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Alpha-(1,3)-fucosyltransferase 6 (EC 2.4.1.65) (Fucosyltransferase 6) (Fucosyltransferase VI) (Fuc-TVI) (FucT-VI) (Galactoside 3-L-fucosyltransferase)

 FUT6_HUMAN              Reviewed;         359 AA.
P51993; A6NEX0; D6W637; Q9UND8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
28-MAR-2018, entry version 158.
RecName: Full=Alpha-(1,3)-fucosyltransferase 6;
EC=2.4.1.65;
AltName: Full=Fucosyltransferase 6;
AltName: Full=Fucosyltransferase VI;
Short=Fuc-TVI;
Short=FucT-VI;
AltName: Full=Galactoside 3-L-fucosyltransferase;
Name=FUT6; Synonyms=FCT3A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1520296; DOI=10.1016/S0006-291X(05)81472-X;
Koszdin K.L., Bowen B.R.;
"The cloning and expression of a human alpha-1,3 fucosyltransferase
capable of forming the E-selectin ligand.";
Biochem. Biophys. Res. Commun. 187:152-157(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1339443;
Weston B.W., Smith P.L., Kelly R.J., Lowe J.B.;
"Molecular cloning of a fourth member of a human alpha
(1,3)fucosyltransferase gene family. Multiple homologous sequences
that determine expression of the Lewis x, sialyl Lewis x, and
difucosyl sialyl Lewis x epitopes.";
J. Biol. Chem. 267:24575-24584(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney;
PubMed=7650030; DOI=10.1074/jbc.270.34.20112;
Cameron H.S., Szczepaniak D., Weston B.W.;
"Expression of human chromosome 19p alpha(1,3)-fucosyltransferase
genes in normal tissues. Alternative splicing, polyadenylation, and
isoforms.";
J. Biol. Chem. 270:20112-20122(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-124.
TISSUE=Squamous cell carcinoma;
Rahim I., Schmidt L.R., Wahl D., Drayson E., Maslanik W.,
Stranahan P.L., Pettijohn D.E.;
"Isolation and expression of human alpha-(1,3)-fucosyltransferase.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
POLYMORPHISM, VARIANT LYS-247, AND CHARACTERIZATION OF VARIANT
LYS-247.
PubMed=8175676;
Mollicone R., Reguigne I., Fletcher A., Aziz A., Rustam M.,
Weston B.W., Kelly R.J., Lowe J.B., Oriol R.;
"Molecular basis for plasma alpha(1,3)-fucosyltransferase gene
deficiency (FUT6).";
J. Biol. Chem. 269:12662-12671(1994).
[8]
VARIANTS SER-124; VAL-244; LYS-247 AND GLY-303, AND CHARACTERIZATION
OF VARIANTS SER-124; VAL-244; LYS-247 AND GLY-303.
PubMed=11102976;
DOI=10.1002/1098-1004(200012)16:6<473::AID-HUMU4>3.0.CO;2-T;
Elmgren A., Borjeson C., Mollicone R., Oriol R., Fletcher A.,
Larson G.;
"Identification of two functionally deficient plasma alpha 3-
fucosyltransferase (FUT6) alleles.";
Hum. Mutat. 16:473-481(2000).
[9]
VARIANTS SER-124; LYS-247 AND GLY-303.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Enzyme involved in the biosynthesis of the E-Selectin
ligand, sialyl-Lewis X. Catalyzes the transfer of fucose from GDP-
beta-fucose to alpha-2,3 sialylated substrates.
-!- CATALYTIC ACTIVITY: GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-
N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->3)-(alpha-
L-fucosyl-(1->4))-N-acetyl-beta-D-glucosaminyl-R.
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P51993-1; Sequence=Displayed;
Name=2;
IsoId=P51993-2; Sequence=VSP_001780;
-!- TISSUE SPECIFICITY: Kidney, liver, colon, small intestine,
bladder, uterus and salivary gland.
-!- POLYMORPHISM: Expression of alpha(1,3)-fucosyltransferase in
plasma can vary among different populations. 9% of individuals on
the isle of Java (Indonesia) do not express this enzyme. Ninety-
five percent of plasma alpha(1,3)-fucosyltransferase-deficient
individuals have Lewis negative phenotype on red cells, suggesting
strong linkage disequilibrium between these two traits. Variations
in FUT6 are responsible for plasma alpha(1,3)-fucosyltransferase
deficiency [MIM:613852].
