FUT7_HUMAN
ID FUT7_HUMAN Reviewed; 342 AA.
AC Q11130; B2R7U7; Q6DK54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 7 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:11404359, ECO:0000269|PubMed:15632313, ECO:0000269|PubMed:15926890, ECO:0000269|PubMed:8207002, ECO:0000269|PubMed:8666674, ECO:0000269|PubMed:8752218, ECO:0000269|PubMed:9299472, ECO:0000269|PubMed:9499379};
DE AltName: Full=Fucosyltransferase 7;
DE AltName: Full=Fucosyltransferase VII {ECO:0000303|PubMed:8207002};
DE Short=Fuc-TVII {ECO:0000303|PubMed:8207002};
DE Short=FucT-VII;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
DE AltName: Full=Selectin ligand synthase;
GN Name=FUT7 {ECO:0000312|HGNC:HGNC:4018};
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], CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=8207002; DOI=10.1016/s0021-9258(19)89461-9;
RA Natsuka S., Gersten K.M., Zenita K., Kannagi R., Lowe J.B.;
RT "Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-
RT fucosyltransferase capable of synthesizing the sialyl Lewis x
RT determinant.";
RL J. Biol. Chem. 269:16789-16794(1994).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8051184; DOI=10.1016/s0021-9258(17)32066-5;
RA Natsuka S., Gersten K.M., Zenita K., Kannagi R., Lowe J.B.;
RT "Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-
RT fucosyltransferase capable of synthesizing the sialyl Lewis x
RT determinant.";
RL J. Biol. Chem. 269:20806-20806(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8182079; DOI=10.1016/s0021-9258(17)36686-3;
RA Sasaki K., Kurata K., Funayama K., Nagata M., Watanabe E., Ohta S.,
RA Hanai N., Nishi T.;
RT "Expression cloning of a novel alpha 1,3-fucosyltransferase that is
RT involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in
RT leukocytes.";
RL J. Biol. Chem. 269:14730-14737(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hiraiwa N., Hiraiwa M., Kannagi R.;
RT "The human selectin-ligand synthase (hFuc-T VII) gene structure and
RT characterization of the promoter.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Mammary gland;
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8752218; DOI=10.1016/s0092-8674(00)80137-3;
RA Maly P., Thall A., Petryniak B., Rogers C.E., Smith P.L., Marks R.M.,
RA Kelly R.J., Gersten K.M., Cheng G., Saunders T.L., Camper S.A.,
RA Camphausen R.T., Sullivan F.X., Isogai Y., Hindsgaul O., von Andrian U.H.,
RA Lowe J.B.;
RT "The alpha(1,3)fucosyltransferase Fuc-TVII controls leukocyte trafficking
RT through an essential role in L-, E-, and P-selectin ligand biosynthesis.";
RL Cell 86:643-653(1996).
RN [9]
RP INDUCTION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8666674; DOI=10.1083/jcb.133.4.911;
RA Knibbs R.N., Craig R.A., Natsuka S., Chang A., Cameron M., Lowe J.B.,
RA Stoolman L.M.;
RT "The fucosyltransferase FucT-VII regulates E-selectin ligand synthesis in
RT human T cells.";
RL J. Cell Biol. 133:911-920(1996).
RN [10]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9299472; DOI=10.1006/bbrc.1997.7254;
RA Stroud M.R., Holmes E.H.;
RT "Fucosylation of complex glycosphingolipids by recombinant
RT fucosyltransferase-VII.";
RL Biochem. Biophys. Res. Commun. 238:165-168(1997).
RN [11]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=9405391; DOI=10.1074/jbc.272.51.31992;
RA Shinoda K., Morishita Y., Sasaki K., Matsuda Y., Takahashi I., Nishi T.;
RT "Enzymatic characterization of human alpha1,3-fucosyltransferase Fuc-TVII
RT synthesized in a B cell lymphoma cell line.";
RL J. Biol. Chem. 272:31992-31997(1997).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9473504; DOI=10.1006/bbrc.1998.8080;
RA Handa K., Withers D.A., Hakomori S.;
RT "The alpha 1-->3 fucosylation at the penultimate GlcNAc catalyzed by
RT fucosyltransferase VII is blocked by internally fucosylated residue in
RT sialosyl long-chain poly-LacNAc: enzymatic basis for expression of
RT physiological E-selectin epitope.";
RL Biochem. Biophys. Res. Commun. 243:199-204(1998).
