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P51569 (AGAL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-galactosidase A

EC=3.2.1.22
Alternative name(s):
Alpha-D-galactosidase A
Alpha-D-galactoside galactohydrolase
Melibiase
Gene names
Name:Gla
Synonyms:Ags
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.

Subunit structure

Homodimer.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the glycosyl hydrolase 27 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycoside catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

glycosylceramide catabolic process

Inferred from direct assay PubMed 10840053PubMed 15629890. Source: MGI

negative regulation of nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 15668341. Source: UniProtKB

negative regulation of nitric-oxide synthase activity

Inferred from mutant phenotype PubMed 15668341. Source: UniProtKB

oligosaccharide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionalpha-galactosidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

galactoside binding

Inferred from electronic annotation. Source: Ensembl

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

raffinose alpha-galactosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 By similarity
Chain32 – 419388Alpha-galactosidase A
PRO_0000001005

Regions

Region203 – 2075Substrate binding By similarity

Sites

Active site1701Nucleophile By similarity
Active site2311Proton donor By similarity

Amino acid modifications

Modified residue1861Phosphotyrosine Ref.5
Glycosylation1391N-linked (GlcNAc...) By similarity
Glycosylation1921N-linked (GlcNAc...) By similarity
Glycosylation2151N-linked (GlcNAc...) By similarity
Disulfide bond52 ↔ 94 By similarity
Disulfide bond56 ↔ 63 By similarity
Disulfide bond142 ↔ 172 By similarity
Disulfide bond202 ↔ 223 By similarity
Disulfide bond378 ↔ 382 By similarity

Sequences

Sequence LengthMass (Da)Tools
P51569 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BD5E6A99AC113613

FASTA41947,643
        10         20         30         40         50         60 
MKLLSRDTRL VCELALCPLA LVFWSILGVR ALDNGLARTP TMGWLHWERF MCNLDCQEEP 

        70         80         90        100        110        120 
DACISEQLFM QMAELMVSDG WRDAGYDYLC IDDCWMAPER DSKGRLQADP QRFPSGIKHL 

       130        140        150        160        170        180 
ANYVHSKGLK LGIYADVGNK TCAGFPGSFG SYDIDAQTFA DWGVDLLKFD GCHCDSVVSL 

       190        200        210        220        230        240 
ENGYKYMALA LNRTGRSIVY SCEWPLYLRP FHKPNYTDIQ YYCNHWRNFD DVYDSWESIK 

       250        260        270        280        290        300 
NILSWTVVYQ KEIVEVAGPG SWNDPDMLVI GNFGLSWDQQ VTQMALWAIM AAPLLMSNDL 

       310        320        330        340        350        360 
RQISSQAKAL LQNKDVIAIN QDPLGKQGYC FRKENHIEVW ERPLSNLAWA VAVRNLQEIG 

       370        380        390        400        410 
GPCPYTIQIS SLGRGLACNP GCIITQLLPE KVHLGFYEWT LTLKTRVNPS GTVLFRLER 

« Hide

References

« Hide 'large scale' references
[1]"Structural organization and expression of the mouse gene encoding alpha-galactosidase A."
Ohshima T., Murray G.J., Nagle J.W., Quirk J.M., Kraus M.H., Barton N.W., Brady R.O., Kulkarni A.B.
Gene 166:277-280(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[2]"Sixty-nine kilobases of contiguous human genomic sequence containing the alpha-galactosidase A and Bruton's tyrosine kinase loci."
Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., Gibbs R.A.
Mamm. Genome 6:334-338(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C129.
[3]"The entire genomic sequence and cDNA expression of mouse alpha-galactosidase A."
Gotlib R.W., Bishop D.F., Wang A.M., Zeidner K.M., Ioannou Y.I., Adler D.A., Disteche C.M., Desnick R.J.
Biochem. Mol. Med. 57:139-148(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"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 gland.
[5]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U34071 mRNA. Translation: AAA96749.1.
L46651 Genomic DNA. Translation: AAA74453.1.
U58105 Genomic DNA. Translation: AAB47244.1.
U50716 mRNA. Translation: AAC52584.1.
U50715 Genomic DNA. Translation: AAC52583.1.
BC009021 mRNA. Translation: AAH09021.1.
PIRJC4522.
UniGeneMm.1114.

3D structure databases

ProteinModelPortalP51569.
SMRP51569. Positions 32-418.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP51569. 1 interaction.
MINTMINT-4087336.

Protein family/group databases

CAZyGH27. Glycoside Hydrolase Family 27.

PTM databases

PhosphoSiteP51569.

Proteomic databases

MaxQBP51569.
PaxDbP51569.
PRIDEP51569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1347344. Gla.

Phylogenomic databases

eggNOGNOG68897.
HOVERGENHBG001989.
InParanoidP51569.

Gene expression databases

ArrayExpressP51569.
BgeeP51569.
CleanExMM_GLA.
GenevestigatorP51569.

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

PROP51569.
SOURCESearch...

Entry information

Entry nameAGAL_MOUSE
AccessionPrimary (citable) accession number: P51569
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 105 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries