ID   SAP3_MACFA              Reviewed;         190 AA.
AC   Q8HXX6; Q60HF5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Ganglioside GM2 activator;
DE   AltName: Full=Cerebroside sulfate activator protein;
DE   AltName: Full=GM2-AP;
DE   AltName: Full=Sphingolipid activator protein 3;
DE            Short=SAP-3;
DE   Flags: Precursor;
GN   Name=GM2A; ORFNames=QccE-17591;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Temporal cortex;
RA   Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The large binding pocket can accommodate several single chain
CC       phospholipids and fatty acids, GM2A also exhibits some calcium-
CC       independent phospholipase activity (By similarity). Binds gangliosides
CC       and stimulates ganglioside GM2 degradation. It stimulates only the
CC       breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase
CC       A. It extracts single GM2 molecules from membranes and presents them in
CC       soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-
CC       galactosamine and conversion to GM3 (By similarity). Has cholesterol
CC       transfer activity (By similarity). {ECO:0000250|UniProtKB:P17900,
CC       ECO:0000250|UniProtKB:Q60648}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC         ChEBI:CHEBI:16113; Evidence={ECO:0000250|UniProtKB:P17900};
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
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DR   EMBL; AB083313; BAC20592.1; -; mRNA.
DR   EMBL; AB125172; BAD51960.1; -; mRNA.
DR   RefSeq; NP_001270491.1; NM_001283562.1.
DR   AlphaFoldDB; Q8HXX6; -.
DR   SMR; Q8HXX6; -.
DR   STRING; 9541.XP_005558361.1; -.
DR   GeneID; 102143555; -.
DR   CTD; 2760; -.
DR   eggNOG; ENOG502S05S; Eukaryota.
DR   OrthoDB; 1548356at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006689; P:ganglioside catabolic process; IEA:InterPro.
DR   Gene3D; 2.70.220.10; -; 1.
DR   InterPro; IPR028996; GM2-AP.
DR   InterPro; IPR036846; GM2-AP_sf.
DR   InterPro; IPR003172; ML_dom.
DR   PANTHER; PTHR17357; PTHR17357; 1.
DR   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
DR   SUPFAM; SSF63707; SSF63707; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid metabolism; Lysosome;
KW   Reference proteome; Signal; Sphingolipid metabolism.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..190
FT                   /note="Ganglioside GM2 activator"
FT                   /id="PRO_0000031642"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..180
FT                   /evidence="ECO:0000250"
FT   DISULFID        96..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..133
FT                   /evidence="ECO:0000250"
FT   CONFLICT        72
FT                   /note="L -> P (in Ref. 1; BAC20592)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="F -> S (in Ref. 1; BAC20592)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="P -> G (in Ref. 1; BAC20592)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20610 MW;  140C12A41AE30937 CRC64;
     MQSLMQAPVL IALGLLFAAP AQAHLKKLGS FSWDNCDEGK DPAVIRSLTL EPDPILIPGN
     VTVSVVGSTS VLLSSPLKVE LVLEKEVAGL WIKIPCTDYI GSCTFEDFCD VLDMLIPTGE
     PCPEPLRTYG LPCHCPFKEG TYSLPKSEFV VPHLELPSWL TTGNYRIESI LSNRGKRLGC
     IKIAASLKGV