ID   ASAH1_MOUSE             Reviewed;         394 AA.
AC   Q9WV54;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Acid ceramidase {ECO:0000305};
DE            Short=AC;
DE            Short=ACDase;
DE            Short=Acid CDase;
DE            EC=3.5.1.23 {ECO:0000269|PubMed:9653654};
DE   AltName: Full=Acylsphingosine deacylase;
DE   AltName: Full=N-acylethanolamine hydrolase ASAH1 {ECO:0000250|UniProtKB:Q13510};
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13510};
DE   AltName: Full=N-acylsphingosine amidohydrolase;
DE   Contains:
DE     RecName: Full=Acid ceramidase subunit alpha {ECO:0000250|UniProtKB:Q13510};
DE   Contains:
DE     RecName: Full=Acid ceramidase subunit beta {ECO:0000250|UniProtKB:Q13510};
DE   Flags: Precursor;
GN   Name=Asah1 {ECO:0000312|MGI:MGI:1277124}; Synonyms=Asah;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=9653654; DOI=10.1006/geno.1998.5334;
RA   Li C.-M., Hong S.-B., Kopal G., He X., Linke T., Hou W.-S., Koch J.,
RA   Gatt S., Sandhoff K., Schuchman E.H.;
RT   "Cloning and characterization of the full-length cDNA and genomic sequences
RT   encoding murine acid ceramidase.";
RL   Genomics 50:267-274(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=10974027; DOI=10.1084/jem.192.5.601;
RA   Strelow A., Bernardo K., Adam-Klages S., Linke T., Sandhoff K., Kroenke M.,
RA   Adam D.;
RT   "Overexpression of acid ceramidase protects from tumor necrosis factor-
RT   induced cell death.";
RL   J. Exp. Med. 192:601-612(2000).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11829492; DOI=10.1006/geno.2002.6686;
RA   Li C.M., Park J.H., Simonaro C.M., He X., Gordon R.E., Friedman A.H.,
RA   Ehleiter D., Paris F., Manova K., Hepbildikler S., Fuks Z., Sandhoff K.,
RA   Kolesnick R., Schuchman E.H., Hepbiloikler S.;
RT   "Insertional mutagenesis of the mouse acid ceramidase gene leads to early
RT   embryonic lethality in homozygotes and progressive lipid storage disease in
RT   heterozygotes.";
RL   Genomics 79:218-224(2002).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=23770692; DOI=10.1038/nm.3214;
RA   Gulbins E., Palmada M., Reichel M., Lueth A., Boehmer C., Amato D.,
RA   Mueller C.P., Tischbirek C.H., Groemer T.W., Tabatabai G., Becker K.A.,
RA   Tripal P., Staedtler S., Ackermann T.F., van Brederode J., Alzheimer C.,
RA   Weller M., Lang U.E., Kleuser B., Grassme H., Kornhuber J.;
RT   "Acid sphingomyelinase-ceramide system mediates effects of antidepressant
RT   drugs.";
RL   Nat. Med. 19:934-938(2013).
CC   -!- FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides
CC       into sphingosine and free fatty acids at acidic pH (PubMed:9653654,
CC       PubMed:11829492). Ceramides, sphingosine, and its phosphorylated form
CC       sphingosine-1-phosphate are bioactive lipids that mediate cellular
CC       signaling pathways regulating several biological processes including
CC       cell proliferation, apoptosis and differentiation (PubMed:9653654). Has
CC       a higher catalytic efficiency towards C12-ceramides versus other
CC       ceramides (By similarity). Also catalyzes the reverse reaction allowing
CC       the synthesis of ceramides from fatty acids and sphingosine (By
CC       similarity). For the reverse synthetic reaction, the natural
CC       sphingosine D-erythro isomer is more efficiently utilized as a
CC       substrate compared to D-erythro-dihydrosphingosine and D-erythro-
CC       phytosphingosine, while the fatty acids with chain lengths of 12 or 14
CC       carbons are the most efficiently used (By similarity). Has also an N-
CC       acylethanolamine hydrolase activity (By similarity). By regulating the
CC       levels of ceramides, sphingosine and sphingosine-1-phosphate in the
CC       epidermis, mediates the calcium-induced differentiation of epidermal
CC       keratinocytes (By similarity). Also indirectly regulates tumor necrosis
CC       factor/TNF-induced apoptosis (PubMed:10974027). By regulating the
CC       intracellular balance between ceramides and sphingosine, in
CC       adrenocortical cells, probably also acts as a regulator of
CC       steroidogenesis (By similarity). {ECO:0000250|UniProtKB:Q13510,
CC       ECO:0000269|PubMed:10974027, ECO:0000269|PubMed:11829492,
CC       ECO:0000269|PubMed:9653654, ECO:0000303|PubMed:9653654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine;
CC         Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23;
CC         Evidence={ECO:0000269|PubMed:9653654};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-
CC         enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:72956;
CC         Evidence={ECO:0000269|PubMed:9653654};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41293;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate
CC         + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996;
CC         Evidence={ECO:0000269|PubMed:9653654};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine +
CC         tetradecanoate; Xref=Rhea:RHEA:41287, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57756, ChEBI:CHEBI:72957;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41289;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-
