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Q9BTY2

- FUCO2_HUMAN

UniProt

Q9BTY2 - FUCO2_HUMAN

Protein

Plasma alpha-L-fucosidase

Gene

FUCA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.

    Catalytic activityi

    An alpha-L-fucoside + H2O = L-fucose + an alcohol.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei294 – 2941May be important for catalysisPROSITE-ProRule annotation

    GO - Molecular functioni

    1. alpha-L-fucosidase activity Source: UniProt
    2. fucose binding Source: RefGenome

    GO - Biological processi

    1. fucose metabolic process Source: UniProt
    2. glycoside catabolic process Source: UniProt
    3. regulation of entry of bacterium into host cell Source: UniProt
    4. response to bacterium Source: UniProt

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.51. 2681.

    Protein family/group databases

    CAZyiGH29. Glycoside Hydrolase Family 29.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plasma alpha-L-fucosidase (EC:3.2.1.51)
    Alternative name(s):
    Alpha-L-fucoside fucohydrolase 2
    Short name:
    Alpha-L-fucosidase 2
    Gene namesi
    Name:FUCA2
    ORF Names:PSEC0151, UNQ227/PRO260
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4008. FUCA2.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. lysosome Source: RefGenome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    MIMi136820. gene+phenotype.
    PharmGKBiPA28424.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 467439Plasma alpha-L-fucosidasePRO_0000010312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...)1 Publication
    Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9BTY2.
    PaxDbiQ9BTY2.
    PRIDEiQ9BTY2.

    PTM databases

    PhosphoSiteiQ9BTY2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BTY2.
    BgeeiQ9BTY2.
    CleanExiHS_FUCA2.
    GenevestigatoriQ9BTY2.

    Organism-specific databases

    HPAiHPA031659.
    HPA031660.
    HPA031661.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi108795. 3 interactions.
    IntActiQ9BTY2. 1 interaction.
    MINTiMINT-7034547.
    STRINGi9606.ENSP00000002165.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BTY2.
    SMRiQ9BTY2. Positions 33-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 29 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3669.
    HOGENOMiHOG000029598.
    HOVERGENiHBG002155.
    InParanoidiQ9BTY2.
    KOiK01206.
    OMAiVGSICKH.
    OrthoDBiEOG7SFHZ9.
    PhylomeDBiQ9BTY2.
    TreeFamiTF313034.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR016286. FUC_metazoa-typ.
    IPR028756. FUCA2.
    IPR013780. Glyco_hydro_13_b.
    IPR000933. Glyco_hydro_29.
    IPR018526. Glyco_hydro_29_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10030. PTHR10030. 1 hit.
    PTHR10030:SF24. PTHR10030:SF24. 1 hit.
    PfamiPF01120. Alpha_L_fucos. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001092. Alpha-L-fucosidase. 1 hit.
    PRINTSiPR00741. GLHYDRLASE29.
    SMARTiSM00812. Alpha_L_fucos. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00385. ALPHA_L_FUCOSIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9BTY2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPQELPRLA FPLLLLLLLL LPPPPCPAHS ATRFDPTWES LDARQLPAWF    50
    DQAKFGIFIH WGVFSVPSFG SEWFWWYWQK EKIPKYVEFM KDNYPPSFKY 100
    EDFGPLFTAK FFNANQWADI FQASGAKYIV LTSKHHEGFT LWGSEYSWNW 150
    NAIDEGPKRD IVKELEVAIR NRTDLRFGLY YSLFEWFHPL FLEDESSSFH 200
    KRQFPVSKTL PELYELVNNY QPEVLWSDGD GGAPDQYWNS TGFLAWLYNE 250
    SPVRGTVVTN DRWGAGSICK HGGFYTCSDR YNPGHLLPHK WENCMTIDKL 300
    SWGYRREAGI SDYLTIEELV KQLVETVSCG GNLLMNIGPT LDGTISVVFE 350
    ERLRQMGSWL KVNGEAIYET HTWRSQNDTV TPDVWYTSKP KEKLVYAIFL 400
    KWPTSGQLFL GHPKAILGAT EVKLLGHGQP LNWISLEQNG IMVELPQLTI 450
    HQMPCKWGWA LALTNVI 467
    Length:467
    Mass (Da):54,067
    Last modified:July 28, 2009 - v2
    Checksum:iA42AA6B369A3AC39
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti400 – 4001L → P in BAC11633. (PubMed:16303743)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti233 – 2331A → E.
    Corresponds to variant rs11155297 [ dbSNP | Ensembl ].
    VAR_055822
    Natural varianti356 – 3561M → V.3 Publications
    Corresponds to variant rs3762002 [ dbSNP | Ensembl ].
    VAR_022444
    Natural varianti371 – 3711H → Y.3 Publications
    Corresponds to variant rs3762001 [ dbSNP | Ensembl ].
    VAR_022445

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358551 mRNA. Translation: AAQ88915.1.
    AK075458 mRNA. Translation: BAC11633.1.
    AL031320 Genomic DNA. Translation: CAB53746.1.
    BC003060 mRNA. Translation: AAH03060.1.
    BC051268 mRNA. Translation: AAH51268.1.
    CCDSiCCDS5200.1.
    RefSeqiNP_114409.2. NM_032020.4.
    UniGeneiHs.17680.

    Genome annotation databases

    EnsembliENST00000002165; ENSP00000002165; ENSG00000001036.
    GeneIDi2519.
    KEGGihsa:2519.
    UCSCiuc003qjm.3. human.

    Polymorphism databases

    DMDMi254763296.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358551 mRNA. Translation: AAQ88915.1 .
    AK075458 mRNA. Translation: BAC11633.1 .
    AL031320 Genomic DNA. Translation: CAB53746.1 .
    BC003060 mRNA. Translation: AAH03060.1 .
    BC051268 mRNA. Translation: AAH51268.1 .
    CCDSi CCDS5200.1.
    RefSeqi NP_114409.2. NM_032020.4.
    UniGenei Hs.17680.

    3D structure databases

    ProteinModelPortali Q9BTY2.
    SMRi Q9BTY2. Positions 33-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108795. 3 interactions.
    IntActi Q9BTY2. 1 interaction.
    MINTi MINT-7034547.
    STRINGi 9606.ENSP00000002165.

    Chemistry

    BindingDBi Q9BTY2.
    ChEMBLi CHEMBL2271.

    Protein family/group databases

    CAZyi GH29. Glycoside Hydrolase Family 29.

    PTM databases

    PhosphoSitei Q9BTY2.

    Polymorphism databases

    DMDMi 254763296.

    Proteomic databases

    MaxQBi Q9BTY2.
    PaxDbi Q9BTY2.
    PRIDEi Q9BTY2.

    Protocols and materials databases

    DNASUi 2519.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000002165 ; ENSP00000002165 ; ENSG00000001036 .
    GeneIDi 2519.
    KEGGi hsa:2519.
    UCSCi uc003qjm.3. human.

    Organism-specific databases

    CTDi 2519.
    GeneCardsi GC06M143857.
    H-InvDB HIX0006268.
    HGNCi HGNC:4008. FUCA2.
    HPAi HPA031659.
    HPA031660.
    HPA031661.
    MIMi 136820. gene+phenotype.
    neXtProti NX_Q9BTY2.
    PharmGKBi PA28424.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3669.
    HOGENOMi HOG000029598.
    HOVERGENi HBG002155.
    InParanoidi Q9BTY2.
    KOi K01206.
    OMAi VGSICKH.
    OrthoDBi EOG7SFHZ9.
    PhylomeDBi Q9BTY2.
    TreeFami TF313034.

    Enzyme and pathway databases

    BRENDAi 3.2.1.51. 2681.

    Miscellaneous databases

    GeneWikii FUCA2.
    GenomeRNAii 2519.
    NextBioi 9919.
    PROi Q9BTY2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BTY2.
    Bgeei Q9BTY2.
    CleanExi HS_FUCA2.
    Genevestigatori Q9BTY2.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR016286. FUC_metazoa-typ.
    IPR028756. FUCA2.
    IPR013780. Glyco_hydro_13_b.
    IPR000933. Glyco_hydro_29.
    IPR018526. Glyco_hydro_29_CS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10030. PTHR10030. 1 hit.
    PTHR10030:SF24. PTHR10030:SF24. 1 hit.
    Pfami PF01120. Alpha_L_fucos. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001092. Alpha-L-fucosidase. 1 hit.
    PRINTSi PR00741. GLHYDRLASE29.
    SMARTi SM00812. Alpha_L_fucos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00385. ALPHA_L_FUCOSIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-356 AND TYR-371.
    2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-356 AND TYR-371.
      Tissue: Placenta.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANTS VAL-356 AND TYR-371.
      Tissue: B-cell and Placenta.
    5. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-239.
      Tissue: Liver.

    Entry informationi

    Entry nameiFUCO2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BTY2
    Secondary accession number(s): Q7Z6Y2, Q8NBK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 104 of the entry and version 2 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3