Full text data of FUT7
FUT7
[Confidence: low (only semi-automatic identification from reviews)]
Alpha-(1,3)-fucosyltransferase 7; 2.4.1.- (Fucosyltransferase 7; Fucosyltransferase VII; Fuc-TVII; FucT-VII; Galactoside 3-L-fucosyltransferase; Selectin ligand synthase)
Alpha-(1,3)-fucosyltransferase 7; 2.4.1.- (Fucosyltransferase 7; Fucosyltransferase VII; Fuc-TVII; FucT-VII; Galactoside 3-L-fucosyltransferase; Selectin ligand synthase)
UniProt
Q11130
ID FUT7_HUMAN Reviewed; 342 AA.
AC Q11130; B2R7U7; Q6DK54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 7;
DE EC=2.4.1.-;
DE AltName: Full=Fucosyltransferase 7;
DE AltName: Full=Fucosyltransferase VII;
DE Short=Fuc-TVII;
DE Short=FucT-VII;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
DE AltName: Full=Selectin ligand synthase;
GN Name=FUT7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8207002;
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-
RT 1,3-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;
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-
RT 1,3-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;
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
RT determinants in 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT engaged in disulfide bridges, forming small loop structures.";
RL Glycobiology 11:423-432(2001).
CC -!- FUNCTION: May catalyze alpha-1,3 glycosidic linkages involved in
CC the expression of sialyl Lewis X antigens.
CC -!- CATALYTIC ACTIVITY: GDP-L-fucose + alpha-2,3-Neu-N-acetyl-1,4-
CC beta-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + alpha-2,3-Neu-
CC N-acetyl-1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-
CC glucosaminyl-R.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
CC Single-pass type II membrane protein. Note=Membrane-bound form in
CC trans cisternae of Golgi.
CC -!- TISSUE SPECIFICITY: Leukocytic/myeloid lineage cells.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/Homolog?cat=symbol&symbol;=FUT7";
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; CAI12771.1; -; Genomic_DNA.
DR EMBL; BC074746; AAH74746.2; -; mRNA.
DR EMBL; BC086312; AAH86312.1; -; mRNA.
DR PIR; A54057; A54057.
DR RefSeq; NP_004470.1; NM_004479.3.
DR UniGene; Hs.457; -.
DR ProteinModelPortal; Q11130; -.
DR SMR; Q11130; 167-307.
DR STRING; 9606.ENSP00000318142; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PhosphoSite; Q11130; -.
DR DMDM; 1730137; -.
DR PaxDb; Q11130; -.
DR PRIDE; Q11130; -.
DR DNASU; 2529; -.
DR Ensembl; ENST00000314412; ENSP00000318142; ENSG00000180549.
DR GeneID; 2529; -.
DR KEGG; hsa:2529; -.
DR UCSC; uc004ckq.2; human.
DR CTD; 2529; -.
DR GeneCards; GC09M139924; -.
DR HGNC; HGNC:4018; FUT7.
DR MIM; 602030; gene.
DR neXtProt; NX_Q11130; -.
DR PharmGKB; PA28434; -.
DR eggNOG; NOG252779; -.
DR HOGENOM; HOG000045583; -.
DR HOVERGEN; HBG000274; -.
DR InParanoid; Q11130; -.
DR KO; K07635; -.
DR OMA; DTCTRYG; -.
DR OrthoDB; EOG7Z69C9; -.
DR PhylomeDB; Q11130; -.
DR BRENDA; 2.4.1.65; 2681.
DR UniPathway; UPA00378; -.
DR GeneWiki; FUT7; -.
DR GenomeRNAi; 2529; -.
DR NextBio; 9967; -.
DR PRO; PR:Q11130; -.
DR Bgee; Q11130; -.
DR CleanEx; HS_FUT7; -.
DR Genevestigator; Q11130; -.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; TAS:UniProtKB.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
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:0006486; P:protein glycosylation; TAS:UniProtKB.
DR InterPro; IPR001503; Glyco_trans_10.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 342 Alpha-(1,3)-fucosyltransferase 7.
FT /FTId=PRO_0000221113.
