mg enzyme toward alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-
CC D-GlcNAc-sp-biotin {ECO:0000269|PubMed:14718375};
CC Note=kcat is 1.70 min(-1) for the alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->4)-D-GlcNAc (PubMed:9737989). kcat is 9.3 min(-1) for the beta-D-
CC galactosyl-(1->4)-N-acetyl-D-glucosamine (PubMed:9737988).
CC {ECO:0000269|PubMed:9737988, ECO:0000269|PubMed:9737989};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:29593094, ECO:0000269|PubMed:7721776}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- TISSUE SPECIFICITY: Liver, colon and testis and trace amounts in T-
CC cells and brain.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_602";
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DR EMBL; M81485; AAA98117.1; -; Genomic_DNA.
DR EMBL; U27329; AAC50188.1; -; mRNA.
DR EMBL; U27330; AAC50189.1; -; mRNA.
DR EMBL; AK291087; BAF83776.1; -; mRNA.
DR EMBL; AC024592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69134.1; -; Genomic_DNA.
DR EMBL; BC140905; AAI40906.1; -; mRNA.
DR CCDS; CCDS12154.1; -.
DR PIR; A42270; A42270.
DR RefSeq; NP_002025.2; NM_002034.2.
DR AlphaFoldDB; Q11128; -.
DR SMR; Q11128; -.
DR STRING; 9606.ENSP00000466880; -.
DR BindingDB; Q11128; -.
DR ChEMBL; CHEMBL3146; -.
DR SwissLipids; SLP:000001430; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q11128; 4 sites.
DR iPTMnet; Q11128; -.
DR PhosphoSitePlus; Q11128; -.
DR BioMuta; FUT5; -.
DR DMDM; 1730135; -.
DR jPOST; Q11128; -.
DR MassIVE; Q11128; -.
DR MaxQB; Q11128; -.
DR PaxDb; Q11128; -.
DR PeptideAtlas; Q11128; -.
DR PRIDE; Q11128; -.
DR ProteomicsDB; 58871; -.
DR Antibodypedia; 24015; 37 antibodies from 11 providers.
DR DNASU; 2527; -.
DR Ensembl; ENST00000252675.6; ENSP00000252675.5; ENSG00000130383.7.
DR GeneID; 2527; -.
DR KEGG; hsa:2527; -.
DR UCSC; uc060sei.1; human.
DR CTD; 2527; -.
DR DisGeNET; 2527; -.
DR GeneCards; FUT5; -.
DR HGNC; HGNC:4016; FUT5.
DR HPA; ENSG00000130383; Not detected.
DR MIM; 136835; gene.
DR neXtProt; NX_Q11128; -.
DR PharmGKB; PA28432; -.
DR VEuPathDB; HostDB:ENSG00000130383; -.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q11128; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q11128; -.
DR BioCyc; MetaCyc:HS05379-MON; -.
DR BRENDA; 2.4.1.152; 2681.
DR BRENDA; 2.4.1.65; 2681.
DR PathwayCommons; Q11128; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2527; 10 hits in 1053 CRISPR screens.
DR GeneWiki; FUT5; -.
DR GenomeRNAi; 2527; -.
DR Pharos; Q11128; Tbio.
DR PRO; PR:Q11128; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q11128; protein.
DR Bgee; ENSG00000130383; Expressed in lower esophagus mucosa and 27 other tissues.
DR ExpressionAtlas; Q11128; baseline and differential.
DR Genevisible; Q11128; HS.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017060; F:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; 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; IDA:BHF-UCL.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA: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 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..374
FT /note="4-galactosyl-N-acetylglucosaminide 3-alpha-L-
FT fucosyltransferase FUT5"
FT /id="PRO_0000221105"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 187
FT /note="P -> L (in dbSNP:rs778970)"
FT /id="VAR_022122"
FT VARIANT 338
FT /note="T -> M (in dbSNP:rs4807054)"
FT /id="VAR_055845"
FT MUTAGEN 86
FT /note="N->H: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity
FT with type 2 oligosaccharide acceptor; when associated with
FT I-87 and S-92. Increases significantly 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity
FT with type 1 oligosaccharide acceptors; when associated with
FT I-87 and S-92. Decreases of 50% the 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity
FT with type 2 glycolipid nLc4Cer; when associated with I-87
FT and S-92. Increases significantly the 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity
FT with type 1 glycolipid Lc4Cer; when associated with I-87
FT and S-92."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 87
FT /note="T->I: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity;
FT when associated with H-86 and S-92. Increases significantly
FT 3-galactosyl-N-acetylglucosaminide 4-alpha-L-
FT fucosyltransferase activity; when associated with H-86 and
FT S-92. Decreases of 50% the 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity
FT with type 2 glycolipid nLc4Cer; when associated with H-86
FT and S-92. Increases significantly the 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity
FT with type 1 glycolipid Lc4Cer; when associated with H-86
FT and S-92."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 87
FT /note="T->K: Reverses the preferential fucosylation
FT properties leading to production of 72% of sialyl-lewis x;
FT when associated with R-124; E-125 and V-126. Significantly
FT decreases cell-surface expression of VIM2 antigen; when
FT associated with R-124; E-125 and V-126."
