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Ganglioside GM2 activator (Cerebroside sulfate activator protein) (GM2-AP) (Sphingolipid activator protein 3) (SAP-3)

 SAP3_MOUSE              Reviewed;         193 AA.
Q60648; Q61610; Q61819;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
12-SEP-2018, entry version 135.
RecName: Full=Ganglioside GM2 activator;
AltName: Full=Cerebroside sulfate activator protein;
AltName: Full=GM2-AP;
AltName: Full=Sphingolipid activator protein 3;
Short=SAP-3;
Flags: Precursor;
Name=Gm2a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=7713516; DOI=10.1006/geno.1994.1674;
Yamanaka S., Johnson O.N., Lyu M.S., Kozak C.A., Proia R.L.;
"The mouse gene encoding the GM2 activator protein (Gm2a): cDNA
sequence, expression, and chromosome mapping.";
Genomics 24:601-604(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7689829; DOI=10.1042/bj2940227;
Bellachioma G., Stirling J.L., Orlacchio A., Beccari T.;
"Cloning and sequence analysis of a cDNA clone coding for the mouse
GM2 activator protein.";
Biochem. J. 294:227-230(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6 X CBA;
PubMed=9060405; DOI=10.1007/s003359900364;
Bertoni C., Appolloni M.G., Stirling J.L., Li S.C., Li Y.T.,
Orlacchio A., Beccari T.;
"Structural organization and expression of the gene for the mouse GM2
activator protein.";
Mamm. Genome 8:90-93(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-193 IN COMPLEX WITH
LYSOPHOSPHATIDYLCHOLINE, FUNCTION, DISULFIDE BONDS, AND MUTAGENESIS OF
TYR-168.
PubMed=16216074; DOI=10.1021/bi050668w;
Wright C.S., Mi L.Z., Lee S., Rastinejad F.;
"Crystal structure analysis of phosphatidylcholine-GM2-activator
product complexes: evidence for hydrolase activity.";
Biochemistry 44:13510-13521(2005).
-!- 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.
{ECO:0000269|PubMed:16216074}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Widely expressed. Most abundant in kidney and
testis.
-----------------------------------------------------------------------
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EMBL; U09816; AAA21543.1; -; mRNA.
EMBL; L19526; AAA61929.1; -; mRNA.
EMBL; U34359; AAB06275.1; ALT_SEQ; Genomic_DNA.
EMBL; U34356; AAB06275.1; JOINED; Genomic_DNA.
EMBL; U34357; AAB06275.1; JOINED; Genomic_DNA.
EMBL; U34358; AAB06275.1; JOINED; Genomic_DNA.
EMBL; BC004651; AAH04651.1; -; mRNA.
CCDS; CCDS24707.1; -.
PIR; S35613; S35613.
RefSeq; NP_034429.1; NM_010299.3.
UniGene; Mm.287807; -.
PDB; 2AGC; X-ray; 2.50 A; A=32-193.
PDBsum; 2AGC; -.
ProteinModelPortal; Q60648; -.
SMR; Q60648; -.
IntAct; Q60648; 2.
MINT; Q60648; -.
STRING; 10090.ENSMUSP00000000608; -.
EPD; Q60648; -.
MaxQB; Q60648; -.
PaxDb; Q60648; -.
PRIDE; Q60648; -.
Ensembl; ENSMUST00000000608; ENSMUSP00000000608; ENSMUSG00000000594.
GeneID; 14667; -.
KEGG; mmu:14667; -.
UCSC; uc007iyw.2; mouse.
CTD; 2760; -.
MGI; MGI:95762; Gm2a.
eggNOG; ENOG410IX9N; Eukaryota.
eggNOG; ENOG4111JSM; LUCA.
GeneTree; ENSGT00390000003288; -.
HOGENOM; HOG000031350; -.
HOVERGEN; HBG000260; -.
InParanoid; Q60648; -.
KO; K12383; -.
OMA; WLSTGNY; -.
OrthoDB; EOG091G0VEB; -.
PhylomeDB; Q60648; -.
TreeFam; TF353575; -.
Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Gm2a; mouse.
EvolutionaryTrace; Q60648; -.
PRO; PR:Q60648; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000594; Expressed in 301 organ(s), highest expression level in placenta.
CleanEx; MM_GM2A; -.
ExpressionAtlas; Q60648; baseline and differential.
Genevisible; Q60648; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0032428; F:beta-N-acetylgalactosaminidase activity; IEA:Ensembl.
GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IMP:MGI.
GO; GO:0008047; F:enzyme activator activity; IDA:MGI.
GO; GO:0005319; F:lipid transporter activity; IEA:Ensembl.
GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
GO; GO:0006689; P:ganglioside catabolic process; IMP:MGI.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:0019915; P:lipid storage; IMP:MGI.
GO; GO:0050877; P:nervous system process; IMP:MGI.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
GO; GO:0009313; P:oligosaccharide catabolic process; IMP:MGI.
GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
Gene3D; 2.70.220.10; -; 1.
InterPro; IPR028996; GM2-AP.
InterPro; IPR036846; GM2-AP_sf.
InterPro; IPR003172; ML_dom.
PANTHER; PTHR17357; PTHR17357; 1.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF63707; SSF63707; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Lipid metabolism; Lysosome; Reference proteome; Signal;
Sphingolipid metabolism.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 193 Ganglioside GM2 activator.
/FTId=PRO_0000031643.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 183 {ECO:0000269|PubMed:16216074}.
DISULFID 99 106 {ECO:0000269|PubMed:16216074}.
DISULFID 112 138 {ECO:0000269|PubMed:16216074}.
DISULFID 125 136 {ECO:0000269|PubMed:16216074}.
MUTAGEN 168 168 Y->S: Abolishes phospholipid binding.
{ECO:0000269|PubMed:16216074}.
CONFLICT 53 53 I -> T (in Ref. 1; AAA21543).
{ECO:0000305}.
STRAND 35 39 {ECO:0000244|PDB:2AGC}.
HELIX 40 42 {ECO:0000244|PDB:2AGC}.
STRAND 44 58 {ECO:0000244|PDB:2AGC}.
STRAND 60 74 {ECO:0000244|PDB:2AGC}.
STRAND 81 90 {ECO:0000244|PDB:2AGC}.
STRAND 93 96 {ECO:0000244|PDB:2AGC}.
STRAND 107 109 {ECO:0000244|PDB:2AGC}.
HELIX 111 118 {ECO:0000244|PDB:2AGC}.
TURN 127 133 {ECO:0000244|PDB:2AGC}.
STRAND 142 153 {ECO:0000244|PDB:2AGC}.
STRAND 165 176 {ECO:0000244|PDB:2AGC}.
STRAND 179 190 {ECO:0000244|PDB:2AGC}.
SEQUENCE 193 AA; 20824 MW; 59CC4ABE56FA1FC7 CRC64;
MHRLPLLLLL GLLLAGSVAP ARLVPKRLSQ LGGFSWDNCD EGKDPAVIKS LTIQPDPIVV
PGDVVVSLEG KTSVPLTAPQ KVELTVEKEV AGFWVKIPCV EQLGSCSYEN ICDLIDEYIP
PGESCPEPLH TYGLPCHCPF KEGTYSLPTS NFTVPDLELP SWLSTGNYRI QSILSSGGKR
LGCIKIAASL KGR


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