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Protein

Alpha-N-acetylgalactosaminidase

Gene

NAGA

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

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

GO - Biological processi

Complete GO annotation...

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

GO - Cellular componenti

Complete GO annotation...

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.

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

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

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: January 7, 2015
This is version 30 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.