FT /evidence="ECO:0000269|PubMed:17604274"
FT MUTAGEN 92
FT /note="P->S: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity;
FT when associated with H-86 and I-87. Increases significantly
FT 3-galactosyl-N-acetylglucosaminide 4-alpha-L-
FT fucosyltransferase activity; when associated with H-86 and
FT I-87. Decreases of 50% the 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L-fucosyltransferase activity
FT with type 2 glycolipid nLc4Cer; when associated with H-86
FT and I-87. Increases significantly the 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity
FT with type 1 glycolipid Lc4Cer; when associated with H-86
FT and I-87."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 101
FT /note="A->T: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity;
FT when associated withH-105; R-110; K-111 and T-118."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 105
FT /note="N->H: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity;
FT when associated with T-101; R-110; K-111 and T-118."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 110
FT /note="S->R: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity;
FT when associated with T-101; H-105; K-111 and T-118."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 111
FT /note="S->K: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity;
FT when associated with T-101; H-105; R-110 and T-118."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 118
FT /note="A->T: Does not affect 4-galactosyl-N-
FT acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-
FT acetylglucosaminide 4-alpha-L-fucosyltransferase activity;
FT when associated with T-101; H-105; R-110 and K-111."
FT /evidence="ECO:0000269|PubMed:9737988"
FT MUTAGEN 124
FT /note="W->A: Decreases both alpha-(1,3)-fucosyltransferase
FT and alpha-(1,4)-fucosyltransferase activity of 50%."
FT /evidence="ECO:0000269|PubMed:14718375"
FT MUTAGEN 124
FT /note="W->R: Increases alpha-(1,3)-fucosyltransferase
FT activity. Loss of alpha-(1,4)-fucosyltransferase activity.
FT Loss of site-specific fucosylation; when associated with E-
FT 125 and V-126. Reverses the preferential fucosylation
FT properties leading to production of 72% of sialyl-lewis x;
FT when associated with K-87; E-125 and V-126. Significantly
FT decreases to cell-surface expression of VIM2 antigen; when
FT associated with K-87; E-125 and V-126."
FT /evidence="ECO:0000269|PubMed:14718375,
FT ECO:0000269|PubMed:17604274"
FT MUTAGEN 124
FT /note="W->V: Does not affect alpha-(1,3)-fucosyltransferase
FT activity. Loss of alpha-(1,4)-fucosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:14718375"
FT MUTAGEN 125
FT /note="D->E: Loss of site-specific fucosylation; when
FT associated with R-124 and V-126. Reverses the preferential
FT fucosylation properties leading to production of 72% of
FT sialyl-lewis x; when associated with K-87; R-124 and V-126.
FT Significantly decreases to cell-surface expression of VIM2
FT antigen; when associated with K-87; R-124 and V-126."
FT /evidence="ECO:0000269|PubMed:17604274"
FT MUTAGEN 126
FT /note="I->V: Loss of site-specific fucosylation; when
FT associated with R-124 and E-125. Reverses the preferential
FT fucosylation properties leading to production of 72% of
FT sialyl-lewis x; when associated with K-87; R-124 and E-125.
FT Significantly decreases to cell-surface expression of VIM2
FT antigen; when associated with K-87; R-124 and E-125."
FT /evidence="ECO:0000269|PubMed:17604274"
SQ SEQUENCE 374 AA; 43008 MW; B825281521B57939 CRC64;
MDPLGPAKPQ WLWRRCLAGL LFQLLVAVCF FSYLRVSRDD ATGSPRPGLM AVEPVTGAPN
GSRCQDSMAT PAHPTLLILL WTWPFNTPVA LPRCSEMVPG AADCNITADS SVYPQADAVI
VHHWDIMYNP SANLPPPTRP QGQRWIWFSM ESPSNCRHLE ALDGYFNLTM SYRSDSDIFT
PYGWLEPWSG QPAHPPLNLS AKTELVAWAV SNWKPDSARV RYYQSLQAHL KVDVYGRSHK
PLPKGTMMET LSRYKFYLAF ENSLHPDYIT EKLWRNALEA WAVPVVLGPS RSNYERFLPP
DAFIHVDDFQ SPKDLARYLQ ELDKDHARYL SYFRWRETLR PRSFSWALAF CKACWKLQQE
SRYQTVRSIA AWFT
