ASAH1_MOUSE
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 03-AUG-2022, entry version 157.
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, Spleen,
RC 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 GlyGen; Q9WV54; 5 sites, 8 N-linked glycans (3 sites).
DR iPTMnet; Q9WV54; -.
DR PhosphoSitePlus; Q9WV54; -.
DR SwissPalm; Q9WV54; -.
DR EPD; Q9WV54; -.
DR jPOST; Q9WV54; -.
DR MaxQB; Q9WV54; -.
DR PaxDb; Q9WV54; -.
DR PeptideAtlas; Q9WV54; -.
DR PRIDE; Q9WV54; -.
DR ProteomicsDB; 277243; -.
DR Antibodypedia; 1611; 310 antibodies from 31 providers.
DR DNASU; 11886; -.
DR Ensembl; ENSMUST00000034000; ENSMUSP00000034000; ENSMUSG00000031591.
DR GeneID; 11886; -.
DR KEGG; mmu:11886; -.
DR UCSC; uc009lnw.2; mouse.
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; RWKNPLF; -.
DR OrthoDB; 745108at2759; -.
DR PhylomeDB; Q9WV54; -.
DR TreeFam; TF313219; -.
DR BRENDA; 3.5.1.23; 3474.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 11886; 3 hits in 75 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 251 other tissues.
DR ExpressionAtlas; Q9WV54; baseline and differential.
DR Genevisible; Q9WV54; MM.
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:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IBA:GO_Central.
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:1903507; P:negative regulation of nucleic acid-templated transcription; 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 InterPro; IPR016699; Acid_ceramidase-like.
DR InterPro; IPR029130; Acid_ceramidase_N.
DR InterPro; IPR029132; CBAH/NAAA_C.
DR Pfam; PF02275; CBAH; 1.
DR Pfam; PF15508; NAAA-beta; 1.
DR PIRSF; PIRSF017632; Acid_ceramidase-like; 1.
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