FT TOPO_DOM 1 14 Cytoplasmic (Potential).
FT TRANSMEM 15 36 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 37 342 Lumenal (Potential).
FT CARBOHYD 81 81 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 291 291 N-linked (GlcNAc...) (Potential).
FT DISULFID 68 76
FT DISULFID 211 214
FT DISULFID 318 321
FT CONFLICT 161 162 GP -> A (in Ref. 1; AAA56869).
FT CONFLICT 304 305 RL -> SV (in Ref. 1; AAA56869).
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
//
ID FUT7_HUMAN Reviewed; 342 AA.
AC Q11130; B2R7U7; Q6DK54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 7;
DE EC=2.4.1.-;
DE AltName: Full=Fucosyltransferase 7;
DE AltName: Full=Fucosyltransferase VII;
DE Short=Fuc-TVII;
DE Short=FucT-VII;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
DE AltName: Full=Selectin ligand synthase;
GN Name=FUT7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8207002;
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-
RT 1,3-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;
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-
RT 1,3-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;
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
RT determinants in 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT engaged in disulfide bridges, forming small loop structures.";
RL Glycobiology 11:423-432(2001).
CC -!- FUNCTION: May catalyze alpha-1,3 glycosidic linkages involved in
CC the expression of sialyl Lewis X antigens.
CC -!- CATALYTIC ACTIVITY: GDP-L-fucose + alpha-2,3-Neu-N-acetyl-1,4-
CC beta-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + alpha-2,3-Neu-
CC N-acetyl-1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-
CC glucosaminyl-R.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
CC Single-pass type II membrane protein. Note=Membrane-bound form in
CC trans cisternae of Golgi.
CC -!- TISSUE SPECIFICITY: Leukocytic/myeloid lineage cells.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/Homolog?cat=symbol&symbol;=FUT7";
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; CAI12771.1; -; Genomic_DNA.
DR EMBL; BC074746; AAH74746.2; -; mRNA.
DR EMBL; BC086312; AAH86312.1; -; mRNA.
DR PIR; A54057; A54057.
DR RefSeq; NP_004470.1; NM_004479.3.
DR UniGene; Hs.457; -.
DR ProteinModelPortal; Q11130; -.
DR SMR; Q11130; 167-307.
DR STRING; 9606.ENSP00000318142; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PhosphoSite; Q11130; -.
DR DMDM; 1730137; -.
DR PaxDb; Q11130; -.
DR PRIDE; Q11130; -.
DR DNASU; 2529; -.
DR Ensembl; ENST00000314412; ENSP00000318142; ENSG00000180549.
DR GeneID; 2529; -.
DR KEGG; hsa:2529; -.
DR UCSC; uc004ckq.2; human.
DR CTD; 2529; -.
DR GeneCards; GC09M139924; -.
DR HGNC; HGNC:4018; FUT7.
DR MIM; 602030; gene.
DR neXtProt; NX_Q11130; -.
DR PharmGKB; PA28434; -.
DR eggNOG; NOG252779; -.
DR HOGENOM; HOG000045583; -.
DR HOVERGEN; HBG000274; -.
DR InParanoid; Q11130; -.
DR KO; K07635; -.
DR OMA; DTCTRYG; -.
DR OrthoDB; EOG7Z69C9; -.
DR PhylomeDB; Q11130; -.
DR BRENDA; 2.4.1.65; 2681.
DR UniPathway; UPA00378; -.
DR GeneWiki; FUT7; -.
DR GenomeRNAi; 2529; -.
DR NextBio; 9967; -.
DR PRO; PR:Q11130; -.
DR Bgee; Q11130; -.
DR CleanEx; HS_FUT7; -.
DR Genevestigator; Q11130; -.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; TAS:UniProtKB.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
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:0006486; P:protein glycosylation; TAS:UniProtKB.
DR InterPro; IPR001503; Glyco_trans_10.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 342 Alpha-(1,3)-fucosyltransferase 7.
FT /FTId=PRO_0000221113.
FT TOPO_DOM 1 14 Cytoplasmic (Potential).
FT TRANSMEM 15 36 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 37 342 Lumenal (Potential).
