Asah2
entrez
114104
canonical
uniprot
Q91XT9
canonical
ensembl
ENSRNOG00000012196
resolver
ensembl
ENSRNOG00055029490
resolver
ensembl
ENSRNOG00060029443
resolver
ensembl
ENSRNOG00065029336
resolver
ensp
ENSRNOP00000073116
resolver
ensp
ENSRNOP00055042083
resolver
ensp
ENSRNOP00060042530
resolver
ensp
ENSRNOP00065041660
resolver
enst
ENSRNOT00055051085
resolver
enst
ENSRNOT00060051120
resolver
enst
ENSRNOT00065050687
resolver
genesymbol
Asah2
resolver
uniprot_entry
ASAH2_RAT
resolver
activity_regulation
ACTIVITY REGULATION: The reverse reaction is inhibited by Zn(2+) and Cu(2+) (PubMed:11278489). Inhibited by cardiolipin and phosphatidic acid (PubMed:11278489). {ECO:0000269|PubMed:11278489}.
uniprot
proteins
amino_acid_sequence
MAKRTFSSLEAFLIFLLVMMTAITVALLTLLFVTSGTIENHKDSGNHWVSTTQGPTTTQSSPTTQTPTTQTPDLPPSQNFSGYYIGVGRADCTGQVSDINLMGYGKNGQNAQGLLTRLFSRAFILADPDGSNRMAFVSVELCMISQRLRLEVLKRLQSKYGSLYRRDNVILSATHTHSGPAGFFQYTLYILASEGFSNRTFQYIVSGIVKSIDIAHTNLKPGKVLINKGNVANVQINRSPSSYLQNPPSERARYSSDTDKEMVVLKLVDLNGEDLGLISWFAVHPVSMNNSNHLVNSDNMGYAAYLFEQEKNRGYLPGQGPFVAGFASSNLGDVSPNILGPHCVNTGESCDNDKSTCPSGGPSMCMASGPGQDMFESTHIIGRVIYQKAKELHASASQEVTGPVLTAHQWVNMTDVSVQLNATHTVKTCKAALGYSFAAGTIDGVSGLNITQGTTEGNLFWDTLRDQLLGKPSEEIIECQKPKPILIHTGELTKPHPWQPDIVDIQIVTLGSLAIAAIPGEFTTMSGRRLREAVKKEFALYGMKDMTVVIAGLSNVYTHYITTYEEYQAQRYEAASTIYGPHTLSAYIQLFRALAKAIATDTVANMSSGPEPPFFKNLIGSLIPNIADRAPIGKQFGDVLQPAKPEYRVGEVVEVVFVGANPKNSAENQTHQTFLTVEKYEDSVANWQIMHNDASWETRFYWHKGVLGLSNATIHWHIPDTALPGVYRIRYFGHNRKQELLKPAVILAFEGISSPFEIVTT
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:10488143, PubMed:11328816, PubMed:15217782). 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:11328816). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:11278489, PubMed:15123644). 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:15217782). Also participates in the hydrolysis of ceramides from the extracellular milieu allowing the production of sphingosine-1-phosphate inside and outside cells. This is the case for instance with the digestion of dietary sphingolipids in the intestinal tract (By similarity). {ECO:0000250|UniProtKB:Q9JHE3, ECO:0000269|PubMed:10488143, ECO:0000269|PubMed:11278489, ECO:0000269|PubMed:11328816, ECO:0000269|PubMed:15123644, ECO:0000269|PubMed:15217782, ECO:0000303|PubMed:11328816}.
uniprot
proteins
mass_dalton
83488
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="S->A: Abolishes O-glycosylation and localization at the cell surface; when associated with A-50; A-51; A-52; A-56; A-57; A-58; A-60; A-61; A-62; A-63; A-65; A-76; A-68; A-69; A-71 and A-77."; /evidence="ECO:0000269|PubMed:12499379"; MUTAGEN 50..71; /note="STTQGPTTTQSSPTTQTPTTQT->AAAQGPAAAQAAPAAQAPAAQA: Abolishes O-glycosylation and localization at the cell surface; when associated with A-44 and A-77."; /evidence="ECO:0000269|PubMed:12499379"; MUTAGEN 77; /note="S->A: Abolishes O-glycosylation and localization at the cell surface; when associated with A-44; A-50; A-51; A-52; A-56; A-57; A-58; A-60; A-61; A-62; A-63; A-65; A-76; A-68; A-69 and A-71."; /evidence="ECO:0000269|PubMed:12499379"; MUTAGEN 756; /note="F->I: No effect."; /evidence="ECO:0000269|PubMed:15123644"; MUTAGEN 756; /note="F->R,D: Loss of function."; /evidence="ECO:0000269|PubMed:15123644"; MUTAGEN 757; /note="E->R: No effect."; /evidence="ECO:0000269|PubMed:15123644"; MUTAGEN 758; /note="I->F: Impairs enzyme activity."; /evidence="ECO:0000269|PubMed:15123644"; MUTAGEN 758; /note="I->R,D: Loss of function."; /evidence="ECO:0000269|PubMed:15123644"; MUTAGEN 758; /note="I->V: No effect."; /evidence="ECO:0000269|PubMed:15123644
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:15217782}.
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:0000269|PubMed:12499379}.; PTM: N-glycosylated (PubMed:11328816, PubMed:15123644). Required for enzyme activity (PubMed:11328816). {ECO:0000269|PubMed:11328816, ECO:0000269|PubMed:15123644}.; PTM: O-glycosylated (PubMed:12499379). Required to retain it as a type II membrane protein at the cell surface (PubMed:12499379). {ECO:0000269|PubMed:12499379}.; PTM: Phosphorylated. May prevent ubiquitination and subsequent degradation. {ECO:0000269|PubMed:12359735, ECO:0000269|PubMed:12482609}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is triggered by nitric oxide. {ECO:0000269|PubMed:12482609}.
uniprot
proteins
protein_family
Neutral ceramidase family
uniprot
proteins
pubmed
10488143
uniprot
proteins
pubmed
10781606
uniprot
proteins
pubmed
11278489
uniprot
proteins
pubmed
11328816
uniprot
proteins
pubmed
11330410
uniprot
proteins
pubmed
11457826
uniprot
proteins
pubmed
12359735
uniprot
proteins
pubmed
12482609
uniprot
proteins
pubmed
12499379
uniprot
proteins
pubmed
15123644
uniprot
proteins
pubmed
15217782
uniprot
proteins
pubmed
21613224
uniprot
proteins
sequence_length
761
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Neutral ceramidase]: Cell membrane {ECO:0000269|PubMed:11328816, ECO:0000269|PubMed:12499379, ECO:0000269|PubMed:15123644}; Single-pass type II membrane protein {ECO:0000269|PubMed:12499379}. Membrane raft {ECO:0000269|PubMed:11328816}; Single-pass type II membrane protein {ECO:0000269|PubMed:12499379}. Membrane, caveola {ECO:0000250|UniProtKB:Q9JHE3}; Single-pass type II membrane protein {ECO:0000269|PubMed:12499379}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NR71}; Single-pass type II membrane protein {ECO:0000269|PubMed:12499379}. 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 (By similarity). The localization to the mitochondrion could not be confirmed (By similarity). {ECO:0000250|UniProtKB:Q9JHE3, ECO:0000250|UniProtKB:Q9NR71}.; SUBCELLULAR LOCATION: [Neutral ceramidase soluble form]: Secreted {ECO:0000269|PubMed:12499379, ECO:0000269|PubMed:15123644}.
uniprot
proteins
transmembrane_region
TRANSMEM 12..32; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins