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Q60648 (SAP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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:
Ganglioside GM2 activator
Alternative name(s):
Cerebroside sulfate activator protein
GM2-AP
Sphingolipid activator protein 3
Short name=SAP-3
Gene names
Name:Gm2a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. Ref.5

Subcellular location

Lysosome.

Tissue specificity

Widely expressed. Most abundant in kidney and testis.

Ontologies

Keywords
   Biological processLipid metabolism
Sphingolipid metabolism
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processganglioside catabolic process

Inferred from mutant phenotype PubMed 9223328. Source: MGI

learning or memory

Inferred from mutant phenotype PubMed 9223328. Source: MGI

lipid storage

Inferred from mutant phenotype PubMed 9223328. Source: MGI

neurological system process

Inferred from mutant phenotype PubMed 9223328. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 9223328. Source: MGI

oligosaccharide catabolic process

Inferred from mutant phenotype PubMed 9584189. Source: MGI

positive regulation of hydrolase activity

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical cortex

Inferred from electronic annotation. Source: Ensembl

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

nucleolus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from mutant phenotype PubMed 9584189. Source: MGI

enzyme activator activity

Inferred from direct assay PubMed 7980537. Source: MGI

lipid transporter activity

Inferred from electronic annotation. Source: Ensembl

phospholipase activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 193173Ganglioside GM2 activator
PRO_0000031643

Amino acid modifications

Glycosylation1511N-linked (GlcNAc...) Potential
Disulfide bond39 ↔ 183 Ref.5
Disulfide bond99 ↔ 106 Ref.5
Disulfide bond112 ↔ 138 Ref.5
Disulfide bond125 ↔ 136 Ref.5

Experimental info

Mutagenesis1681Y → S: Abolishes phospholipid binding. Ref.5
Sequence conflict531I → T in AAA21543. Ref.1

Secondary structure

........................ 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60648 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 59CC4ABE56FA1FC7

FASTA19320,824
        10         20         30         40         50         60 
MHRLPLLLLL GLLLAGSVAP ARLVPKRLSQ LGGFSWDNCD EGKDPAVIKS LTIQPDPIVV 

        70         80         90        100        110        120 
PGDVVVSLEG KTSVPLTAPQ KVELTVEKEV AGFWVKIPCV EQLGSCSYEN ICDLIDEYIP 

       130        140        150        160        170        180 
PGESCPEPLH TYGLPCHCPF KEGTYSLPTS NFTVPDLELP SWLSTGNYRI QSILSSGGKR 

       190 
LGCIKIAASL KGR 

« Hide

References

« Hide 'large scale' references
[1]"The mouse gene encoding the GM2 activator protein (Gm2a): cDNA sequence, expression, and chromosome mapping."
Yamanaka S., Johnson O.N., Lyu M.S., Kozak C.A., Proia R.L.
Genomics 24:601-604(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"Cloning and sequence analysis of a cDNA clone coding for the mouse GM2 activator protein."
Bellachioma G., Stirling J.L., Orlacchio A., Beccari T.
Biochem. J. 294:227-230(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structural organization and expression of the gene for the mouse GM2 activator protein."
Bertoni C., Appolloni M.G., Stirling J.L., Li S.C., Li Y.T., Orlacchio A., Beccari T.
Mamm. Genome 8:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6 X CBA.
[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: C57BL/6J.
Tissue: Mammary gland.
[5]"Crystal structure analysis of phosphatidylcholine-GM2-activator product complexes: evidence for hydrolase activity."
Wright C.S., Mi L.Z., Lee S., Rastinejad F.
Biochemistry 44:13510-13521(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-193 IN COMPLEX WITH LYSOPHOSPHATIDYLCHOLINE, FUNCTION, DISULFIDE BONDS, MUTAGENESIS OF TYR-168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09816 mRNA. Translation: AAA21543.1.
L19526 mRNA. Translation: AAA61929.1.
U34359 expand/collapse EMBL AC list , U34356, U34357, U34358 Genomic DNA. Translation: AAB06275.1. Sequence problems.
BC004651 mRNA. Translation: AAH04651.1.
CCDSCCDS24707.1.
PIRS35613.
RefSeqNP_034429.1. NM_010299.3.
UniGeneMm.287807.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGCX-ray2.50A32-193[»]
ProteinModelPortalQ60648.
SMRQ60648. Positions 32-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ60648. 2 interactions.
MINTMINT-4133787.

Proteomic databases

MaxQBQ60648.
PaxDbQ60648.
PRIDEQ60648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000608; ENSMUSP00000000608; ENSMUSG00000000594.
GeneID14667.
KEGGmmu:14667.
UCSCuc007iyw.2. mouse.

Organism-specific databases

CTD2760.
MGIMGI:95762. Gm2a.

Phylogenomic databases

eggNOGNOG47814.
GeneTreeENSGT00390000003288.
HOGENOMHOG000031350.
HOVERGENHBG000260.
InParanoidQ60648.
KOK12383.
OMAFSWENCD.
OrthoDBEOG7PCJHC.
PhylomeDBQ60648.
TreeFamTF353575.

Gene expression databases

ArrayExpressQ60648.
BgeeQ60648.
CleanExMM_GM2A.
GenevestigatorQ60648.

Family and domain databases

InterProIPR028996. GM2-AP.
IPR003172. ML_dom.
[Graphical view]
PANTHERPTHR17357. PTHR17357. 1 hit.
PfamPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60648.
NextBio286546.
PROQ60648.
SOURCESearch...

Entry information

Entry nameSAP3_MOUSE
AccessionPrimary (citable) accession number: Q60648
Secondary accession number(s): Q61610, Q61819
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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