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P48300

- FUCO_CANFA

UniProt

P48300 - FUCO_CANFA

Protein

Tissue alpha-L-fucosidase

Gene

FUCA1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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
    Sitei296 – 2961May be important for catalysis

    GO - Molecular functioni

    1. alpha-L-fucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fucose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.51. 1154.

    Protein family/group databases

    CAZyiGH29. Glycoside Hydrolase Family 29.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tissue alpha-L-fucosidase (EC:3.2.1.51)
    Alternative name(s):
    Alpha-L-fucosidase I
    Alpha-L-fucoside fucohydrolase 1
    Short name:
    Alpha-L-fucosidase 1
    Gene namesi
    Name:FUCA1
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Defects in FUCA1 are the cause of fucosidosis. It is a lysosomal storage disease characterized by accumulation of fucose-containing glycolipids and glycoproteins in various tissues.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 465439Tissue alpha-L-fucosidasePRO_0000010307Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP48300.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi9615.ENSCAFP00000019256.

    Structurei

    3D structure databases

    ProteinModelPortaliP48300.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 29 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3669.
    HOGENOMiHOG000029598.
    HOVERGENiHBG002155.
    InParanoidiP48300.
    KOiK01206.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR016286. FUC_metazoa-typ.
    IPR028755. FUCA1.
    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:SF2. PTHR10030:SF2. 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.

    P48300-1 [UniParc]FASTAAdd to Basket

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    MKPWAVGLGP PPPAVPLLLL LLLGAALVRA AAPPRRYTPD WQSLDSRPLP    50
    DWFDKAKFGV FVHWGEFAVP AWGSEWFWWH WKGEGLPQYE QFMSENYPPG 100
    FSYADFGPQF TARFFHPDTW ADLFQAAGAR YVVLTTKHHE GFTNWPSSVS 150
    WNWNSNDVGP HRDLVGELGR ALRKRNIRYG LYHSLLEWFH PLYLLDKKNN 200
    FKTQFFVRAK TMPELYDLVN RYEPDLIWSD GEWKCPDTYW NSTEFLSWLY 250
    NDSPVKDHVV VNDRWGQNCS CHHGGYYNCQ DKYKPESLPD LKWEMCTSID 300
    KVSWGYRRNM VMSDVASECE IISELVQTVS LGGNYLLNIG PTKDGLIVPI 350
    FQERLLSIGK WLSINGEAIY ASKPWRVQLE KNTTSVWYTS RGMTVYAIFL 400
    RWPENGVLSL KSPVTTSTTQ ITMLGIQKDL KWSTEPEGLL IYLPQLSLFT 450
    LPVEFGWTIK LTGVE 465
    Length:465
    Mass (Da):53,757
    Last modified:February 1, 1996 - v1
    Checksum:i832BA3C3510341B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 152AV → LPL in AAB17403. (PubMed:8661697)Curated
    Sequence conflicti14 – 152AV → LPL in AAB17401. (PubMed:8661697)Curated
    Sequence conflicti30 – 323AAA → GPP in AAB17403. (PubMed:8661697)Curated
    Sequence conflicti30 – 323AAA → GPP in AAB17401. (PubMed:8661697)Curated
    Sequence conflicti66 – 661E → V in AAB17403. (PubMed:8661697)Curated
    Sequence conflicti66 – 661E → V in AAB17401. (PubMed:8661697)Curated
    Sequence conflicti234 – 2341K → E in AAB17403. (PubMed:8661697)Curated
    Sequence conflicti257 – 2571D → G in CAA63197. (PubMed:8730282)Curated
    Sequence conflicti291 – 2911L → H in AAB17403. (PubMed:8661697)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92671
    , X92672, X92673, X92674, X92675, X92676, X92677, X92678 Genomic DNA. Translation: CAA63362.1.
    X92448 mRNA. Translation: CAA63197.1.
    U29765 mRNA. Translation: AAB17403.1.
    U29766 Genomic DNA. Translation: AAB17401.1.
    RefSeqiNP_001003250.1. NM_001003250.1.
    UniGeneiCfa.3785.

    Genome annotation databases

    GeneIDi403929.
    KEGGicfa:403929.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X92671
    , X92672 , X92673 , X92674 , X92675 , X92676 , X92677 , X92678 Genomic DNA. Translation: CAA63362.1 .
    X92448 mRNA. Translation: CAA63197.1 .
    U29765 mRNA. Translation: AAB17403.1 .
    U29766 Genomic DNA. Translation: AAB17401.1 .
    RefSeqi NP_001003250.1. NM_001003250.1.
    UniGenei Cfa.3785.

    3D structure databases

    ProteinModelPortali P48300.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000019256.

    Protein family/group databases

    CAZyi GH29. Glycoside Hydrolase Family 29.

    Proteomic databases

    PaxDbi P48300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 403929.
    KEGGi cfa:403929.

    Organism-specific databases

    CTDi 2517.

    Phylogenomic databases

    eggNOGi COG3669.
    HOGENOMi HOG000029598.
    HOVERGENi HBG002155.
    InParanoidi P48300.
    KOi K01206.

    Enzyme and pathway databases

    BRENDAi 3.2.1.51. 1154.

    Miscellaneous databases

    NextBioi 20817420.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR016286. FUC_metazoa-typ.
    IPR028755. FUCA1.
    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:SF2. PTHR10030:SF2. 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 [GENOMIC DNA / MRNA], DISEASE.
      Strain: English Springer spaniel.
      Tissue: Blood and Liver.
    2. "Isolation of the canine alpha-L-fucosidase cDNA and definition of the fucosidosis mutation in English Springer Spaniels."
      Occhiodoro T., Anson D.S.
      Mamm. Genome 7:271-274(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DISEASE.
      Strain: English Springer spaniel.

    Entry informationi

    Entry nameiFUCO_CANFA
    AccessioniPrimary (citable) accession number: P48300
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3