CC         enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:72959;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38893;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-
CC         enine; Xref=Rhea:RHEA:41279, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:72961;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41280;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41281;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-dodecanoyl-(4R)-hydroxysphinganine = (4R)-
CC         hydroxysphinganine + dodecanoate; Xref=Rhea:RHEA:41303,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:64124,
CC         ChEBI:CHEBI:78001; Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41305;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(dodecanoyl)-sphinganine = dodecanoate + sphinganine;
CC         Xref=Rhea:RHEA:45448, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC         ChEBI:CHEBI:57817, ChEBI:CHEBI:85261;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45450;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(acetyl)-sphing-4-enine = acetate + sphing-4-enine;
CC         Xref=Rhea:RHEA:58484, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:46979, ChEBI:CHEBI:57756;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58485;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine;
CC         Xref=Rhea:RHEA:41295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:63867;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41296;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-octanoylsphing-4-enine = octanoate + sphing-4-enine;
CC         Xref=Rhea:RHEA:45092, ChEBI:CHEBI:15377, ChEBI:CHEBI:25646,
CC         ChEBI:CHEBI:45815, ChEBI:CHEBI:57756;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45093;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine;
CC         Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262,
CC         ChEBI:CHEBI:57603, ChEBI:CHEBI:85263;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457;
CC         Evidence={ECO:0000250|UniProtKB:Q13510};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000269|PubMed:9653654}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. The heterodimer is composed of
CC       the disulfide-linked alpha and beta chains produced by autocatalytic
CC       cleavage of the precursor. {ECO:0000250|UniProtKB:Q13510}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted
CC       {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and
CC       localization to lysosomes is mannose-6-phosphate receptor-dependent.
CC       {ECO:0000250|UniProtKB:Q13510}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9653654}.
CC   -!- DEVELOPMENTAL STAGE: Expression is detected from 7 dpc to 17 dpc,
CC       during fetal development. {ECO:0000269|PubMed:23770692}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13510}.
CC   -!- PTM: Proteolytically cleaved into two chains alpha and beta that remain
CC       associated via a disulfide bond. Cleavage gives rise to a conformation
CC       change that activates the enzyme. The same catalytic Cys residue
CC       mediates the autoproteolytic cleavage and subsequent hydrolysis of
CC       lipid substrates. The beta chain may undergo an additional C-terminal
CC       processing. {ECO:0000250|UniProtKB:Q13510}.
CC   -!- DISRUPTION PHENOTYPE: Lethal for homozygous knockout embryos
CC       (PubMed:11829492). Heterozygous knockout mice are viable, grow normally
CC       and do not present overt clinical phenotype (PubMed:11829492). However,
CC       they progressively develop lipid storage-associated phenotypes, with an
CC       elevation of ceramides levels and an accumulation of lipid-laden
CC       inclusions in liver, more specifically in Kupffer cells, and other
CC       tissues (PubMed:11829492). Associated with the accumulation of
CC       ceramides, a depression-like phenotype is observed for heterozygous
CC       knockout mice (PubMed:23770692). {ECO:0000269|PubMed:11829492,
CC       ECO:0000269|PubMed:23770692}.
CC   -!- SIMILARITY: Belongs to the acid ceramidase family. {ECO:0000305}.
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DR   EMBL; AF157500; AAD39551.1; -; mRNA.
DR   EMBL; AK075666; BAC35884.1; -; mRNA.
DR   EMBL; BC003204; AAH03204.1; -; mRNA.
DR   CCDS; CCDS22262.1; -.
DR   RefSeq; NP_062708.1; NM_019734.3.
DR   RefSeq; XP_017168016.1; XM_017312527.1.
DR   RefSeq; XP_017168017.1; XM_017312528.1.
DR   RefSeq; XP_017168018.1; XM_017312529.1.
DR   RefSeq; XP_017168019.1; XM_017312530.1.
DR   RefSeq; XP_017168020.1; XM_017312531.1.
DR   RefSeq; XP_017168021.1; XM_017312532.1.
DR   AlphaFoldDB; Q9WV54; -.
DR   SMR; Q9WV54; -.
DR   BioGRID; 198219; 12.
DR   IntAct; Q9WV54; 1.
DR   STRING; 10090.ENSMUSP00000034000; -.
DR   MEROPS; C89.001; -.
DR   GlyConnect; 2101; 8 N-Linked glycans (3 sites).
DR   GlyCosmos; Q9WV54; 5 sites, 8 glycans.
DR   GlyGen; Q9WV54; 6 sites, 8 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WV54; -.