FT CARBOHYD 81 81 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 291 291 N-linked (GlcNAc...) (Potential).
FT DISULFID 68 76
FT DISULFID 211 214
FT DISULFID 318 321
FT CONFLICT 161 162 GP -> A (in Ref. 1; AAA56869).
FT CONFLICT 304 305 RL -> SV (in Ref. 1; AAA56869).
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
//
MIM
602030
*RECORD*
*FIELD* NO
602030
*FIELD* TI
*602030 FUCOSYLTRANSFERASE 7; FUT7
*FIELD* TX
CLONING
The sialyl Lewis x oligosaccharide determinant is an essential component
read moreof leukocyte counterreceptors for E-selectin (131210)- and P-selectin
(173610)-mediated adhesions of leukocytes. This oligosaccharide molecule
is displayed on the surfaces of granulocytes, monocytes, and natural
killer cells. Formation of leukocyte adhesions to these selectins is an
early and important step in the process that ultimately allows
leukocytes to leave the vascular tree and become recruited into lymphoid
tissues and sites of inflammation. Natsuka et al. (1994) and Sasaki et
al. (1994) isolated cDNAs encoding a human leukocyte
alpha-1,3-fucosyltransferase, FUT7, capable of synthesizing the sialyl
Lewis x determinant. The cDNA predicts a 342-amino acid type II
transmembrane protein typical of mammalian glycosyltransferases. By
Northern blot analysis, Natsuka et al. (1994) showed that FUT7 was
expressed in HL-60 cells, a human promyelocytic cell line, and in YT
cells, a natural killer-like cell line. Sequence comparisons indicate
that the predicted polypeptide sequence shares approximately 38 to 47%
overall identity with other FUTs (e.g., FUT3, 111100; FUT6, 136836).
GENE FUNCTION
Natsuka et al. (1994) found when FUT7 was expressed in mammalian cells,
the cDNA directed synthesis of cell surface sialyl Lewis x moieties, but
not Lewis x, Lewis A, sialyl Lewis a, or VIM-2 determinants. Sasaki et
al. (1994) demonstrated in vivo ability of FUT7 to synthesize the sialyl
Lewis x moiety that binds to E-selectin and reported the restricted
expression of FUT7 in leukocytes.
Mahdavi et al. (2002) identified sialyl-dimeric-Lewis x
glycosphingolipid as a receptor for H. pylori and showed that H. pylori
infection induced formation of sialyl-Lewis x antigens in gastric
epithelium in humans and in a Rhesus monkey. The corresponding sialic
acid-binding adhesin was identified as sabA. Mahdavi et al. (2002)
concluded that the ability of many H. pylori strains to adhere to
sialylated glycoconjugates expressed during chronic inflammation might
contribute to virulence and the extraordinary chronicity of H. pylori
infection.
Chen et al. (2006) noted that activated T cells, particularly Th1 cells,
express sialyl Lewis x, but resting T cells do not. Using reporter
analysis, they showed that TBET (TBX21; 604895) promoted and GATA3
(131320) repressed transcription of FUT7. TBET interfered with GATA3
binding to its target DNA, but GATA3 also interfered with TBET binding
to the FUT7 promoter. GATA3 regulated FUT7 transcription by recruiting,
in a phosphorylation-dependent manner, histone deacetylase-3 (HDAC3;
605166) and HDAC5 (605315) and by competing with CBP (CREBBP;
600140)/p300 (EP300; 602700) in binding to the N terminus of TBET.
Maximal expression of FUT7 and sialyl Lewis x in T cells was obtained by
ROG (ZBTB32; 605859)-mediated suppression of GATA3. Chen et al. (2006)
concluded that the GATA3/TBET transcription factor complex regulates
cell lineage-specific expression of lymphocyte homing receptors and that
glycoconjugates are regulated by this complex to attain cell
lineage-specific expression in Th1 and Th2 lymphocyte subsets.
MAPPING
Natsuka et al. (1994) mapped the FUT7 gene to chromosome 9 by somatic
cell hybrid analysis.
MOLECULAR GENETICS
Bengtson et al. (2001) identified 3 individuals who were heterozygous
for a 326G-A point mutation (arg110 to gln) in the FUT7 gene. Screening
of family members revealed a homozygote for the mutation. Neutrophils
isolated from individuals carrying the mutation showed lowered
expression of SLeX and elevated expression of CD65 compared to controls.
The homozygous individual was found to have ulcer disease,
noninsulin-dependent diabetes, osteoporosis, spondyloarthrosis, and
Sjogren syndrome, but the relationship between disease and the mutation
was not clear. Bengtson et al. (2001) determined that the mutation
causes loss of function. Biochemical analysis of lysates obtained from
COS-7 cells transiently transfected with the mutated FUT7 construct
revealed no FUT7 activity, and immunocytochemical visualization revealed
no SLeX on the surface of these cells.
OTHER FEATURES
Pang et al. (2011) used ultrasensitive mass spectrometric analyses to
demonstrate that the sialyl-Lewis(X) (SLEX) sequence, comprised of
NeuAc-alpha2-3Gal-beta1-4(Fuc-alpha1-3)GlcNAc, a well-known selectin
ligand, is the most abundant terminal sequence on the N- and O-glycans
of human zona pellucida. Sperm-ZP binding was largely inhibited by
glycoconjugates terminated with sialyl-Lewis(X) sequences or by
antibodies directed against this sequence. Thus, Pang et al. (2011)
concluded that the sialyl-Lewis(X) sequence represents the major
carbohydrate ligand for human sperm-egg binding.
*FIELD* RF
1. Bengtson, P.; Larson, C.; Lundblad, A.; Larson, G.; Pahlsson, P.
: Identification of a missense mutation (G329A; arg110-to-gln) in
the human FUT7 gene. J. Biol. Chem. 276: 31575-31582, 2001.
2. Chen, G.-Y.; Osada, H.; Santamaria-Babi, L. F.; Kannagi, R.: Interaction
of GATA-3/T-bet transcription factors regulates expression of sialyl
Lewis X homing receptors on Th1/Th2 lymphocytes. Proc. Nat. Acad.
Sci. 103: 16894-16899, 2006.
3. Mahdavi, J.; Sonden, B.; Hurtig, M.; Olfat, F. O.; Forsberg, L.;
Roche, N.; Angstrom, J.; Larsson, T.; Teneberg, S.; Karlsson, K.-A.;
Altraja, S.; Wadstrom, T.; and 11 others: Helicobacter pylori SabA
adhesin in persistent infection and chronic inflammation. Science 297:
573-578, 2002.
4. Natsuka, S.; Gersten, K. M.; Zenita, K.; Kannagi, R.; Lowe, J.
B.: Molecular cloning of a cDNA encoding a novel human leukocyte
alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis
x determinant. J. Biol. Chem. 269: 16789-16794, 1994. Note: Erratum:
J. Biol. Chem. 269: 20806 only, 1994.
5. Pang, P.-C.; Chiu, P. C. N.; Lee, C.-L.; Chang, L.-Y.; Panico,
M.; Morris, H. R.; Haslam, S. M.; Khoo, K.-H.; Clark, G. F.; Yeung,
W. S. B.; Dell, A.: Human sperm binding is mediated by the sialyl-Lewis(X)
oligosaccharide on the zona pellucida. Science 333: 1761-1764, 2011.
6. Sasaki, K.; Kurata, K.; Funayama, K.; Nagata, M.; Watanabe, E.;
Ohta, S.; Hannai, N.; Nishi, T.: Expression cloning of a novel alpha-1,3-fucosyltransferase
that is involved in biosynthesis of the sialyl Lewis x carbohydrate
determinants in leukocytes. J. Biol. Chem. 269: 14730-14737, 1994.
*FIELD* CN
Ada Hamosh - updated: 11/28/2011
Paul J. Converse - updated: 1/16/2007
Ada Hamosh - updated: 8/7/2002
Patricia A. Hartz - updated: 4/29/2002
*FIELD* CD
Ethylin Wang Jabs: 10/2/1997
*FIELD* ED
carol: 03/13/2013
alopez: 11/28/2011
mgross: 1/16/2007
alopez: 8/8/2002
terry: 8/7/2002
carol: 4/29/2002
mark: 1/19/1998
mark: 1/13/1998
terry: 10/2/1997
*RECORD*
*FIELD* NO
602030
*FIELD* TI
*602030 FUCOSYLTRANSFERASE 7; FUT7
*FIELD* TX
CLONING
The sialyl Lewis x oligosaccharide determinant is an essential component
read moreof leukocyte counterreceptors for E-selectin (131210)- and P-selectin
(173610)-mediated adhesions of leukocytes. This oligosaccharide molecule
is displayed on the surfaces of granulocytes, monocytes, and natural
killer cells. Formation of leukocyte adhesions to these selectins is an
early and important step in the process that ultimately allows
leukocytes to leave the vascular tree and become recruited into lymphoid
tissues and sites of inflammation. Natsuka et al. (1994) and Sasaki et
al. (1994) isolated cDNAs encoding a human leukocyte
alpha-1,3-fucosyltransferase, FUT7, capable of synthesizing the sialyl
Lewis x determinant. The cDNA predicts a 342-amino acid type II
transmembrane protein typical of mammalian glycosyltransferases. By
Northern blot analysis, Natsuka et al. (1994) showed that FUT7 was
expressed in HL-60 cells, a human promyelocytic cell line, and in YT
cells, a natural killer-like cell line. Sequence comparisons indicate
that the predicted polypeptide sequence shares approximately 38 to 47%
overall identity with other FUTs (e.g., FUT3, 111100; FUT6, 136836).
GENE FUNCTION
Natsuka et al. (1994) found when FUT7 was expressed in mammalian cells,
the cDNA directed synthesis of cell surface sialyl Lewis x moieties, but
not Lewis x, Lewis A, sialyl Lewis a, or VIM-2 determinants. Sasaki et
al. (1994) demonstrated in vivo ability of FUT7 to synthesize the sialyl
Lewis x moiety that binds to E-selectin and reported the restricted
expression of FUT7 in leukocytes.
Mahdavi et al. (2002) identified sialyl-dimeric-Lewis x
glycosphingolipid as a receptor for H. pylori and showed that H. pylori
infection induced formation of sialyl-Lewis x antigens in gastric
epithelium in humans and in a Rhesus monkey. The corresponding sialic
acid-binding adhesin was identified as sabA. Mahdavi et al. (2002)
concluded that the ability of many H. pylori strains to adhere to
sialylated glycoconjugates expressed during chronic inflammation might
contribute to virulence and the extraordinary chronicity of H. pylori
infection.
Chen et al. (2006) noted that activated T cells, particularly Th1 cells,
express sialyl Lewis x, but resting T cells do not. Using reporter
analysis, they showed that TBET (TBX21; 604895) promoted and GATA3
(131320) repressed transcription of FUT7. TBET interfered with GATA3
binding to its target DNA, but GATA3 also interfered with TBET binding
to the FUT7 promoter. GATA3 regulated FUT7 transcription by recruiting,
in a phosphorylation-dependent manner, histone deacetylase-3 (HDAC3;
605166) and HDAC5 (605315) and by competing with CBP (CREBBP;
600140)/p300 (EP300; 602700) in binding to the N terminus of TBET.
Maximal expression of FUT7 and sialyl Lewis x in T cells was obtained by
ROG (ZBTB32; 605859)-mediated suppression of GATA3. Chen et al. (2006)
concluded that the GATA3/TBET transcription factor complex regulates
cell lineage-specific expression of lymphocyte homing receptors and that
glycoconjugates are regulated by this complex to attain cell
lineage-specific expression in Th1 and Th2 lymphocyte subsets.
MAPPING
Natsuka et al. (1994) mapped the FUT7 gene to chromosome 9 by somatic
cell hybrid analysis.
MOLECULAR GENETICS
Bengtson et al. (2001) identified 3 individuals who were heterozygous
for a 326G-A point mutation (arg110 to gln) in the FUT7 gene. Screening
of family members revealed a homozygote for the mutation. Neutrophils
isolated from individuals carrying the mutation showed lowered
expression of SLeX and elevated expression of CD65 compared to controls.