RN [13]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9499379; DOI=10.1093/glycob/8.4.321;
RA Britten C.J., van den Eijnden D.H., McDowell W., Kelly V.A., Witham S.J.,
RA Edbrooke M.R., Bird M.I., de Vries T., Smithers N.;
RT "Acceptor specificity of the human leukocyte alpha3 fucosyltransferase:
RT role of FucT-VII in the generation of selectin ligands.";
RL Glycobiology 8:321-327(1998).
RN [14]
RP ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=10386892; DOI=10.1023/a:1006953626578;
RA Shinoda K., Shitara K., Yoshihara Y., Kusano A., Uosaki Y., Ohta S.,
RA Hanai N., Takahashi I.;
RT "Panosialins, inhibitors of an alpha1,3-fucosyltransferase Fuc-TVII,
RT suppress the expression of selectin ligands on U937 cells.";
RL Glycoconj. J. 15:1079-1083(1998).
RN [15]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=9461592; DOI=10.1074/jbc.273.7.4021;
RA Niemelae R., Natunen J., Majuri M.L., Maaheimo H., Helin J., Lowe J.B.,
RA Renkonen O., Renkonen R.;
RT "Complementary acceptor and site specificities of Fuc-TIV and Fuc-TVII
RT allow effective biosynthesis of sialyl-TriLex and related polylactosamines
RT present on glycoprotein counterreceptors of selectins.";
RL J. Biol. Chem. 273:4021-4026(1998).
RN [16]
RP INDUCTION.
RX PubMed=9858509; DOI=10.1084/jem.188.12.2225;
RA Wagers A.J., Waters C.M., Stoolman L.M., Kansas G.S.;
RT "Interleukin 12 and interleukin 4 control T cell adhesion to endothelial
RT selectins through opposite effects on alpha1, 3-fucosyltransferase VII gene
RT expression.";
RL J. Exp. Med. 188:2225-2231(1998).
RN [17]
RP FUNCTION.
RX PubMed=9834120;
RA Knibbs R.N., Craig R.A., Maly P., Smith P.L., Wolber F.M., Faulkner N.E.,
RA Lowe J.B., Stoolman L.M.;
RT "Alpha(1,3)-fucosyltransferase VII-dependent synthesis of P- and E-selectin
RT ligands on cultured T lymphoblasts.";
RL J. Immunol. 161:6305-6315(1998).
RN [18]
RP FUNCTION.
RX PubMed=10200296; DOI=10.1073/pnas.96.8.4530;
RA Kimura N., Mitsuoka C., Kanamori A., Hiraiwa N., Uchimura K., Muramatsu T.,
RA Tamatani T., Kansas G.S., Kannagi R.;
RT "Reconstitution of functional L-selectin ligands on a cultured human
RT endothelial cell line by cotransfection of alpha1-->3 fucosyltransferase
RT VII and newly cloned GlcNAcbeta:6-sulfotransferase cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4530-4535(1999).
RN [19]
RP DISULFIDE BONDS.
RX PubMed=11425803; DOI=10.1093/glycob/11.5.423;
RA de Vries T., Yen T.Y., Joshi R.K., Storm J., van Den Eijnden D.H.,
RA Knegtel R.M.A., Bunschoten H., Joziasse D.H., Macher B.A.;
RT "Neighboring cysteine residues in human fucosyltransferase VII are engaged
RT in disulfide bridges, forming small loop structures.";
RL Glycobiology 11:423-432(2001).
RN [20]
RP ACTIVITY REGULATION.
RX PubMed=15081893; DOI=10.1016/j.abb.2004.02.039;
RA Niu X., Fan X., Sun J., Ting P., Narula S., Lundell D.;
RT "Inhibition of fucosyltransferase VII by gallic acid and its derivatives.";
RL Arch. Biochem. Biophys. 425:51-57(2004).
RN [21]
RP CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND ACTIVITY REGULATION.
RX PubMed=15632313; DOI=10.1093/jb/mvh179;
RA Miyashiro M., Furuya S., Sugita T.;
RT "Development of a sensitive separation and quantification method for sialyl
RT Lewis X and Lewis X involving anion-exchange chromatography: biochemical
RT characterization of alpha1-3 fucosyltransferase-VII.";
RL J. Biochem. 136:723-731(2004).
