SMPDL3A
entrez
10924
canonical
uniprot
Q92484
canonical
ensembl
ENSG00000172594
resolver
ensp
ENSP00000357425
resolver
ensp
ENSP00000442152
resolver
genesymbol
SMPDL3A
resolver
genesymbol_syn
ASML3A
resolver
hgnc
HGNC:17389
resolver
uniprot
B7Z729
resolver
uniprot
Q8WV13
resolver
uniprot_entry
ASM3A_HUMAN
resolver
uniprot_sec
B7Z729
resolver
uniprot_sec
Q8WV13
resolver
activity_regulation
ACTIVITY REGULATION: Requires micromolar levels of Zn(2+) for activity (PubMed:26783088). Inhibited by millimolar levels of Zn(2+) (PubMed:25288789, PubMed:26783088). {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:26783088}.
uniprot
proteins
amino_acid_sequence
MALVRALVCCLLTAWHCRSGLGLPVAPAGGRNPPPAIGQFWHVTDLHLDPTYHITDDHTKVCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLDEEAISTLRKGGFYSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNITAMREYYNEKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIKHNY
uniprot
proteins
ec_number
3.1.4.-
uniprot
proteins
ec_number
3.6.1.15
uniprot
proteins
function
FUNCTION: Cyclic-nucleotide phosphodiesterase that acts as a negative regulator of innate immunity by mediating degradation of 2',3'-cGAMP, thereby inhibiting the cGAS-STING signaling (PubMed:37890481). Specifically linearizes 2',3'-cGAMP into 2'5'-bond pGpA and further hydrolyzes pGpA to produce GpA (PubMed:37890481). Also has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP (PubMed:25288789, PubMed:26783088). Has in vitro activity with p-nitrophenyl-TMP (PubMed:25288789). Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates (PubMed:25288789, PubMed:26783088, PubMed:28104755). Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine (PubMed:26783088). Does not have sphingomyelin phosphodiesterase activity (PubMed:25288789, PubMed:26783088). {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:26783088, ECO:0000269|PubMed:28104755, ECO:0000269|PubMed:37890481}.
uniprot
proteins
mass_dalton
51260
uniprot
proteins
mutagenesis
MUTAGEN 69; /note="N->Q: Impaired protein maturation and secretion."; /evidence="ECO:0000269|PubMed:28104755"; MUTAGEN 112..113; /note="PP->LL: Abolished ability to hydrolyze 2',3'-cGAMP."; /evidence="ECO:0000269|PubMed:37890481"; MUTAGEN 114; /note="H->Q: Decreased but not abolished ability to hydrolyze 2',3'-cGAMP."; /evidence="ECO:0000269|PubMed:37890481"; MUTAGEN 222; /note="N->Q: Impaired protein maturation and secretion."; /evidence="ECO:0000269|PubMed:28104755"; MUTAGEN 356; /note="N->Q: Increased degradation by the proteasome and decreased phosphodiesterase activity."; /evidence="ECO:0000269|PubMed:28104755"; MUTAGEN 359..362; /note="EANL->DANA: Abolished ability to dimerize and hydrolyze 2',3'-cGAMP."; /evidence="ECO:0000269|PubMed:37890481
uniprot
proteins
post_translational_modification
PTM: N-glycosylation is required for protein maturation, secretion and phosphodiesterase activity. {ECO:0000269|PubMed:28104755}.
uniprot
proteins
protein_family
Acid sphingomyelinase family
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
25288789
uniprot
proteins
pubmed
26783088
uniprot
proteins
pubmed
28104755
uniprot
proteins
pubmed
37890481
uniprot
proteins
sequence_length
453
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:28104755, ECO:0000269|PubMed:37890481}.
uniprot
proteins