O70362
uniprot
O70362
canonical
amino_acid_sequence
MSAGRLWSSLLLLLPLFCSKSSSCGLSTHVEIGHRALEFLRLQDGRINYKELILEHQDAYQAGTVFPDAFYPSICKRGKYHDVSERTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGITSHMVADLSWHNLGFLRTMGAIDFYNSYSDAHSAGDFGGDVLSQFEFNFNYLSRRWYVPVRDLLRIYDNLYGRKVITKDVLVDCTYLQFLEMHGEMFAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRNHTLSGSKVQKNDFHRNLTMFISRDIRKNLNYTERGVFYSTGSWARPESVTFMYQTLERNLRLMLAGSSQKNLNHVSSPSASYTLSVPYARLGWVMTSADLNQDGHGDLVVGAPGYSHPGRFQIGRVYIIYGNDLGLPPIDLDLNKEGILEGFQPSGRFGSALAVLDFNQDGLPDLAVGAPSVGSGQLTYNGSVYVYYGSQQGRLSSSPNVTISCKDTYCNLGWTLLATDADGDGRHDLVISSPFAPGGRKQKGIVATFYSHPRRNDKELLTLEEADWKVNGEEDFSWFGYSLHGVTVANRSLLLIGSPTWKNVSRMARSSHKKNQEEKSLGKVYGYFLPNRQSTITISGDKAMGKLGTSLSSGYVRVNGTLTQVLLVGAPTHDDVSKMAFLTMTLHQGGATRMYELAPEKTQPALLSTFSGDRRFSRFGSVLHLTDLDDDGLDEIIMAAPLRITDVTSGLLGGEDGRVYIYNGMYTTLGDMTGKCKSWMTPCPEEKAQYVLTSPEASSRFGSSLVSVRSKGRNQVVVAAGRSSWGARLSGALHVYSFSSD
uniprot
proteins
ec_number
3.1.4.50
uniprot
proteins
function
FUNCTION: Hydrolyzes the inositol phosphate linkage of glycosylphosphatidylinositol (GPI)-anchored membrane proteins, thereby releasing them from the cell surface. Cleaves on the inositol side of the anchor, leaving the phosphate group attached to the membrane (PubMed:17720976). This release of GPI-anchored proteins can modulate diverse biological processes, including the activation of signaling pathways (PubMed:17720976). {ECO:0000269|PubMed:17720976}.
uniprot
proteins
mass_dalton
93255
uniprot
proteins
protein_family
GPLD1 family
uniprot
proteins
pubmed
16944957
uniprot
proteins
pubmed
17330941
uniprot
proteins
pubmed
17720976
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9716655
uniprot
proteins
sequence_length
837
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80108}. Note=Associated with the High-Density Lipoproteins (HDL). {ECO:0000250|UniProtKB:P80109}.
uniprot
proteins