RN [22]
RP GLYCOSYLATION AT ASN-81 AND ASN-291, MUTAGENESIS OF ASN-81 AND ASN-291,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15926890; DOI=10.1042/bj20050344;
RA Prorok-Hamon M., Notel F., Mathieu S., Langlet C., Fukuda M.,
RA El-Battari A.;
RT "N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I)
RT but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required
RT for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1):
RT effects on P-, L- and E-selectin binding.";
RL Biochem. J. 391:491-502(2005).
RN [23]
RP FUNCTION.
RX PubMed=17229154; DOI=10.1111/j.1742-4658.2006.05599.x;
RA Wang Q.Y., Zhang Y., Chen H.J., Shen Z.H., Chen H.L.;
RT "Alpha 1,3-fucosyltransferase-VII regulates the signaling molecules of the
RT insulin receptor pathway.";
RL FEBS J. 274:526-538(2007).
RN [24]
RP FUNCTION.
RX PubMed=18553500; DOI=10.1002/iub.62;
RA Liu S., Zhang Y., Liu Y., Qin H., Wang X., Yan Q.;
RT "FUT7 antisense sequence inhibits the expression of FUT7/sLeX and adhesion
RT between embryonic and uterine cells.";
RL IUBMB Life 60:461-466(2008).
RN [25]
RP FUNCTION.
RX PubMed=18402946; DOI=10.1016/j.fertnstert.2007.12.012;
RA Zhang Y., Liu S., Liu Y., Wang Z., Wang X., Yan Q.;
RT "Overexpression of fucosyltransferase VII (FUT7) promotes embryo adhesion
RT and implantation.";
RL Fertil. Steril. 91:908-914(2009).
RN [26]
RP INDUCTION.
RX PubMed=19455659; DOI=10.1002/mrd.21055;
RA Zhang Q., Liu S., Zhu Z., Yan Q.;
RT "Regulating effect of LIF on the expression of FuT7: Probe into the
RT mechanism of sLe(x) in implantation.";
RL Mol. Reprod. Dev. 76:692-692(2009).
RN [27]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [28]
RP INDUCTION, AND FUNCTION.
RX PubMed=29138114; DOI=10.1016/j.lfs.2017.11.017;
RA Zhang J., Ju N., Yang X., Chen L., Yu C.;
RT "The alpha1,3-fucosyltransferase FUT7 regulates IL-1beta-induced monocyte-
RT endothelial adhesion via fucosylation of endomucin.";
RL Life Sci. 192:231-237(2018).
RN [29]
RP VARIANT GLN-110, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT GLN-110,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=11404359; DOI=10.1074/jbc.m104165200;
RA Bengtson P., Larson C., Lundblad A., Larson G., Paahlsson P.;
RT "Identification of a missense mutation (G329A;Arg(110)--> GLN) in the human
RT FUT7 gene.";
RL J. Biol. Chem. 276:31575-31582(2001).
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 alpha2,3 sialylated lactosamine unit of a glycoprotein or a
CC glycolipid-linked sialopolylactosamines chain through an alpha-1,3
CC glycosidic linkage and participates in the final fucosylation step in
CC the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate
CC involved in cell and matrix adhesion during leukocyte trafficking and
CC fertilization (PubMed:8207002, PubMed:8752218, PubMed:8666674,
CC PubMed:9299472, PubMed:9405391, PubMed:9473504, PubMed:9499379,
CC PubMed:9461592, PubMed:15632313, PubMed:15926890, PubMed:18553500,
CC PubMed:18402946, PubMed:11404359, PubMed:29593094). In vitro, also
CC synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and
CC both di-fucosylated and trifucosylated structures from mono-fucosylated
CC precursors (PubMed:9499379). However does not catalyze alpha 1-3
CC fucosylation when an internal alpha 1-3 fucosylation is present in
CC polylactosamine chain and the fucosylation rate of the internal GlcNAc
CC residues is reduced once fucose has been added to the distal GlcNAc
CC (PubMed:9473504, PubMed:9499379). Also catalyzes the transfer of a
CC fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated
CC substrate to produce 6-sulfo sLex mediating significant L-selectin-
CC dependent cell adhesion (PubMed:10200296, PubMed:8752218). Through
CC sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell
CC adhesion with leukocytes and allows leukocytes tethering and rolling
CC along the endothelial tissue thereby enabling the leukocytes to
CC accumulate at a site of inflammation (PubMed:10386892, PubMed:29138114,
CC PubMed:8666674, PubMed:9473504, PubMed:9834120). May enhance embryo
CC implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo
CC cells to endometrium (PubMed:18402946, PubMed:18553500). May affect
CC insulin signaling by up-regulating the phosphorylation and expression
CC of some signaling molecules involved in the insulin-signaling pathway
CC through SLe(x) which is present on the glycans of the INSRR alpha
CC subunit (PubMed:17229154). {ECO:0000269|PubMed:10200296,
CC ECO:0000269|PubMed:10386892, ECO:0000269|PubMed:11404359,
CC ECO:0000269|PubMed:15632313, ECO:0000269|PubMed:15926890,
CC ECO:0000269|PubMed:17229154, ECO:0000269|PubMed:18402946,
CC ECO:0000269|PubMed:18553500, ECO:0000269|PubMed:29138114,
CC ECO:0000269|PubMed:8207002, ECO:0000269|PubMed:8666674,
CC ECO:0000269|PubMed:8752218, ECO:0000269|PubMed:9299472,
CC ECO:0000269|PubMed:9405391, ECO:0000269|PubMed:9461592,
CC ECO:0000269|PubMed:9473504, ECO:0000269|PubMed:9499379,
CC ECO:0000269|PubMed:9834120}.
