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Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) (Selectin ligand synthase)

 FUT7_HUMAN              Reviewed;         342 AA.
Q11130; B2R7U7; Q6DK54;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 157.
RecName: Full=Alpha-(1,3)-fucosyltransferase 7;
EC=2.4.1.- {ECO:0000269|PubMed:11404359, ECO:0000269|PubMed:8207002};
AltName: Full=Fucosyltransferase 7;
AltName: Full=Fucosyltransferase VII {ECO:0000303|PubMed:8207002};
Short=Fuc-TVII {ECO:0000303|PubMed:8207002};
Short=FucT-VII;
AltName: Full=Galactoside 3-L-fucosyltransferase;
AltName: Full=Selectin ligand synthase;
Name=FUT7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=8207002;
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).
[2]
SEQUENCE REVISION.
PubMed=8051184;
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. 269:20806-20806(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8182079;
Sasaki K., Kurata K., Funayama K., Nagata M., Watanabe E., Ohta S.,
Hanai 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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hiraiwa N., Hiraiwa M., Kannagi R.;
"The human selectin-ligand synthase (hFuc-T VII) gene structure and
characterization of the promoter.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=9299472; DOI=10.1006/bbrc.1997.7254;
Stroud M.R., Holmes E.H.;
"Fucosylation of complex glycosphingolipids by recombinant
fucosyltransferase-VII.";
Biochem. Biophys. Res. Commun. 238:165-168(1997).
[9]
DISULFIDE BONDS.
PubMed=11425803; DOI=10.1093/glycob/11.5.423;
de Vries T., Yen T.Y., Joshi R.K., Storm J., van Den Eijnden D.H.,
Knegtel R.M.A., Bunschoten H., Joziasse D.H., Macher B.A.;
"Neighboring cysteine residues in human fucosyltransferase VII are
engaged in disulfide bridges, forming small loop structures.";
Glycobiology 11:423-432(2001).
[10]
VARIANT GLN-110, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT
GLN-110, BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
PubMed=11404359; DOI=10.1074/jbc.M104165200;
Bengtson P., Larson C., Lundblad A., Larson G., Paahlsson P.;
"Identification of a missense mutation (G329A;Arg(110)--> GLN) in the
human FUT7 gene.";
J. Biol. Chem. 276:31575-31582(2001).
-!- FUNCTION: Catalyzes alpha-1,3 glycosidic linkages involved in the
expression of sialyl Lewis X antigens.
{ECO:0000269|PubMed:11404359, ECO:0000269|PubMed:8207002,
ECO:0000269|PubMed:9299472}.
-!- CATALYTIC ACTIVITY: GDP-L-fucose + alpha-2,3-Neu-N-acetyl-1,4-
beta-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + alpha-2,3-Neu-
N-acetyl-1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D-
glucosaminyl-R. {ECO:0000269|PubMed:11404359,
ECO:0000269|PubMed:8207002, ECO:0000269|PubMed:9299472}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5 uM for GDP-fucose {ECO:0000269|PubMed:11404359};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
Single-pass type II membrane protein. Note=Membrane-bound form in
trans cisternae of Golgi.
-!- TISSUE SPECIFICITY: Leukocytic/myeloid lineage cells.
-!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Fucosyltransferase 7;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_604";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X78031; CAA54962.1; -; mRNA.
EMBL; U11282; AAA20468.1; -; mRNA.
EMBL; U08112; AAA56869.1; -; mRNA.
EMBL; AB012668; BAA32819.1; -; Genomic_DNA.
EMBL; AK313124; BAG35944.1; -; mRNA.
EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC074746; AAH74746.2; -; mRNA.
EMBL; BC086312; AAH86312.1; -; mRNA.
CCDS; CCDS7022.1; -.
PIR; A54057; A54057.
RefSeq; NP_004470.1; NM_004479.3.
UniGene; Hs.457; -.
ProteinModelPortal; Q11130; -.
BioGrid; 108805; 3.
IntAct; Q11130; 2.
STRING; 9606.ENSP00000318142; -.
BindingDB; Q11130; -.
ChEMBL; CHEMBL3596077; -.
SwissLipids; SLP:000001438; -.
CAZy; GT10; Glycosyltransferase Family 10.
iPTMnet; Q11130; -.
PhosphoSitePlus; Q11130; -.
BioMuta; FUT7; -.
PaxDb; Q11130; -.
PeptideAtlas; Q11130; -.
PRIDE; Q11130; -.
ProteomicsDB; 58872; -.
DNASU; 2529; -.
Ensembl; ENST00000314412; ENSP00000318142; ENSG00000180549.
GeneID; 2529; -.
KEGG; hsa:2529; -.
UCSC; uc004ckq.3; human.
CTD; 2529; -.
DisGeNET; 2529; -.
EuPathDB; HostDB:ENSG00000180549.7; -.
GeneCards; FUT7; -.
HGNC; HGNC:4018; FUT7.
HPA; HPA042780; -.
MIM; 602030; gene.
neXtProt; NX_Q11130; -.
OpenTargets; ENSG00000180549; -.
PharmGKB; PA28434; -.
eggNOG; KOG2619; Eukaryota.
eggNOG; ENOG410ZIMX; LUCA.
GeneTree; ENSGT00680000099679; -.
HOGENOM; HOG000045583; -.
HOVERGEN; HBG000274; -.
InParanoid; Q11130; -.
KO; K07635; -.
OMA; HTHGLSH; -.
OrthoDB; EOG091G0846; -.
PhylomeDB; Q11130; -.
TreeFam; TF316348; -.
BioCyc; MetaCyc:HS11506-MONOMER; -.
BRENDA; 2.4.1.214; 2681.
BRENDA; 2.4.1.65; 2681.
SABIO-RK; Q11130; -.
UniPathway; UPA00378; -.
GeneWiki; FUT7; -.
GenomeRNAi; 2529; -.
PRO; PR:Q11130; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000180549; -.
CleanEx; HS_FUT7; -.
Genevisible; Q11130; HS.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:UniProtKB.
GO; GO:0008417; F:fucosyltransferase activity; IDA:UniProtKB.
GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0006672; P:ceramide metabolic process; IDA:BHF-UCL.
GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
GO; GO:0002522; P:leukocyte migration involved in immune response; IEA:Ensembl.
GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
Gene3D; 3.40.50.11660; -; 1.
InterPro; IPR031481; Glyco_tran_10_N.
InterPro; IPR001503; Glyco_trans_10.
InterPro; IPR038577; GT10-like_sf.
PANTHER; PTHR11929; PTHR11929; 1.
Pfam; PF17039; Glyco_tran_10_N; 1.
Pfam; PF00852; Glyco_transf_10; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Membrane; Polymorphism; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 342 Alpha-(1,3)-fucosyltransferase 7.
/FTId=PRO_0000221113.
TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.
TRANSMEM 15 36 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 37 342 Lumenal. {ECO:0000255}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 68 76 {ECO:0000269|PubMed:11425803}.
DISULFID 211 214 {ECO:0000269|PubMed:11425803}.
DISULFID 318 321 {ECO:0000269|PubMed:11425803}.
VARIANT 110 110 R -> Q (found in patients with ulcerative
colitis; loss of alpha-(1,3)-
fucosyltransferase activity;
dbSNP:rs545570871).
{ECO:0000269|PubMed:11404359}.
/FTId=VAR_079131.
CONFLICT 161 162 GP -> A (in Ref. 1; AAA56869).
{ECO:0000305}.
CONFLICT 304 305 RL -> SV (in Ref. 1; AAA56869).
{ECO:0000305}.
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


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