Asah2
entrez
54447
canonical
uniprot
Q9JHE3
canonical
ensembl
ENSMUSG00000024887
resolver
ensp
ENSMUSP00000093830
resolver
ensp
ENSMUSP00000157424
resolver
ensp
ENSMUSP00000157744
resolver
ensp
ENSMUSP00000158185
resolver
enst
ENSMUST00000096119
resolver
enst
ENSMUST00000236030
resolver
enst
ENSMUST00000236504
resolver
enst
ENSMUST00000237104
resolver
genesymbol
Asah2
resolver
uniprot
B9EHG7
resolver
uniprot
Q3UWP9
resolver
uniprot
Q8BNP0
resolver
uniprot
Q8BQN7
resolver
uniprot
Q8R236
resolver
uniprot_entry
ASAH2_MOUSE
resolver
uniprot_entry
B9EHG7_MOUSE
resolver
uniprot_sec
Q3UWP9
resolver
uniprot_sec
Q8BNP0
resolver
uniprot_sec
Q8BQN7
resolver
uniprot_sec
Q8R236
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by D-erythro-MAPP. {ECO:0000269|PubMed:14557071}.
uniprot
proteins
amino_acid_sequence
MAKRTFSTLEAFLIFLLVIMTVITVALLTLLFVTSGTIENHKDSGNHWFSTTLGSTTTQPPPITQTPNFPSFRNFSGYYIGVGRADCTGQVSDINLMGYGKNGQNARGLLTRLFSRAFILADPDGSNRMAFVSVELCMISQRLRLEVLKRLESKYGSLYRRDNVILSAIHTHSGPAGFFQYTLYILASEGFSNRTFQYIVSGIMKSIDIAHTNLKPGKIFINKGNVANVQINRSPSSYLLNPQSERARYSSNTDKEMLVLKLVDLNGEDLGLISWFAIHPVSMNNSNHFVNSDNMGYAAYLFEQEKNKGYLPGQGPFVAGFASSNLGDVSPNILGPHCVNTGESCDNDKSTCPNGGPSMCMASGPGQDMFESTHIIGRIIYQKAKELYASASQEVTGPVLAAHQWVNMTDVSVQLNATHTVKTCKPALGYSFAAGTIDGVSGLNITQGTTEGDPFWDTLRDQLLGKPSEEIVECQKPKPILLHSGELTIPHPWQPDIVDVQIVTVGSLAIAAIPGELTTMSGRRFREAIKKEFALYGMKDMTVVIAGLSNVYTHYITTYEEYQAQRYEAASTIYGPHTLSAYIQLFRDLAKAIATDTVANMSSGPEPPFFKNLIASLIPNIADRAPIGKHFGDVLQPAKPEYRVGEVVEVIFVGANPKNSAENQTHQTFLTVEKYEDSVADWQIMYNDASWETRFYWHKGILGLSNATIYWHIPDTAYPGIYRIRYFGHNRKQELLKPAVILAFEGISSPFEVVTT
uniprot
proteins
ec_number
3.5.1.-
uniprot
proteins
ec_number
3.5.1.23
uniprot
proteins
function
FUNCTION: Plasma membrane ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at neutral pH (PubMed:10652340, PubMed:10753931, PubMed:16380386). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed:14557071). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:10652340, PubMed:21613224). Together with sphingomyelinase, participates in the production of sphingosine and sphingosine-1-phosphate from the degradation of sphingomyelin, a sphingolipid enriched in the plasma membrane of cells (PubMed:16126722). Also participates in the hydrolysis of ceramides from the extracellular milieu allowing the production of sphingosine-1-phosphate inside and outside cells (PubMed:16126722). This is the case for instance with the digestion of dietary sphingolipids in the intestinal tract (PubMed:16380386). {ECO:0000269|PubMed:10652340, ECO:0000269|PubMed:10753931, ECO:0000269|PubMed:14557071, ECO:0000269|PubMed:16126722, ECO:0000269|PubMed:16380386, ECO:0000269|PubMed:21613224}.
uniprot
proteins
mass_dalton
83509
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:16380386, ECO:0000269|PubMed:21613224}.
uniprot
proteins
post_translational_modification
PTM: Proteolytic cleavage of the N-terminus removes the signal-anchor and produces a soluble form of the protein. {ECO:0000250|UniProtKB:Q91XT9}.; PTM: N-glycosylated. Required for enzyme activity. {ECO:0000269|PubMed:10652340, ECO:0000269|PubMed:10753931}.; PTM: O-glycosylated. Required to retain it as a type II membrane protein at the cell surface. {ECO:0000250|UniProtKB:Q9NR71}.; PTM: Phosphorylated. May prevent ubiquitination and subsequent degradation. {ECO:0000250|UniProtKB:Q91XT9}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxide. {ECO:0000250|UniProtKB:Q91XT9}.
uniprot
proteins
protein_family
Neutral ceramidase family
uniprot
proteins
pubmed
10652340
uniprot
proteins
pubmed
10753931
uniprot
proteins
pubmed
11591392
uniprot
proteins
pubmed
12921776
uniprot
proteins
pubmed
14557071
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16126722
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16380386
uniprot
proteins
pubmed
21613224
uniprot
proteins
sequence_length
756
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Neutral ceramidase]: Cell membrane {ECO:0000269|PubMed:11591392, ECO:0000269|PubMed:12921776, ECO:0000269|PubMed:16126722}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Membrane raft {ECO:0000269|PubMed:12921776}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Membrane, caveola {ECO:0000269|PubMed:12921776}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NR71}; Single-pass type II membrane protein {ECO:0000269|PubMed:16126722}. Mitochondrion {ECO:0000269|PubMed:21613224}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9NR71}. Note=Enriched in exosomes upon stimulation by cytokine (By similarity). Enriched in caveolae and lipid rafts (PubMed:12921776). {ECO:0000250|UniProtKB:Q9NR71, ECO:0000269|PubMed:12921776}.; SUBCELLULAR LOCATION: [Neutral ceramidase soluble form]: Secreted {ECO:0000269|PubMed:16126722}.
uniprot
proteins
transmembrane_region
TRANSMEM 12..32; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins