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Protein

Ganglioside GM2 activator

Gene

Gm2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • beta-N-acetylgalactosaminidase activity Source: Ensembl
  • beta-N-acetylhexosaminidase activity Source: MGI
  • enzyme activator activity Source: MGI
  • lipid transporter activity Source: Ensembl
  • phospholipase activator activity Source: Ensembl

GO - Biological processi

  • ganglioside catabolic process Source: MGI
  • learning or memory Source: MGI
  • lipid storage Source: MGI
  • neurological system process Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • oligosaccharide catabolic process Source: MGI
  • positive regulation of hydrolase activity Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ganglioside GM2 activator
Alternative name(s):
Cerebroside sulfate activator protein
GM2-AP
Sphingolipid activator protein 3
Short name:
SAP-3
Gene namesi
Name:Gm2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95762. Gm2a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi168Y → S: Abolishes phospholipid binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003164321 – 193Ganglioside GM2 activatorAdd BLAST173

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 1831 Publication
Disulfide bondi99 ↔ 1061 Publication
Disulfide bondi112 ↔ 1381 Publication
Disulfide bondi125 ↔ 1361 Publication
Glycosylationi151N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ60648.
MaxQBiQ60648.
PaxDbiQ60648.
PRIDEiQ60648.

Expressioni

Tissue specificityi

Widely expressed. Most abundant in kidney and testis.

Gene expression databases

BgeeiENSMUSG00000000594.
CleanExiMM_GM2A.
ExpressionAtlasiQ60648. baseline and differential.
GenevisibleiQ60648. MM.

Interactioni

Protein-protein interaction databases

IntActiQ60648. 2 interactors.
MINTiMINT-4133787.
STRINGi10090.ENSMUSP00000000608.

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 39Combined sources5
Helixi40 – 42Combined sources3
Beta strandi44 – 58Combined sources15
Beta strandi60 – 74Combined sources15
Beta strandi81 – 90Combined sources10
Beta strandi93 – 96Combined sources4
Beta strandi107 – 109Combined sources3
Helixi111 – 118Combined sources8
Turni127 – 133Combined sources7
Beta strandi142 – 153Combined sources12
Beta strandi165 – 176Combined sources12
Beta strandi179 – 190Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGCX-ray2.50A32-193[»]
ProteinModelPortaliQ60648.
SMRiQ60648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60648.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IX9N. Eukaryota.
ENOG4111JSM. LUCA.
GeneTreeiENSGT00390000003288.
HOGENOMiHOG000031350.
HOVERGENiHBG000260.
InParanoidiQ60648.
KOiK12383.
OMAiGCIKIAA.
OrthoDBiEOG091G0VEB.
PhylomeDBiQ60648.
TreeFamiTF353575.

Family and domain databases

InterProiIPR028996. GM2-AP.
IPR003172. ML_dom.
[Graphical view]
PANTHERiPTHR17357. PTHR17357. 1 hit.
PfamiPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTiSM00737. ML. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q60648-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRLPLLLLL GLLLAGSVAP ARLVPKRLSQ LGGFSWDNCD EGKDPAVIKS
60 70 80 90 100
LTIQPDPIVV PGDVVVSLEG KTSVPLTAPQ KVELTVEKEV AGFWVKIPCV
110 120 130 140 150
EQLGSCSYEN ICDLIDEYIP PGESCPEPLH TYGLPCHCPF KEGTYSLPTS
160 170 180 190
NFTVPDLELP SWLSTGNYRI QSILSSGGKR LGCIKIAASL KGR
Length:193
Mass (Da):20,824
Last modified:November 1, 1997 - v2
Checksum:i59CC4ABE56FA1FC7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53I → T in AAA21543 (PubMed:7713516).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09816 mRNA. Translation: AAA21543.1.
L19526 mRNA. Translation: AAA61929.1.
U34359
, U34356, U34357, U34358 Genomic DNA. Translation: AAB06275.1. Sequence problems.
BC004651 mRNA. Translation: AAH04651.1.
CCDSiCCDS24707.1.
PIRiS35613.
RefSeqiNP_034429.1. NM_010299.3.
UniGeneiMm.287807.

Genome annotation databases

EnsembliENSMUST00000000608; ENSMUSP00000000608; ENSMUSG00000000594.
GeneIDi14667.
KEGGimmu:14667.
UCSCiuc007iyw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09816 mRNA. Translation: AAA21543.1.
L19526 mRNA. Translation: AAA61929.1.
U34359
, U34356, U34357, U34358 Genomic DNA. Translation: AAB06275.1. Sequence problems.
BC004651 mRNA. Translation: AAH04651.1.
CCDSiCCDS24707.1.
PIRiS35613.
RefSeqiNP_034429.1. NM_010299.3.
UniGeneiMm.287807.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGCX-ray2.50A32-193[»]
ProteinModelPortaliQ60648.
SMRiQ60648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60648. 2 interactors.
MINTiMINT-4133787.
STRINGi10090.ENSMUSP00000000608.

Proteomic databases

EPDiQ60648.
MaxQBiQ60648.
PaxDbiQ60648.
PRIDEiQ60648.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000608; ENSMUSP00000000608; ENSMUSG00000000594.
GeneIDi14667.
KEGGimmu:14667.
UCSCiuc007iyw.2. mouse.

Organism-specific databases

CTDi2760.
MGIiMGI:95762. Gm2a.

Phylogenomic databases

eggNOGiENOG410IX9N. Eukaryota.
ENOG4111JSM. LUCA.
GeneTreeiENSGT00390000003288.
HOGENOMiHOG000031350.
HOVERGENiHBG000260.
InParanoidiQ60648.
KOiK12383.
OMAiGCIKIAA.
OrthoDBiEOG091G0VEB.
PhylomeDBiQ60648.
TreeFamiTF353575.

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiGm2a. mouse.
EvolutionaryTraceiQ60648.
PROiQ60648.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000594.
CleanExiMM_GM2A.
ExpressionAtlasiQ60648. baseline and differential.
GenevisibleiQ60648. MM.

Family and domain databases

InterProiIPR028996. GM2-AP.
IPR003172. ML_dom.
[Graphical view]
PANTHERiPTHR17357. PTHR17357. 1 hit.
PfamiPF02221. E1_DerP2_DerF2. 1 hit.
[Graphical view]
SMARTiSM00737. ML. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAP3_MOUSE
AccessioniPrimary (citable) accession number: Q60648
Secondary accession number(s): Q61610, Q61819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.