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Protein

Alpha-(1,3)-fucosyltransferase 7

Gene

FUT7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May catalyze alpha-1,3 glycosidic linkages involved in the expression of sialyl Lewis X antigens.

Catalytic activityi

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.

Pathwayi

GO - Molecular functioni

  • alpha-(1->3)-fucosyltransferase activity Source: UniProtKB
  • fucosyltransferase activity Source: ProtInc

GO - Biological processi

  • CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: Ensembl
  • fucosylation Source: GOC
  • leukocyte migration involved in immune response Source: Ensembl
  • L-fucose catabolic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.214. 2681.
2.4.1.65. 2681.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT10. Glycosyltransferase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-(1,3)-fucosyltransferase 7 (EC:2.4.1.-)
Alternative name(s):
Fucosyltransferase 7
Fucosyltransferase VII
Short name:
Fuc-TVII
Short name:
FucT-VII
Galactoside 3-L-fucosyltransferase
Selectin ligand synthase
Gene namesi
Name:FUT7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:4018. FUT7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei15 – 3622Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini37 – 342306LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: ProtInc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28434.

Polymorphism and mutation databases

BioMutaiFUT7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Alpha-(1,3)-fucosyltransferase 7PRO_0000221113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 761 Publication
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi211 ↔ 2141 Publication
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi318 ↔ 3211 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ11130.
PRIDEiQ11130.

PTM databases

PhosphoSiteiQ11130.

Expressioni

Tissue specificityi

Leukocytic/myeloid lineage cells.

Gene expression databases

BgeeiQ11130.
CleanExiHS_FUT7.
GenevestigatoriQ11130.

Interactioni

Protein-protein interaction databases

BioGridi108805. 1 interaction.
STRINGi9606.ENSP00000318142.

Structurei

3D structure databases

ProteinModelPortaliQ11130.
SMRiQ11130. Positions 167-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 10 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG252779.
GeneTreeiENSGT00680000099679.
HOGENOMiHOG000045583.
HOVERGENiHBG000274.
InParanoidiQ11130.
KOiK07635.
OMAiRGIFNWV.
OrthoDBiEOG7Z69C9.
PhylomeDBiQ11130.
TreeFamiTF316348.

Family and domain databases

InterProiIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERiPTHR11929. PTHR11929. 1 hit.
PfamiPF00852. Glyco_transf_10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q11130-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNAGHGPTR RLRGLGVLAG VALLAALWLL WLLGSAPRGT PAPQPTITIL
60 70 80 90 100
VWHWPFTDQP PELPSDTCTR YGIARCHLSA NRSLLASADA VVFHHRELQT
110 120 130 140 150
RRSHLPLAQR PRGQPWVWAS MESPSHTHGL SHLRGIFNWV LSYRRDSDIF
160 170 180 190 200
VPYGRLEPHW GPSPPLPAKS RVAAWVVSNF QERQLRARLY RQLAPHLRVD
210 220 230 240 250
VFGRANGRPL CASCLVPTVA QYRFYLSFEN SQHRDYITEK FWRNALVAGT
260 270 280 290 300
VPVVLGPPRA TYEAFVPADA FVHVDDFGSA RELAAFLTGM NESRYQRFFA
310 320 330 340
WRDRLRVRLF TDWRERFCAI CDRYPHLPRS QVYEDLEGWF QA
Length:342
Mass (Da):39,239
Last modified:October 1, 1996 - v1
Checksum:iD31BFF90DD64DFAB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1622GP → A in AAA56869 (PubMed:8207002).Curated
Sequence conflicti304 – 3052RL → SV in AAA56869 (PubMed:8207002).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78031 mRNA. Translation: CAA54962.1.
U11282 mRNA. Translation: AAA20468.1.
U08112 mRNA. Translation: AAA56869.1.
AB012668 Genomic DNA. Translation: BAA32819.1.
AK313124 mRNA. Translation: BAG35944.1.
AL807752 Genomic DNA. Translation: CAI12771.1.
BC074746 mRNA. Translation: AAH74746.2.
BC086312 mRNA. Translation: AAH86312.1.
CCDSiCCDS7022.1.
PIRiA54057.
RefSeqiNP_004470.1. NM_004479.3.
UniGeneiHs.457.

