ID   ACER1_HUMAN             Reviewed;         264 AA.
AC   Q8TDN7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-JAN-2012, entry version 66.
DE   RecName: Full=Alkaline ceramidase 1;
DE            Short=AlkCDase 1;
DE            Short=Alkaline CDase 1;
DE            EC=3.5.1.23;
DE   AltName: Full=Acylsphingosine deacylase 3;
DE   AltName: Full=N-acylsphingosine amidohydrolase 3;
GN   Name=ACER1; Synonyms=ASAH3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22791695; PubMed=12783875; DOI=10.1074/jbc.M303875200;
RA   Mao C., Xu R., Szulc Z.M., Bielawski J., Becker K.P., Bielawska A.,
RA   Galadari S.H., Hu W., Obeid L.M.;
RT   "Cloning and characterization of a mouse endoplasmic reticulum
RT   alkaline ceramidase: an enzyme that preferentially regulates
RT   metabolism of very long chain ceramides.";
RL   J. Biol. Chem. 278:31184-31191(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16477081; DOI=10.1194/jlr.M600001-JLR200;
RA   Houben E., Holleran W.M., Yaginuma T., Mao C., Obeid L.M., Rogiers V.,
RA   Takagi Y., Elias P.M., Uchida Y.;
RT   "Differentiation-associated expression of ceramidase isoforms in
RT   cultured keratinocytes and epidermis.";
RL   J. Lipid Res. 47:1063-1070(2006).
CC   -!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine
CC       and free fatty acid at an optimal pH of 8.0. Has a highly
CC       restricted substrate specificity for the natural stereoisomer of
CC       ceramide with D-erythro-sphingosine but not D-ribo-
CC       phytosphingosine or D-erythro-dihydrosphingosine as a backbone.
CC       May have a role in regulating the levels of bioactive lipids
CC       ceramide and sphingosine 1-phosphate, as well as complex
CC       sphingolipids (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-acylsphingosine + H(2)O = a carboxylate +
CC       sphingosine.
CC   -!- ENZYME REGULATION: Inhibited by sphingosine (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in epidermis.
CC   -!- SIMILARITY: Belongs to the alkaline ceramidase family.
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DR   EMBL; AF347024; AAL83822.1; -; mRNA.
DR   EMBL; BC112122; AAI12123.1; -; mRNA.
DR   EMBL; BC112124; AAI12125.1; -; mRNA.
DR   IPI; IPI00152570; -.
DR   RefSeq; NP_597999.1; NM_133492.2.
DR   UniGene; Hs.352609; -.
DR   ProteinModelPortal; Q8TDN7; -.
DR   STRING; Q8TDN7; -.
DR   DMDM; 74715919; -.
DR   Ensembl; ENST00000301452; ENSP00000301452; ENSG00000167769.
DR   GeneID; 125981; -.
DR   KEGG; hsa:125981; -.
DR   UCSC; uc002mel.1; human.
DR   CTD; 125981; -.
DR   GeneCards; GC19M006261; -.
DR   H-InvDB; HIX0039998; -.
DR   HGNC; HGNC:18356; ACER1.
DR   HPA; HPA042506; -.
DR   MIM; 613491; gene.
DR   neXtProt; NX_Q8TDN7; -.
DR   PharmGKB; PA134897634; -.
DR   PharmGKB; PA164714838; -.
DR   eggNOG; prNOG04896; -.
DR   GeneTree; ENSGT00390000004916; -.
DR   HOGENOM; HBG446871; -.
DR   InParanoid; Q8TDN7; -.
DR   OMA; FQYSELV; -.
DR   OrthoDB; EOG4XD3RW; -.
DR   PhylomeDB; Q8TDN7; -.
DR   Reactome; REACT_22258; Metabolism of lipids and lipoproteins.
DR   NextBio; 81606; -.
DR   ArrayExpress; Q8TDN7; -.
DR   Bgee; Q8TDN7; -.
DR   CleanEx; HS_ACER1; -.
DR   Genevestigator; Q8TDN7; -.
DR   GermOnline; ENSG00000167769; Homo sapiens.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017040; F:ceramidase activity; IEA:EC.
DR   InterPro; IPR008901; Ceramidase.
DR   KO; K01441; -.
DR   Pfam; PF05875; Ceramidase; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; Hydrolase; Lipid metabolism;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    264       Alkaline ceramidase 1.
FT                                /FTId=PRO_0000247745.
FT   TOPO_DOM      1     27       Lumenal (Potential).
FT   TRANSMEM     28     48       Helical; (Potential).
FT   TOPO_DOM     49     57       Cytoplasmic (Potential).
FT   TRANSMEM     58     78       Helical; (Potential).
FT   TOPO_DOM     79     81       Lumenal (Potential).
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TOPO_DOM    103    119       Cytoplasmic (Potential).
FT   TRANSMEM    120    137       Helical; (Potential).
FT   TOPO_DOM    138    138       Lumenal (Potential).
FT   TRANSMEM    139    159       Helical; (Potential).
FT   TOPO_DOM    160    176       Cytoplasmic (Potential).
FT   TRANSMEM    177    197       Helical; (Potential).
FT   TOPO_DOM    198    206       Lumenal (Potential).
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TOPO_DOM    228    264       Cytoplasmic (Potential).
SQ   SEQUENCE   264 AA;  31095 MW;  E16E5DB81D064F60 CRC64;
     MPSIFAYQSS EVDWCESNFQ YSELVAEFYN TFSNIPFFIF GPLMMLLMHP YAQKRSRYIY
     VVWVLFMIIG LFSMYFHMTL SFLGQLLDEI AILWLLGSGY SIWMPRCYFP SFLGGNRSQF
     IRLVFITTVV STLLSFLRPT VNAYALNSIA LHILYIVCQE YRKTSNKELR HLIEVSVVLW
     AVALTSWISD RLLCSFWQRI HFFYLHSIWH VLISITFPYG MVTMALVDAN YEMPGETLKV
     RYWPRDSWPV GLPYVEIRGD DKDC
//