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Q66H12 (NAGAB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 415398Alpha-N-acetylgalactosaminidase
PRO_0000001020

Regions

Region78 – 792Substrate binding By similarity

Sites

Active site1561Nucleophile By similarity
Active site2171Proton donor By similarity
Binding site1541Substrate By similarity
Binding site1881Substrate By similarity
Binding site2131Substrate By similarity
Binding site2171Substrate By similarity

Amino acid modifications

Modified residue3221Phosphoserine By similarity
Modified residue3321Phosphoserine By similarity
Glycosylation1771N-linked (GlcNAc...) By similarity
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3851N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Disulfide bond38 ↔ 80 By similarity
Disulfide bond42 ↔ 49 By similarity
Disulfide bond127 ↔ 158 By similarity
Disulfide bond187 ↔ 209 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66H12 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 57605634B3F74C6E

FASTA41546,871
        10         20         30         40         50         60 
MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI NCEEDPKNCI SERLFMEMAD 

        70         80         90        100        110        120 
RLAQDGWRDL GYVYLNIDDC WIGGRDATGR LIPDPKRFPH GIAFLADYAH SLGLKLGIYE 

       130        140        150        160        170        180 
DMGKMTCMGY PGTTLDKVEL DAATFAEWKV DMLKLDGCYS TPKERAEGYP KMAAALNATG 

       190        200        210        220        230        240 
RPIAFSCSWP AYEGGLPPKV NYTEVAGTCN LWRNYKDIQD SWKSVLSILD WFVKHQDILQ 

       250        260        270        280        290        300 
PVSGPGHWND PDMLLIGNFG LSFDESRAQM ALWTVLAAPL FMSTDLRTIS PQNIDILQNP 

       310        320        330        340        350        360 
LLIKINQDPL GIQGRLIFKS KSHIEVFKRN LSDDASALVF FSRRTDMPYH FHCSLLELNY 

       370        380        390        400        410 
PKGSVYEGQN VFTGDIISGL HPETNFTVII NPSGVVMWYL YPVKGLGIYT MMSQL 

« Hide

References

[1]"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].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC082084 mRNA. Translation: AAH82084.1.
RefSeqNP_001012120.1. NM_001012120.1.
XP_006242149.1. XM_006242087.1.
XP_006242150.1. XM_006242088.1.
UniGeneRn.55746.

3D structure databases

ProteinModelPortalQ66H12.
SMRQ66H12. Positions 18-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ66H12. 1 interaction.
STRING10116.ENSRNOP00000011045.

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

Proteomic databases

PaxDbQ66H12.
PRIDEQ66H12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000068020; ENSRNOP00000060590; ENSRNOG00000008064.
GeneID315165.
KEGGrno:315165.
UCSCRGD:1306025. rat.

Organism-specific databases

CTD4668.
RGD1306025. Naga.

Phylogenomic databases

eggNOGNOG68897.
GeneTreeENSGT00390000008751.
HOGENOMHOG000161224.
HOVERGENHBG001989.
InParanoidQ66H12.
KOK01204.
OMAERAKGYP.
OrthoDBEOG7F24SV.
PhylomeDBQ66H12.
TreeFamTF312909.

Gene expression databases

GenevestigatorQ66H12.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR013780. Glyco_hydro_13_b.
IPR002241. Glyco_hydro_27.
IPR000111. Glyco_hydro_GHD.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02065. Melibiase. 1 hit.
[Graphical view]
PRINTSPR00740. GLHYDRLASE27.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00512. ALPHA_GALACTOSIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio668806.
PROQ66H12.

Entry information

Entry nameNAGAB_RAT
AccessionPrimary (citable) accession number: Q66H12
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 73 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