Genome annotation databases

EnsembliENST00000314412; ENSP00000318142; ENSG00000180549.
GeneIDi2529.
KEGGihsa:2529.
UCSCiuc004ckq.2. human.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Fucosyltransferase 7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78031 mRNA. Translation: CAA54962.1.
U11282 mRNA. Translation: AAA20468.1.
U08112 mRNA. Translation: AAA56869.1.
AB012668 Genomic DNA. Translation: BAA32819.1.
AK313124 mRNA. Translation: BAG35944.1.
AL807752 Genomic DNA. Translation: CAI12771.1.
BC074746 mRNA. Translation: AAH74746.2.
BC086312 mRNA. Translation: AAH86312.1.
CCDSiCCDS7022.1.
PIRiA54057.
RefSeqiNP_004470.1. NM_004479.3.
UniGeneiHs.457.

3D structure databases

ProteinModelPortaliQ11130.
SMRiQ11130. Positions 167-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108805. 1 interaction.
STRINGi9606.ENSP00000318142.

Protein family/group databases

CAZyiGT10. Glycosyltransferase Family 10.

PTM databases

PhosphoSiteiQ11130.

Polymorphism and mutation databases

BioMutaiFUT7.

Proteomic databases

PaxDbiQ11130.
PRIDEiQ11130.

Protocols and materials databases

DNASUi2529.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314412; ENSP00000318142; ENSG00000180549.
GeneIDi2529.
KEGGihsa:2529.
UCSCiuc004ckq.2. human.

Organism-specific databases

CTDi2529.
GeneCardsiGC09M139924.
HGNCiHGNC:4018. FUT7.
MIMi602030. gene.
neXtProtiNX_Q11130.
PharmGKBiPA28434.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252779.
GeneTreeiENSGT00680000099679.
HOGENOMiHOG000045583.
HOVERGENiHBG000274.
InParanoidiQ11130.
KOiK07635.
OMAiRGIFNWV.
OrthoDBiEOG7Z69C9.
PhylomeDBiQ11130.
TreeFamiTF316348.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.214. 2681.
2.4.1.65. 2681.

Miscellaneous databases

GeneWikiiFUT7.
GenomeRNAii2529.
NextBioi9967.
PROiQ11130.
SOURCEiSearch...

Gene expression databases

BgeeiQ11130.
CleanExiHS_FUT7.
GenevestigatoriQ11130.

Family and domain databases

InterProiIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERiPTHR11929. PTHR11929. 1 hit.
PfamiPF00852. Glyco_transf_10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant."
    Natsuka S., Gersten K.M., Zenita K., Kannagi R., Lowe J.B.
    J. Biol. Chem. 269:16789-16794(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning of a cDNA encoding a novel human leukocyte alpha-1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant."
    Natsuka S., Gersten K.M., Zenita K., Kannagi R., Lowe J.B.
    J. Biol. Chem. 269:20806-20806(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Expression cloning of a novel alpha 1,3-fucosyltransferase that is involved in biosynthesis of the sialyl Lewis x carbohydrate determinants in leukocytes."
    Sasaki K., Kurata K., Funayama K., Nagata M., Watanabe E., Ohta S., Hanai N., Nishi T.
    J. Biol. Chem. 269:14730-14737(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The human selectin-ligand synthase (hFuc-T VII) gene structure and characterization of the promoter."
    Hiraiwa N., Hiraiwa M., Kannagi R.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  6. "DNA sequence and analysis of human chromosome 9."
    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.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Mammary gland.
  8. "Neighboring cysteine residues in human fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures."
    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.
    Glycobiology 11:423-432(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.

Entry informationi

Entry nameiFUT7_HUMAN
AccessioniPrimary (citable) accession number: Q11130
Secondary accession number(s): B2R7U7, Q6DK54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.