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:11404359, ECO:0000269|PubMed:15632313,
CC ECO:0000269|PubMed:15926890, ECO:0000269|PubMed:29593094,
CC ECO:0000269|PubMed:8207002, ECO:0000269|PubMed:8666674,
CC ECO:0000269|PubMed:8752218, ECO:0000269|PubMed:9299472,
CC ECO:0000269|PubMed:9461592, ECO:0000269|PubMed:9499379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000305|PubMed:29593094, ECO:0000305|PubMed:9499379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer + GDP-beta-L-fucose =
CC GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48392, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90390, ChEBI:CHEBI:90392;
CC Evidence={ECO:0000269|PubMed:9299472};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48393;
CC Evidence={ECO:0000305|PubMed:9299472};
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)-[alpha-L-
CC fucosyl-(1->3)]-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;
CC Xref=Rhea:RHEA:48356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90336, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000269|PubMed:9299472};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48357;
CC Evidence={ECO:0000305|PubMed:9299472};
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, ECO:0000269|PubMed:9499379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000269|PubMed:29593094, ECO:0000305|PubMed:9499379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S
CC derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345;
CC Evidence={ECO:0000269|PubMed:8752218};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000305|PubMed:8752218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-D-Glc + GDP + H(+); Xref=Rhea:RHEA:62008,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145346, ChEBI:CHEBI:145347;
CC Evidence={ECO:0000269|PubMed:9405391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62009;
CC Evidence={ECO:0000305|PubMed:9405391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=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-(1->3)-beta-D-
CC Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62060,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145400, ChEBI:CHEBI:145401;
CC Evidence={ECO:0000269|PubMed:9473504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62061;
CC Evidence={ECO:0000305|PubMed:9473504};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-
CC [alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H(+);
CC Xref=Rhea:RHEA:62056, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145398, ChEBI:CHEBI:145399;
CC Evidence={ECO:0000269|PubMed:9461592, ECO:0000269|PubMed:9473504};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62057;
CC Evidence={ECO:0000305|PubMed:9461592, ECO:0000305|PubMed:9473504};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl (Probable). Inhibited by GDP in
CC a concentration dependent manner, with an IC(50) value of 93 uM
CC (PubMed:9405391, PubMed:15632313). Also inhibited by GMP and GTP
CC (PubMed:9405391). Inhibited by N-ethylmaleimide (Probable). Activated
CC by poly(ethylene glycol) by enhancing the thermal stability of FUT7
CC (PubMed:9405391). Activated by Mn2+, Ca2+, and Mg2+ (PubMed:9405391).
CC Both panosialin A and B inhibit activity with IC(50) values of 4.8 and
CC 5.3 ug/ml, respectively (PubMed:10386892). Inhibited by gallic acid
CC (GA) and (-)-epigallocatechin gallate (EGCG) in a time-dependent and
CC irreversible manner with IC(50) values of 60 and 700 nM, respectively
CC (PubMed:15081893). {ECO:0000269|PubMed:10386892,
CC ECO:0000269|PubMed:15081893, ECO:0000269|PubMed:15632313,
CC ECO:0000269|PubMed:9405391, ECO:0000305|PubMed:9405391}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for GDP-fucose {ECO:0000269|PubMed:11404359};
CC KM=8 uM for GDP-fucose {ECO:0000269|PubMed:9499379};
CC KM=1.6 mM for N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-
CC (1->4)-N-acetyl-beta-D-glucosaminyl {ECO:0000269|PubMed:9499379};
CC KM=16.4 uM for GDP-fucose {ECO:0000269|PubMed:9405391};
CC KM=3.08 mM for alpha2,3-sialyl lacto-N-neotetraose
CC {ECO:0000269|PubMed:9405391};
CC KM=7.8 mM for alpha2-3 sialyl N-acetyllactosamine
CC {ECO:0000269|PubMed:15632313};
CC KM=21 uM for GDP-fucose {ECO:0000269|PubMed:15632313};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9405391};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:9405391};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8207002}.
