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P83127 (NAGAB_BOSIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-N-acetylgalactosaminidase

EC=3.2.1.49
Alternative name(s):
Alpha-galactosidase B
Gene names
Name:NAGA
OrganismBos indicus (Zebu)
Taxonomic identifier9915 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length12 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Subunit structure

Homodimer By similarity.

Subcellular location

Lysosome By similarity.

Tissue specificity

Placenta. Ref.1

Post-translational modification

Glycosylated. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Ontologies

Keywords
   Cellular componentLysosome
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycolipid catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-N-acetylgalactosaminidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›12›12Alpha-N-acetylgalactosaminidase
PRO_0000134872

Experimental info

Non-terminal residue121

Sequences

Sequence LengthMass (Da)Tools
P83127 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 53B124381F240727

FASTA121,325
        10 
LENGLLRKPP MG 

« Hide

References

[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.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameNAGAB_BOSIN
AccessionPrimary (citable) accession number: P83127
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2002
Last modified: February 19, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries