ID   FUT5_HUMAN              Reviewed;         374 AA.
AC   Q11128; A8K4X2; K7ENC0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 2.
DT   27-MAR-2024, entry version 182.
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-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-
CC         D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + GDP-beta-
CC         L-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
CC         alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc-sp-biotin
CC         {ECO:0000269|PubMed:14718375};
CC         Note=kcat is 1.70 min(-1) for the
CC         alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc (PubMed:9737989). kcat
CC         is 9.3 min(-1) for the
CC         beta-D-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   GlyCosmos; Q11128; 4 sites, No reported glycans.
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; 9606-ENSP00000466880; -.
DR   PeptideAtlas; Q11128; -.
DR   PRIDE; Q11128; -.
DR   ProteomicsDB; 58871; -.
DR   Pumba; Q11128; -.
DR   Antibodypedia; 24015; 41 antibodies from 12 providers.
DR   DNASU; 2527; -.
DR   Ensembl; ENST00000252675.6; ENSP00000252675.5; ENSG00000130383.7.
DR   Ensembl; ENST00000588525.1; ENSP00000466880.1; ENSG00000130383.7.
DR   GeneID; 2527; -.
DR   KEGG; hsa:2527; -.
DR   MANE-Select; ENST00000588525.1; ENSP00000466880.1; NM_002034.2; NP_002025.2.
DR   UCSC; uc060sei.1; human.
DR   AGR; HGNC:4016; -.
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   OpenTargets; ENSG00000130383; -.
DR   PharmGKB; PA28432; -.
DR   VEuPathDB; HostDB:ENSG00000130383; -.
DR   eggNOG; KOG2619; Eukaryota.
DR   GeneTree; ENSGT00940000163389; -.
DR   HOGENOM; CLU_032075_4_1_1; -.
DR   InParanoid; Q11128; -.
DR   OMA; PQWPWRH; -.
DR   OrthoDB; 1331128at2759; -.
DR   PhylomeDB; Q11128; -.
DR   TreeFam; TF316348; -.
DR   BioCyc; MetaCyc:HS05379-MONOMER; -.
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; 13 hits in 1129 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 cell types or tissues.
DR   ExpressionAtlas; Q11128; baseline and differential.
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: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; 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:SF11; 4-GALACTOSYL-N-ACETYLGLUCOSAMINIDE 3-ALPHA-L-FUCOSYLTRANSFERASE FUT5; 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; Q11128; HS.
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
FT                   4-galactosyl-N-acetylglucosaminide
FT                   3-alpha-L-fucosyltransferase activity with type 2
FT                   oligosaccharide acceptor; when associated with I-87 and
FT                   S-92. Increases significantly
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity with type 1
FT                   oligosaccharide acceptors; when associated with I-87 and
FT                   S-92. Decreases of 50% the
FT                   4-galactosyl-N-acetylglucosaminide
FT                   3-alpha-L-fucosyltransferase activity with type 2
FT                   glycolipid nLc4Cer; when associated with I-87 and S-92.
FT                   Increases significantly the
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity with type 1
FT                   glycolipid Lc4Cer; when associated with I-87 and S-92."
FT                   /evidence="ECO:0000269|PubMed:9737988"
FT   MUTAGEN         87
FT                   /note="T->I: Does not affect
FT                   4-galactosyl-N-acetylglucosaminide
FT                   3-alpha-L-fucosyltransferase activity; when associated with
FT                   H-86 and S-92. Increases significantly
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated with
FT                   H-86 and S-92. Decreases of 50% the
FT                   4-galactosyl-N-acetylglucosaminide
FT                   3-alpha-L-fucosyltransferase activity with type 2
FT                   glycolipid nLc4Cer; when associated with H-86 and S-92.
FT                   Increases significantly the
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity with type 1
FT                   glycolipid Lc4Cer; when associated with H-86 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
FT                   4-galactosyl-N-acetylglucosaminide
FT                   3-alpha-L-fucosyltransferase activity; when associated with
FT                   H-86 and I-87. Increases significantly
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated with
FT                   H-86 and I-87. Decreases of 50% the
FT                   4-galactosyl-N-acetylglucosaminide
FT                   3-alpha-L-fucosyltransferase activity with type 2
FT                   glycolipid nLc4Cer; when associated with H-86 and I-87.
FT                   Increases significantly the
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity with type 1
FT                   glycolipid Lc4Cer; when associated with H-86 and I-87."
FT                   /evidence="ECO:0000269|PubMed:9737988"
FT   MUTAGEN         101
FT                   /note="A->T: Does not affect
FT                   4-galactosyl-N-acetylglucosaminide 3-alpha-L- and
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated
FT                   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
FT                   4-galactosyl-N-acetylglucosaminide 3-alpha-L- and
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated with
FT                   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
FT                   4-galactosyl-N-acetylglucosaminide 3-alpha-L- and
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated with
FT                   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
FT                   4-galactosyl-N-acetylglucosaminide 3-alpha-L- and
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated with
FT                   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
FT                   4-galactosyl-N-acetylglucosaminide 3-alpha-L- and
FT                   3-galactosyl-N-acetylglucosaminide
FT                   4-alpha-L-fucosyltransferase activity; when associated with
FT                   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
FT                   E-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"
FT   CONFLICT        334
FT                   /note="H -> R (in Ref. 1; AAA98117, 2; AAC50188/AAC50189,
FT                   3; BAF83776, 5; EAW69134 and 6; AAI40906)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  42989 MW;  A519DBC721B57939 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 SYFHWRETLR PRSFSWALAF CKACWKLQQE
     SRYQTVRSIA AWFT
//