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Q11130

- FUT7_HUMAN

UniProt

Q11130 - FUT7_HUMAN

Protein

Alpha-(1,3)-fucosyltransferase 7

Gene

FUT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

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

    GO - Biological processi

    1. CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: Ensembl
    2. fucosylation Source: GOC
    3. leukocyte migration involved in immune response Source: Ensembl
    4. L-fucose catabolic process Source: UniProtKB
    5. protein glycosylation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.65. 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: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:4018. FUT7.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein
    Note: Membrane-bound form in trans cisternae of Golgi.

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: ProtInc
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28434.

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1414CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini37 – 342306LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei15 – 3622Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 10 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG252779.
    HOGENOMiHOG000045583.
    HOVERGENiHBG000274.
    InParanoidiQ11130.
    KOiK07635.
    OMAiGAMDSAN.
    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

    MNNAGHGPTR RLRGLGVLAG VALLAALWLL WLLGSAPRGT PAPQPTITIL    50
    VWHWPFTDQP PELPSDTCTR YGIARCHLSA NRSLLASADA VVFHHRELQT 100
    RRSHLPLAQR PRGQPWVWAS MESPSHTHGL SHLRGIFNWV LSYRRDSDIF 150
    VPYGRLEPHW GPSPPLPAKS RVAAWVVSNF QERQLRARLY RQLAPHLRVD 200
    VFGRANGRPL CASCLVPTVA QYRFYLSFEN SQHRDYITEK FWRNALVAGT 250
    VPVVLGPPRA TYEAFVPADA FVHVDDFGSA RELAAFLTGM NESRYQRFFA 300
    WRDRLRVRLF TDWRERFCAI CDRYPHLPRS QVYEDLEGWF QA 342
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7022.1.
    PIRi A54057.
    RefSeqi NP_004470.1. NM_004479.3.
    UniGenei Hs.457.

    3D structure databases

    ProteinModelPortali Q11130.
    SMRi Q11130. Positions 167-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108805. 1 interaction.
    STRINGi 9606.ENSP00000318142.

    Protein family/group databases

    CAZyi GT10. Glycosyltransferase Family 10.

    PTM databases

    PhosphoSitei Q11130.

    Proteomic databases

    PaxDbi Q11130.
    PRIDEi Q11130.

    Protocols and materials databases

    DNASUi 2529.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314412 ; ENSP00000318142 ; ENSG00000180549 .
    GeneIDi 2529.
    KEGGi hsa:2529.
    UCSCi uc004ckq.2. human.

    Organism-specific databases

    CTDi 2529.
    GeneCardsi GC09M139924.
    HGNCi HGNC:4018. FUT7.
    MIMi 602030. gene.
    neXtProti NX_Q11130.
    PharmGKBi PA28434.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252779.
    HOGENOMi HOG000045583.
    HOVERGENi HBG000274.
    InParanoidi Q11130.
    KOi K07635.
    OMAi GAMDSAN.
    OrthoDBi EOG7Z69C9.
    PhylomeDBi Q11130.
    TreeFami TF316348.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.65. 2681.

    Miscellaneous databases

    GeneWikii FUT7.
    GenomeRNAii 2529.
    NextBioi 9967.
    PROi Q11130.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q11130.
    CleanExi HS_FUT7.
    Genevestigatori Q11130.

    Family and domain databases

    InterProi IPR001503. Glyco_trans_10.
    [Graphical view ]
    PANTHERi PTHR11929. PTHR11929. 1 hit.
    Pfami PF00852. Glyco_transf_10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 129 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