CC -!- INTERACTION:
CC Q11130; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-12817667, EBI-12019274;
CC Q11130; Q07325: CXCL9; NbExp=3; IntAct=EBI-12817667, EBI-3911467;
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: Leukocytic/myeloid lineage cells.
CC -!- INDUCTION: By T-cell activation (PubMed:8666674). Up-regulated by LIF
CC (PubMed:19455659). Induced by IL1B (PubMed:29138114). Induced at higher
CC levels by interleukin 12 in activated T cells (PubMed:9858509). Down-
CC regulated by IL4 (PubMed:9858509). {ECO:0000269|PubMed:19455659,
CC ECO:0000269|PubMed:29138114, ECO:0000269|PubMed:8666674,
CC ECO:0000269|PubMed:9858509}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15632313}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 7;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_604";
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DR EMBL; X78031; CAA54962.1; -; mRNA.
DR EMBL; U11282; AAA20468.1; -; mRNA.
DR EMBL; U08112; AAA56869.1; -; mRNA.
DR EMBL; AB012668; BAA32819.1; -; Genomic_DNA.
DR EMBL; AK313124; BAG35944.1; -; mRNA.
DR EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074746; AAH74746.2; -; mRNA.
DR EMBL; BC086312; AAH86312.1; -; mRNA.
DR CCDS; CCDS7022.1; -.
DR PIR; A54057; A54057.
DR RefSeq; NP_004470.1; NM_004479.3.
DR AlphaFoldDB; Q11130; -.
DR BioGRID; 108805; 7.
DR IntAct; Q11130; 2.
DR STRING; 9606.ENSP00000318142; -.
DR BindingDB; Q11130; -.
DR ChEMBL; CHEMBL3596077; -.
DR SwissLipids; SLP:000001438; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR GlyGen; Q11130; 2 sites.
DR iPTMnet; Q11130; -.
DR PhosphoSitePlus; Q11130; -.
DR BioMuta; FUT7; -.
DR MassIVE; Q11130; -.
DR PaxDb; Q11130; -.
DR PeptideAtlas; Q11130; -.
DR PRIDE; Q11130; -.
DR ProteomicsDB; 58872; -.
DR Antibodypedia; 32341; 157 antibodies from 26 providers.
DR DNASU; 2529; -.
DR Ensembl; ENST00000314412.7; ENSP00000318142.6; ENSG00000180549.8.
DR GeneID; 2529; -.
DR KEGG; hsa:2529; -.
DR MANE-Select; ENST00000314412.7; ENSP00000318142.6; NM_004479.4; NP_004470.1.
DR UCSC; uc004ckq.3; human.
DR CTD; 2529; -.
DR DisGeNET; 2529; -.
DR GeneCards; FUT7; -.
DR HGNC; HGNC:4018; FUT7.
DR HPA; ENSG00000180549; Group enriched (bone marrow, brain, lymphoid tissue).
DR MIM; 602030; gene.
DR neXtProt; NX_Q11130; -.
DR OpenTargets; ENSG00000180549; -.
DR PharmGKB; PA28434; -.
DR VEuPathDB; HostDB:ENSG00000180549; -.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000161618; -.
DR HOGENOM; CLU_032075_4_1_1; -.
DR InParanoid; Q11130; -.
DR OMA; SDTCTRY; -.
DR OrthoDB; 551308at2759; -.
DR PhylomeDB; Q11130; -.
DR TreeFam; TF316348; -.
DR BioCyc; MetaCyc:HS11506-MON; -.
DR BRENDA; 2.4.1.152; 2681.
DR BRENDA; 2.4.1.214; 2681.
DR BRENDA; 2.4.1.65; 2681.
DR PathwayCommons; Q11130; -.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SABIO-RK; Q11130; -.
DR SignaLink; Q11130; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2529; 10 hits in 1061 CRISPR screens.