-!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC50191.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Fucosyltransferase 6;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_603";
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EMBL; M98825; AAA99222.1; -; mRNA.
EMBL; L01698; AAB03078.1; -; Genomic_DNA.
EMBL; U27331; AAC50190.1; -; mRNA.
EMBL; U27332; AAC50191.1; ALT_SEQ; mRNA.
EMBL; U27333; AAC50192.1; -; mRNA.
EMBL; U27334; AAC50193.1; -; mRNA.
EMBL; U27335; AAC50194.1; -; mRNA.
EMBL; U27336; AAC50195.1; -; mRNA.
EMBL; U27337; AAC50196.1; -; mRNA.
EMBL; AF131211; AAD33509.1; -; mRNA.
EMBL; AL031258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471139; EAW69136.1; -; Genomic_DNA.
EMBL; CH471139; EAW69137.1; -; Genomic_DNA.
EMBL; CH471139; EAW69138.1; -; Genomic_DNA.
EMBL; CH471139; EAW69139.1; -; Genomic_DNA.
CCDS; CCDS12152.1; -. [P51993-1]
PIR; A45156; A45156.
PIR; I39048; I39048.
PIR; I39049; I39049.
RefSeq; NP_000141.1; NM_000150.2. [P51993-1]
RefSeq; NP_001035791.1; NM_001040701.1. [P51993-1]
RefSeq; XP_005259583.1; XM_005259526.4. [P51993-1]
RefSeq; XP_011526170.1; XM_011527868.2. [P51993-1]
RefSeq; XP_011526171.1; XM_011527869.2. [P51993-1]
RefSeq; XP_011526172.1; XM_011527870.2. [P51993-1]
RefSeq; XP_011526174.1; XM_011527872.2. [P51993-1]
RefSeq; XP_011526175.1; XM_011527873.2. [P51993-1]
RefSeq; XP_011526176.1; XM_011527874.2. [P51993-1]
RefSeq; XP_011526177.1; XM_011527875.2. [P51993-1]
RefSeq; XP_011526178.1; XM_011527876.2. [P51993-1]
RefSeq; XP_011526180.1; XM_011527878.2. [P51993-1]
RefSeq; XP_011526181.1; XM_011527879.2. [P51993-1]
UniGene; Hs.631846; -.
UniGene; Hs.705615; -.
ProteinModelPortal; P51993; -.
STRING; 9606.ENSP00000286955; -.
BindingDB; P51993; -.
ChEMBL; CHEMBL4443; -.
SwissLipids; SLP:000001436; -. [P51993-1]
CAZy; GT10; Glycosyltransferase Family 10.
iPTMnet; P51993; -.
PhosphoSitePlus; P51993; -.
BioMuta; FUT6; -.
DMDM; 1730136; -.
MaxQB; P51993; -.
PaxDb; P51993; -.
PeptideAtlas; P51993; -.
PRIDE; P51993; -.
DNASU; 2528; -.
Ensembl; ENST00000286955; ENSP00000286955; ENSG00000156413. [P51993-1]
Ensembl; ENST00000318336; ENSP00000313398; ENSG00000156413. [P51993-1]
Ensembl; ENST00000524754; ENSP00000431708; ENSG00000156413. [P51993-1]
Ensembl; ENST00000527106; ENSP00000432954; ENSG00000156413. [P51993-1]
Ensembl; ENST00000592563; ENSP00000466016; ENSG00000156413. [P51993-2]
GeneID; 2528; -.
KEGG; hsa:2528; -.
UCSC; uc002mdf.2; human. [P51993-1]
CTD; 2528; -.
DisGeNET; 2528; -.
EuPathDB; HostDB:ENSG00000156413.13; -.
GeneCards; FUT6; -.
HGNC; HGNC:4017; FUT6.
HPA; HPA043707; -.
HPA; HPA046966; -.
MalaCards; FUT6; -.
MIM; 136836; gene.
MIM; 613852; phenotype.
neXtProt; NX_P51993; -.
