UniProt functional annotation for P17900



	UniProt functional annotation for P17900

UniProt code: P17900.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium- independent phospholipase activity (By similarity). 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 (By similarity). Has cholesterol transfer activity (PubMed:17552909). {ECO:0000250|UniProtKB:Q60648, ECO:0000269|PubMed:17552909}.

Catalytic activity: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:17552909};

Subcellular location: Lysosome.

Ptm: The serines in positions 32 and 33 are absent in 80% of the sequenced protein.

Disease: GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the presence of both normal hexosaminidase A and B. {ECO:0000269|PubMed:1915858, ECO:0000269|PubMed:8244332, ECO:0000269|PubMed:8900233}. Note=The disease is caused by variants affecting the gene represented in this entry.

Sequence caution: Sequence=CAA43408.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=CAA43994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium- independent phospholipase activity (By similarity). 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 (By similarity). Has cholesterol transfer activity (PubMed:17552909). {ECO:0000250\|UniProtKB:Q60648, ECO:0000269\|PubMed:17552909}.


Catalytic activity:		Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000269\|PubMed:17552909};
Subcellular location:		Lysosome.
Ptm:		The serines in positions 32 and 33 are absent in 80% of the sequenced protein.
Disease:		GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal recessive lysosomal storage disease marked by the accumulation of GM2 gangliosides in the neuronal cells. It is characterized by GM2 gangliosides accumulation in the presence of both normal hexosaminidase A and B. {ECO:0000269\|PubMed:1915858, ECO:0000269\|PubMed:8244332, ECO:0000269\|PubMed:8900233}. Note=The disease is caused by variants affecting the gene represented in this entry.
Sequence caution:		Sequence=CAA43408.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; Sequence=CAA43994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};