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P83127

- NAGAB_BOSIN

UniProt

P83127 - NAGAB_BOSIN

Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

Organism
Bos indicus (Zebu)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Removes terminal alpha-N-acetylgalactosamine residues from glycolipids and glycopeptides. Required for the breakdown of glycolipids By similarity.By similarity

    Catalytic activityi

    Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine residues from human blood group A and AB mucin glycoproteins, Forssman hapten and blood group A lacto series glycolipids.

    GO - Molecular functioni

    1. alpha-N-acetylgalactosaminidase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate catabolic process Source: UniProtKB
    2. glycolipid catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-N-acetylgalactosaminidase (EC:3.2.1.49)
    Alternative name(s):
    Alpha-galactosidase B
    Gene namesi
    Name:NAGA
    OrganismiBos indicus (Zebu)
    Taxonomic identifieri9915 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›12›12Alpha-N-acetylgalactosaminidasePRO_0000134872Add
    BLAST

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Tissue specificityi

    Placenta.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 27 family.Curated

    Sequencei

    Sequence statusi: Fragment.

    P83127-1 [UniParc]FASTAAdd to Basket

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    LENGLLRKPP MG                                            12
    Length:12
    Mass (Da):1,325
    Last modified:June 1, 2002 - v1
    Checksum:i53B124381F240727
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei12 – 121

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Characterization of pregnancy-associated glycoproteins extracted from zebu (Bos indicus) placentas removed at different gestational periods."
      Sousa N.M., Remy B., El Amiri B., De Figueiredo J.R., Banga-Mboko H., Dias Goncalves P.B., Beckers J.-F.M.P.
      Reprod. Nutr. Dev. 42:227-241(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, TISSUE SPECIFICITY, GLYCOSYLATION.
      Tissue: Fetal cotyledon.

    Entry informationi

    Entry nameiNAGAB_BOSIN
    AccessioniPrimary (citable) accession number: P83127
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 28 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

    Direct protein sequencing

    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