The homozygous individual was found to have ulcer disease,
noninsulin-dependent diabetes, osteoporosis, spondyloarthrosis, and
Sjogren syndrome, but the relationship between disease and the mutation
was not clear. Bengtson et al. (2001) determined that the mutation
causes loss of function. Biochemical analysis of lysates obtained from
COS-7 cells transiently transfected with the mutated FUT7 construct
revealed no FUT7 activity, and immunocytochemical visualization revealed
no SLeX on the surface of these cells.
OTHER FEATURES
Pang et al. (2011) used ultrasensitive mass spectrometric analyses to
demonstrate that the sialyl-Lewis(X) (SLEX) sequence, comprised of
NeuAc-alpha2-3Gal-beta1-4(Fuc-alpha1-3)GlcNAc, a well-known selectin
ligand, is the most abundant terminal sequence on the N- and O-glycans
of human zona pellucida. Sperm-ZP binding was largely inhibited by
glycoconjugates terminated with sialyl-Lewis(X) sequences or by
antibodies directed against this sequence. Thus, Pang et al. (2011)
concluded that the sialyl-Lewis(X) sequence represents the major
carbohydrate ligand for human sperm-egg binding.
*FIELD* RF
1. Bengtson, P.; Larson, C.; Lundblad, A.; Larson, G.; Pahlsson, P.
: Identification of a missense mutation (G329A; arg110-to-gln) in
the human FUT7 gene. J. Biol. Chem. 276: 31575-31582, 2001.
2. Chen, G.-Y.; Osada, H.; Santamaria-Babi, L. F.; Kannagi, R.: Interaction
of GATA-3/T-bet transcription factors regulates expression of sialyl
Lewis X homing receptors on Th1/Th2 lymphocytes. Proc. Nat. Acad.
Sci. 103: 16894-16899, 2006.
3. Mahdavi, J.; Sonden, B.; Hurtig, M.; Olfat, F. O.; Forsberg, L.;
Roche, N.; Angstrom, J.; Larsson, T.; Teneberg, S.; Karlsson, K.-A.;
Altraja, S.; Wadstrom, T.; and 11 others: Helicobacter pylori SabA
adhesin in persistent infection and chronic inflammation. Science 297:
573-578, 2002.
4. Natsuka, S.; Gersten, K. M.; Zenita, K.; Kannagi, R.; Lowe, J.
B.: Molecular cloning of a cDNA encoding a novel human leukocyte
alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis
x determinant. J. Biol. Chem. 269: 16789-16794, 1994. Note: Erratum:
J. Biol. Chem. 269: 20806 only, 1994.
5. Pang, P.-C.; Chiu, P. C. N.; Lee, C.-L.; Chang, L.-Y.; Panico,
M.; Morris, H. R.; Haslam, S. M.; Khoo, K.-H.; Clark, G. F.; Yeung,
W. S. B.; Dell, A.: Human sperm binding is mediated by the sialyl-Lewis(X)
oligosaccharide on the zona pellucida. Science 333: 1761-1764, 2011.
6. Sasaki, K.; Kurata, K.; Funayama, K.; Nagata, M.; Watanabe, E.;
Ohta, S.; Hannai, N.; Nishi, T.: Expression cloning of a novel alpha-1,3-fucosyltransferase
that is involved in biosynthesis of the sialyl Lewis x carbohydrate
determinants in leukocytes. J. Biol. Chem. 269: 14730-14737, 1994.
*FIELD* CN
Ada Hamosh - updated: 11/28/2011
Paul J. Converse - updated: 1/16/2007
Ada Hamosh - updated: 8/7/2002
Patricia A. Hartz - updated: 4/29/2002
*FIELD* CD
Ethylin Wang Jabs: 10/2/1997
*FIELD* ED
carol: 03/13/2013
alopez: 11/28/2011
mgross: 1/16/2007
alopez: 8/8/2002
terry: 8/7/2002
carol: 4/29/2002
mark: 1/19/1998
mark: 1/13/1998
terry: 10/2/1997