DR   PhosphoSitePlus; Q9WV54; -.
DR   SwissPalm; Q9WV54; -.
DR   EPD; Q9WV54; -.
DR   jPOST; Q9WV54; -.
DR   MaxQB; Q9WV54; -.
DR   PaxDb; 10090-ENSMUSP00000034000; -.
DR   PeptideAtlas; Q9WV54; -.
DR   ProteomicsDB; 277243; -.
DR   Pumba; Q9WV54; -.
DR   Antibodypedia; 1611; 328 antibodies from 31 providers.
DR   DNASU; 11886; -.
DR   Ensembl; ENSMUST00000034000.15; ENSMUSP00000034000.9; ENSMUSG00000031591.15.
DR   GeneID; 11886; -.
DR   KEGG; mmu:11886; -.
DR   UCSC; uc009lnw.2; mouse.
DR   AGR; MGI:1277124; -.
DR   CTD; 427; -.
DR   MGI; MGI:1277124; Asah1.
DR   VEuPathDB; HostDB:ENSMUSG00000031591; -.
DR   eggNOG; ENOG502QVBG; Eukaryota.
DR   GeneTree; ENSGT00530000063548; -.
DR   HOGENOM; CLU_054401_0_0_1; -.
DR   InParanoid; Q9WV54; -.
DR   OMA; GEDCRSK; -.
DR   OrthoDB; 5485766at2759; -.
DR   PhylomeDB; Q9WV54; -.
DR   TreeFam; TF313219; -.
DR   BRENDA; 3.5.1.23; 3474.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9840310; Glycosphingolipid catabolism.
DR   UniPathway; UPA00222; -.
DR   BioGRID-ORCS; 11886; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Asah1; mouse.
DR   PRO; PR:Q9WV54; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9WV54; Protein.
DR   Bgee; ENSMUSG00000031591; Expressed in saccule of membranous labyrinth and 254 other cell types or tissues.
DR   ExpressionAtlas; Q9WV54; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0102121; F:ceramidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017064; F:fatty acid amide hydrolase activity; IEA:InterPro.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISO:MGI.
DR   GO; GO:0017040; F:N-acylsphingosine amidohydrolase activity; IDA:MGI.
DR   GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR   GO; GO:0046513; P:ceramide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0046514; P:ceramide catabolic process; IDA:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0030324; P:lung development; ISO:MGI.
DR   GO; GO:0062098; P:regulation of programmed necrotic cell death; IMP:UniProtKB.
DR   GO; GO:0050810; P:regulation of steroid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IDA:UniProtKB.
DR   CDD; cd01903; Ntn_AC_NAAA; 1.
DR   InterPro; IPR016699; Acid_ceramidase-like.
DR   InterPro; IPR029130; Acid_ceramidase_N.
DR   InterPro; IPR029132; CBAH/NAAA_C.
DR   PANTHER; PTHR28583; ACID AMIDASE; 1.
DR   PANTHER; PTHR28583:SF1; ACID CERAMIDASE; 1.
DR   Pfam; PF02275; CBAH; 1.
DR   Pfam; PF15508; NAAA-beta; 1.
DR   PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
DR   Genevisible; Q9WV54; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid metabolism; Lysosome;
KW   Reference proteome; Secreted; Signal; Sphingolipid metabolism; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..141
FT                   /note="Acid ceramidase subunit alpha"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT                   /id="PRO_0000002316"
FT   CHAIN           142..394
FT                   /note="Acid ceramidase subunit beta"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT                   /id="PRO_0000002317"
FT   ACT_SITE        142
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT   SITE            161
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT   SITE            319
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT   SITE            332
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..339
FT                   /note="Interchain (between alpha and beta subunits)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13510"
FT   DISULFID        387..391
FT                   /evidence="ECO:0000250|UniProtKB:A0A0P6JG37"
SQ   SEQUENCE   394 AA;  44670 MW;  DA7BFBFDC45C9F65 CRC64;
     MRGQSLLTWV LAAAVTCAQA QDVPPWTEDC RKSTYPPSGP TYRGPVPWHT INLDLPPYKR
     WHELLAQKAP ALRILVNSIT SLVNTFVPSG KLMKMVDQKL PGMIGSLPDP FGEEMRGIAD
     VTGIPLGEII SFNIFYELFT MCTSIITEDE KGHLLHGRNM DFGIFLGWNI NNNTWVVTEE
     LKPLTVNLDF QRNNKTVFKA TSFVGYVGML TGFKPGLFSL SLNERFSING GYLGILEWMF
     GRKDAQWVGF ITRSVLENTT SYEEAKNTLT KTKIMAPVYF ILGGKKSGEG CVITRERKES
     LDVYELDPKH GRWYVVQTNY DRWKNTLFID DRRTPAKKCL NHTTQKNLSF ATIYDVLSTK
     PVLNKLTVFT TLMDVTKGQF ESHLRDCPDP CIGW
//