Smpd3
entrez
58994
canonical
uniprot
Q9JJY3
canonical
ensembl
ENSMUSG00000031906
resolver
ensp
ENSMUSP00000069255
resolver
ensp
ENSMUSP00000148282
resolver
ensp
ENSMUSP00000188100
resolver
enst
ENSMUST00000067512
resolver
enst
ENSMUST00000212896
resolver
genesymbol
Smpd3
resolver
uniprot
Q3UTQ5
resolver
uniprot_entry
NSMA2_MOUSE
resolver
uniprot_sec
Q3UTQ5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by nSMase inhibitor GW4869. Binding of anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) increases enzymatic activity (PubMed:21550973). {ECO:0000269|PubMed:12566438, ECO:0000269|PubMed:21550973}.
uniprot
proteins
amino_acid_sequence
MVLYTTPFPNSCLSALHAVSWALIFPCYWLVDRLLASFIPTTYEKRQRADDPCCLQLFCTVLFTPVYLALLVAALPFAFLGFIFWSPLQSARRPYSYSRLEDKNPAGGAALLSEWKGTGAGKSFCFATANVCLLPDSLARLNNVFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSISAASFSSLVSPQGGDGSRAVPGSIKRTASVEYKGDGGRHPSDEAANGPASGEQADGSLEDSCIVRIGGEEGGRPQEADDPAAGSQARNGAGGTPKGQTPNHNQRDGDSGSLGSPSASRESLVKARAGQDSGGSGEPGANSKLLYKTSVVKKAAARRRRHPDEAFDHEVSAFFPANLDFLCLQEVFDKRAAAKLKEQLHGYFEYILYDVGVYGCHGCCNFKCLNSGLFFASRYPVMDVAYHCYPNGCSFDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPPEDSAVRCEQLDLLQDWLADFRKSTSSTSTANPEELVVFDVICGDLNFDNCSSDDKLEQQHSLFTRYKDPCRLGPGEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSPGAGQKGRKDLLKGNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSAGEEEA
uniprot
proteins
ec_number
3.1.4.12
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization (PubMed:15051724, PubMed:15764706, PubMed:15929065, PubMed:16025116). Binds to anionic phospholipids (APLs) such as phosphatidylserine (PS) and phosphatidic acid (PA) that modulate enzymatic activity and subcellular location (PubMed:21550973). May be involved in IL-1-beta-induced JNK activation in hepatocytes (By similarity). May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF-kappa-B activation under inflammatory conditions (By similarity). {ECO:0000250|UniProtKB:O35049, ECO:0000269|PubMed:15051724, ECO:0000269|PubMed:15764706, ECO:0000269|PubMed:15929065, ECO:0000269|PubMed:16025116, ECO:0000269|PubMed:21550973}.
uniprot
proteins
mass_dalton
71197
uniprot
proteins
mutagenesis
MUTAGEN 33; /note="R->A: Strongly decreases binding with phosphatidic acid and phosphatidylserine. Abolishes binding with phosphatidic acid and phosphatidylserine; when associated with 45-DEL-48. Strongly decreases sphingomyelin phosphodiesterase activity; when associated with 45-DEL-48. Abolishes sphingomyelin phosphodiesterase activity and locates at endoplasmic reticulum; when associated with 45-DEL-48 and 92-A-A-93."; /evidence="ECO:0000269|PubMed:21550973"; MUTAGEN 45..48; /note="Missing: Strongly decreases binding with phosphatidic acid and phosphatidylserine. Abolishes binding with phosphatidic acid and phosphatidylserine; when associated with A-33. Strongly decreases sphingomyelin phosphodiesterase activity; when associated with A-33. Abolishes sphingomyelin phosphodiesterase activity and locates at endoplasmic reticulum; when associated with A-33 and 92-A-A-93."; /evidence="ECO:0000269|PubMed:21550973"; MUTAGEN 92..93; /note="RR->AA: Abolishes binding with phosphatidic acid. No effect on cell membrane location. Strongly decreases sphingomyelin phosphodiesterase activity. Abolishes sphingomyelin phosphodiesterase activity and locates at endoplasmic reticulum; when associated with A-33 and 45-DEL-48."; /evidence="ECO:0000269|PubMed:21550973"; MUTAGEN 92; /note="R->A: Strongly decreases binding with phosphatidic acid."; /evidence="ECO:0000269|PubMed:21550973"; MUTAGEN 93; /note="R->A: Strongly decreases binding with phosphatidic acid."; /evidence="ECO:0000269|PubMed:21550973"; MUTAGEN 99; /note="R->A: No effect on binding with phosphatidic acid."; /evidence="ECO:0000269|PubMed:21550973
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:15051724}.
uniprot
proteins
post_translational_modification
PTM: Palmitoylated, palmitoylation-deficient proteins are targeted for lysosomal degradation. {ECO:0000269|PubMed:17272284}.
uniprot
proteins
protein_family
Neutral sphingomyelinase family
uniprot
proteins
pubmed
10823942
uniprot
proteins
pubmed
12566438
uniprot
proteins
pubmed
15051724
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15764706
uniprot
proteins
pubmed
15929065
uniprot
proteins
pubmed
16025116
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17272284
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21550973
uniprot
proteins
sequence_length
655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15764706}; Lipid-anchor {ECO:0000269|PubMed:15764706}. Cell membrane {ECO:0000269|PubMed:17272284, ECO:0000269|PubMed:21550973}; Lipid-anchor {ECO:0000269|PubMed:17272284}. Note=May localize to detergent-resistant subdomains of Golgi membranes of hypothalamic neurosecretory neurons (PubMed:15764706).
uniprot
proteins