OpenTargets; ENSG00000156413; -.
PharmGKB; PA28433; -.
eggNOG; KOG2619; Eukaryota.
eggNOG; ENOG410ZIMX; LUCA.
GeneTree; ENSGT00680000099679; -.
HOGENOM; HOG000045583; -.
HOVERGEN; HBG000274; -.
InParanoid; P51993; -.
KO; K07634; -.
OMA; NITADRK; -.
OrthoDB; EOG091G0846; -.
PhylomeDB; P51993; -.
TreeFam; TF316348; -.
BioCyc; MetaCyc:HS08124-MONOMER; -.
BRENDA; 2.4.1.152; 2681.
BRENDA; 2.4.1.65; 2681.
UniPathway; UPA00378; -.
ChiTaRS; FUT6; human.
GeneWiki; FUT6; -.
GenomeRNAi; 2528; -.
PRO; PR:P51993; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000156413; -.
CleanEx; HS_FUT6; -.
ExpressionAtlas; P51993; baseline and differential.
Genevisible; P51993; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; IEA:UniProtKB-KW.
GO; GO:0017060; F:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; TAS:UniProtKB.
GO; GO:0008417; F:fucosyltransferase activity; IDA:BHF-UCL.
GO; GO:0006672; P:ceramide metabolic process; IDA:BHF-UCL.
GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
GO; GO:0006486; P:protein glycosylation; TAS: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;
Alternative splicing; Complete proteome; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Membrane; Polymorphism;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 359 Alpha-(1,3)-fucosyltransferase 6.
/FTId=PRO_0000221110.
TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.
TRANSMEM 15 34 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 35 359 Lumenal. {ECO:0000255}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 348 359 RYQTRGIAAWFT -> SGGLIYLRTRLPEASPA (in
isoform 2). {ECO:0000303|PubMed:7650030}.
/FTId=VSP_001780.
VARIANT 124 124 P -> S (polymorphism; found in
individuals with plasma alpha(1,3)-
fucosyltransferase deficiency and no
clinically relevant phenotype; results in
partial enzyme inactivation; complete
enzyme inactivation when associated with
V-244 and G-303; dbSNP:rs778805).
{ECO:0000269|PubMed:11102976,
ECO:0000269|PubMed:27535533,
ECO:0000269|Ref.4}.
/FTId=VAR_024463.
VARIANT 230 230 Q -> K (in dbSNP:rs364637).
/FTId=VAR_024464.
VARIANT 244 244 L -> V (found in individuals with plasma
alpha(1,3)-fucosyltransferase deficiency
and no clinically relevant phenotype;
complete enzyme inactivation when
associated with S-124 and G-303).
{ECO:0000269|PubMed:11102976}.
/FTId=VAR_065915.
VARIANT 247 247 E -> K (polymorphism; found in
individuals with plasma alpha(1,3)-
fucosyltransferase deficiency and no
clinically relevant phenotype; complete
enzyme inactivation; dbSNP:rs17855739).
{ECO:0000269|PubMed:11102976,
ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:8175676}.
/FTId=VAR_065916.
VARIANT 303 303 R -> G (polymorphism; found in
individuals with plasma alpha(1,3)-
fucosyltransferase deficiency and no
clinically relevant phenotype; complete
enzyme inactivation when associated with
S-124 and V-244; dbSNP:rs61147939).
{ECO:0000269|PubMed:11102976,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_065917.
SEQUENCE 359 AA; 41860 MW; 67ABDF058F0999DA CRC64;
MDPLGPAKPQ WSWRCCLTTL LFQLLMAVCF FSYLRVSQDD PTVYPNGSRF PDSTGTPAHS
IPLILLWTWP FNKPIALPRC SEMVPGTADC NITADRKVYP QADAVIVHHR EVMYNPSAQL
PRSPRRQGQR WIWFSMESPS HCWQLKAMDG YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH
PPLNLSAKTE LVAWAVSNWG PNSARVRYYQ SLQAHLKVDV YGRSHKPLPQ GTMMETLSRY
KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD
LARYLQELDK DHARYLSYFR WRETLRPRSF SWALAFCKAC WKLQEESRYQ TRGIAAWFT


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