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Q60648

- SAP3_MOUSE

UniProt

Q60648 - SAP3_MOUSE

Protein

Ganglioside GM2 activator

Gene

Gm2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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

    1. beta-N-acetylhexosaminidase activity Source: MGI
    2. enzyme activator activity Source: MGI
    3. lipid transporter activity Source: Ensembl
    4. phospholipase activator activity Source: Ensembl

    GO - Biological processi

    1. ganglioside catabolic process Source: MGI
    2. learning or memory Source: MGI
    3. lipid storage Source: MGI
    4. neurological system process Source: MGI
    5. neuromuscular process controlling balance Source: MGI
    6. oligosaccharide catabolic process Source: MGI
    7. positive regulation of hydrolase activity Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Sphingolipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199008. Glycosphingolipid metabolism.

    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
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95762. Gm2a.

    Subcellular locationi

    GO - Cellular componenti

    1. apical cortex Source: Ensembl
    2. cytoplasmic side of plasma membrane Source: Ensembl
    3. lysosome Source: UniProtKB-SubCell
    4. mitochondrion Source: MGI
    5. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681Y → S: Abolishes phospholipid binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 193173Ganglioside GM2 activatorPRO_0000031643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 1831 Publication
    Disulfide bondi99 ↔ 1061 Publication
    Disulfide bondi112 ↔ 1381 Publication
    Disulfide bondi125 ↔ 1361 Publication
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ60648.
    PaxDbiQ60648.
    PRIDEiQ60648.

    Expressioni

    Tissue specificityi

    Widely expressed. Most abundant in kidney and testis.

    Gene expression databases

    ArrayExpressiQ60648.
    BgeeiQ60648.
    CleanExiMM_GM2A.
    GenevestigatoriQ60648.

    Interactioni

    Protein-protein interaction databases

    IntActiQ60648. 2 interactions.
    MINTiMINT-4133787.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 395
    Helixi40 – 423
    Beta strandi44 – 5815
    Beta strandi60 – 7415
    Beta strandi81 – 9010
    Beta strandi93 – 964
    Beta strandi107 – 1093
    Helixi111 – 1188
    Turni127 – 1337
    Beta strandi142 – 15312
    Beta strandi165 – 17612
    Beta strandi179 – 19012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AGCX-ray2.50A32-193[»]
    ProteinModelPortaliQ60648.
    SMRiQ60648. Positions 32-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60648.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG47814.
    GeneTreeiENSGT00390000003288.
    HOGENOMiHOG000031350.
    HOVERGENiHBG000260.
    InParanoidiQ60648.
    KOiK12383.
    OMAiFSWENCD.
    OrthoDBiEOG7PCJHC.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q60648-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHRLPLLLLL GLLLAGSVAP ARLVPKRLSQ LGGFSWDNCD EGKDPAVIKS    50
    LTIQPDPIVV PGDVVVSLEG KTSVPLTAPQ KVELTVEKEV AGFWVKIPCV 100
    EQLGSCSYEN ICDLIDEYIP PGESCPEPLH TYGLPCHCPF KEGTYSLPTS 150
    NFTVPDLELP SWLSTGNYRI QSILSSGGKR LGCIKIAASL KGR 193
    Length:193
    Mass (Da):20,824
    Last modified:November 1, 1997 - v2
    Checksum:i59CC4ABE56FA1FC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531I → T in AAA21543. (PubMed:7713516)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS24707.1.
    PIRi S35613.
    RefSeqi NP_034429.1. NM_010299.3.
    UniGenei Mm.287807.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AGC X-ray 2.50 A 32-193 [» ]
    ProteinModelPortali Q60648.
    SMRi Q60648. Positions 32-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q60648. 2 interactions.
    MINTi MINT-4133787.

    Proteomic databases

    MaxQBi Q60648.
    PaxDbi Q60648.
    PRIDEi Q60648.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000608 ; ENSMUSP00000000608 ; ENSMUSG00000000594 .
    GeneIDi 14667.
    KEGGi mmu:14667.
    UCSCi uc007iyw.2. mouse.

    Organism-specific databases

    CTDi 2760.
    MGIi MGI:95762. Gm2a.

    Phylogenomic databases

    eggNOGi NOG47814.
    GeneTreei ENSGT00390000003288.
    HOGENOMi HOG000031350.
    HOVERGENi HBG000260.
    InParanoidi Q60648.
    KOi K12383.
    OMAi FSWENCD.
    OrthoDBi EOG7PCJHC.
    PhylomeDBi Q60648.
    TreeFami TF353575.

    Enzyme and pathway databases

    Reactomei REACT_199008. Glycosphingolipid metabolism.

    Miscellaneous databases

    EvolutionaryTracei Q60648.
    NextBioi 286546.
    PROi Q60648.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60648.
    Bgeei Q60648.
    CleanExi MM_GM2A.
    Genevestigatori Q60648.

    Family and domain databases

    InterProi IPR028996. GM2-AP.
    IPR003172. ML_dom.
    [Graphical view ]
    PANTHERi PTHR17357. PTHR17357. 1 hit.
    Pfami PF02221. E1_DerP2_DerF2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 108 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

    External Data

    Dasty 3