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Q99LJ1

- FUCO_MOUSE

UniProt

Q99LJ1 - FUCO_MOUSE

Protein

Tissue alpha-L-fucosidase

Gene

Fuca1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei282 – 2821May be important for catalysisPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. fucose metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi3.2.1.51. 3474.
    SABIO-RKQ99LJ1.

    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
    Synonyms:Fuca
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:95593. Fuca1.

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: RefGenome

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 452435Tissue alpha-L-fucosidasePRO_0000010310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ99LJ1.
    PaxDbiQ99LJ1.
    PRIDEiQ99LJ1.

    PTM databases

    PhosphoSiteiQ99LJ1.

    Expressioni

    Gene expression databases

    BgeeiQ99LJ1.
    GenevestigatoriQ99LJ1.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000030434.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99LJ1.
    SMRiQ99LJ1. Positions 22-435.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 29 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3669.
    GeneTreeiENSGT00440000035378.
    HOGENOMiHOG000029598.
    HOVERGENiHBG002155.
    InParanoidiB1AV51.
    KOiK01206.
    OMAiIFLHWPD.
    OrthoDBiEOG7DC249.
    PhylomeDBiQ99LJ1.
    TreeFamiTF313034.

    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.

    Q99LJ1-1 [UniParc]FASTAAdd to Basket

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    MLLLLLLLLV AAAQAVALAP RRFTPDWQSL DSRPLPSWFD EAKFGVFVHW    50
    GVFSVPAWGS EWFWWHWQGD RMPAYQRFMT ENYPPGFSYA DFAPQFTARF 100
    FHPDQWAELF QAAGAKYVVL TTKHHEGFTN WPSPVSWNWN SKDVGPHRDL 150
    VGELGAAVRK RNIRYGLYHS LLEWFHPLYL LDKKNGFKTQ HFVRAKTMPE 200
    LYDLVNSYKP DLIWSDGEWE CPDTYWNSTS FLAWLYNDSP VKDEVIVNDR 250
    WGQNCSCHHG GYYNCQDKYK PQSLPDHKWE MCTSMDRASW GYRKDMTMST 300
    IAKENEIIEE LVQTVSLGGN YLLNIGPTKD GLIVPIFQER LLAVGKWLQI 350
    NGEAIYASKP WRVQSEKNKT VVWYTTKNAT VYATFLYWPE NGIVNLKSPK 400
    TTSATKITML GLEGDLSWTQ DPLEGVLISL PQLPPTVLPV EFAWTLKLTK 450
    VN 452
    Length:452
    Mass (Da):52,281
    Last modified:June 1, 2001 - v1
    Checksum:i41B319A040152B2C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti379 – 3791A → T in BAC41012. (PubMed:16141072)Curated
    Sequence conflicti396 – 3961L → F in BAB21949. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002230 mRNA. Translation: BAB21949.1.
    AK053323 mRNA. Translation: BAC35346.1.
    AK089958 mRNA. Translation: BAC41012.1.
    AK151258 mRNA. Translation: BAE30247.1.
    AK151361 mRNA. Translation: BAE30336.1.
    AK151879 mRNA. Translation: BAE30765.1.
    AK151908 mRNA. Translation: BAE30789.1.
    AK165604 mRNA. Translation: BAE38288.1.
    AL672076 Genomic DNA. Translation: CAM15900.1.
    BC003235 mRNA. Translation: AAH03235.1.
    CCDSiCCDS18794.1.
    RefSeqiNP_077205.3. NM_024243.4.
    UniGeneiMm.439940.

    Genome annotation databases

    EnsembliENSMUST00000030434; ENSMUSP00000030434; ENSMUSG00000028673.
    GeneIDi71665.
    KEGGimmu:71665.
    UCSCiuc008vhi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK002230 mRNA. Translation: BAB21949.1 .
    AK053323 mRNA. Translation: BAC35346.1 .
    AK089958 mRNA. Translation: BAC41012.1 .
    AK151258 mRNA. Translation: BAE30247.1 .
    AK151361 mRNA. Translation: BAE30336.1 .
    AK151879 mRNA. Translation: BAE30765.1 .
    AK151908 mRNA. Translation: BAE30789.1 .
    AK165604 mRNA. Translation: BAE38288.1 .
    AL672076 Genomic DNA. Translation: CAM15900.1 .
    BC003235 mRNA. Translation: AAH03235.1 .
    CCDSi CCDS18794.1.
    RefSeqi NP_077205.3. NM_024243.4.
    UniGenei Mm.439940.

    3D structure databases

    ProteinModelPortali Q99LJ1.
    SMRi Q99LJ1. Positions 22-435.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000030434.

    Protein family/group databases

    CAZyi GH29. Glycoside Hydrolase Family 29.

    PTM databases

    PhosphoSitei Q99LJ1.

    Proteomic databases

    MaxQBi Q99LJ1.
    PaxDbi Q99LJ1.
    PRIDEi Q99LJ1.

    Protocols and materials databases

    DNASUi 71665.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030434 ; ENSMUSP00000030434 ; ENSMUSG00000028673 .
    GeneIDi 71665.
    KEGGi mmu:71665.
    UCSCi uc008vhi.2. mouse.

    Organism-specific databases

    CTDi 2517.
    MGIi MGI:95593. Fuca1.

    Phylogenomic databases

    eggNOGi COG3669.
    GeneTreei ENSGT00440000035378.
    HOGENOMi HOG000029598.
    HOVERGENi HBG002155.
    InParanoidi B1AV51.
    KOi K01206.
    OMAi IFLHWPD.
    OrthoDBi EOG7DC249.
    PhylomeDBi Q99LJ1.
    TreeFami TF313034.

    Enzyme and pathway databases

    BRENDAi 3.2.1.51. 3474.
    SABIO-RK Q99LJ1.

    Miscellaneous databases

    ChiTaRSi FUCA1. mouse.
    NextBioi 334183.
    PROi Q99LJ1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99LJ1.
    Genevestigatori Q99LJ1.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c and C57BL/6J.
      Tissue: Bone marrow, Colon, Eye and Kidney.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiFUCO_MOUSE
    AccessioniPrimary (citable) accession number: Q99LJ1
    Secondary accession number(s): B1AV51
    , Q3UAH8, Q8BN13, Q9DD22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3