DR GeneWiki; FUT7; -.
DR GenomeRNAi; 2529; -.
DR Pharos; Q11130; Tchem.
DR PRO; PR:Q11130; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q11130; protein.
DR Bgee; ENSG00000180549; Expressed in olfactory bulb and 179 other tissues.
DR Genevisible; Q11130; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
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; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; 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; IDA:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0006672; P:ceramide metabolic process; IDA:BHF-UCL.
DR GO; GO:0007566; P:embryo implantation; IMP:UniProtKB.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0002522; P:leukocyte migration involved in immune response; IEA:Ensembl.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; ISS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR GO; GO:0060353; P:regulation of cell adhesion molecule production; IMP:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IMP: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 GO; GO:2000389; P:regulation of neutrophil extravasation; IEA:Ensembl.
DR GO; GO:0001807; P:regulation of type IV hypersensitivity; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; IEA:Ensembl.
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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..342
FT /note="Alpha-(1,3)-fucosyltransferase 7"
FT /id="PRO_0000221113"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..342
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15926890"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15926890"
FT DISULFID 68..76
FT /evidence="ECO:0000269|PubMed:11425803"
FT DISULFID 211..214
FT /evidence="ECO:0000269|PubMed:11425803"
FT DISULFID 318..321
FT /evidence="ECO:0000269|PubMed:11425803"
FT VARIANT 110
FT /note="R -> Q (found in patients with ulcerative colitis;
FT loss of alpha-(1,3)-fucosyltransferase activity;
FT dbSNP:rs545570871)"
FT /evidence="ECO:0000269|PubMed:11404359"
FT /id="VAR_079131"
FT MUTAGEN 81
FT /note="N->Q: Impairs glycosylation. Impairs glycosylation;
FT when associated with Q-291. Does not affect SELP and SELL
FT binding on SELPLG. Does not affect SELP and SELL binding on
FT SELPLG; when associated with Q-291. Abolishes alpha-(1,3)-
FT fucosyltransferase activity. Abolishes alpha-(1,3)-
FT fucosyltransferase activity; when associated with Q-291.
FT Fails to synthetises sLe(x) antigens or to generate SELE
FT binding. Fails to synthetises sLe(x) antigens or to
FT generate SELE binding; when associated with Q-291. Does not
FT affect sLe(x) antigens synthesis or SELE binding only in
FT presence of SELPLG and GCNT1; when associated with Q-291."
FT /evidence="ECO:0000269|PubMed:15926890"
FT MUTAGEN 291
FT /note="N->Q: Slightly affects glycosylation. Impairs
FT glycosylation; when associated with Q-81. Does not affect
FT SELP and SELL binding on SELPLG. Does not affect SELP and
FT SELL binding on SELPLG; when associated with Q-81.
FT Abolishes alpha-(1,3)-fucosyltransferase activity.
FT Abolishes alpha-(1,3)-fucosyltransferase activity; when
FT associated with Q-81. Fails to synthetises sLe(x) antigens
FT or to generate SELE binding. Fails to synthetises sLe(x)
FT antigens or to generate SELE binding; when associated with
FT Q-81. Does not affect sLe(x) antigens synthesis or SELE
FT binding only in presence of SELPLG and GCNT1; when
FT associated with Q-81."
FT /evidence="ECO:0000269|PubMed:15926890"
FT CONFLICT 161..162
FT /note="GP -> A (in Ref. 1; AAA56869)"
FT /evidence="ECO:0000305"
FT CONFLICT 304..305
FT /note="RL -> SV (in Ref. 1; AAA56869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 39239 MW; D31BFF90DD64DFAB CRC64;
MNNAGHGPTR RLRGLGVLAG VALLAALWLL WLLGSAPRGT PAPQPTITIL VWHWPFTDQP
PELPSDTCTR YGIARCHLSA NRSLLASADA VVFHHRELQT RRSHLPLAQR PRGQPWVWAS
MESPSHTHGL SHLRGIFNWV LSYRRDSDIF VPYGRLEPHW GPSPPLPAKS RVAAWVVSNF
QERQLRARLY RQLAPHLRVD VFGRANGRPL CASCLVPTVA QYRFYLSFEN SQHRDYITEK
FWRNALVAGT VPVVLGPPRA TYEAFVPADA FVHVDDFGSA RELAAFLTGM NESRYQRFFA
WRDRLRVRLF TDWRERFCAI CDRYPHLPRS QVYEDLEGWF QA
