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Alkaline ceramidase 1 (AlkCDase 1) (Alkaline CDase 1) (EC 3.5.1.23) (Acylsphingosine deacylase 3) (N-acylsphingosine amidohydrolase 3)

 ACER1_HUMAN             Reviewed;         264 AA.
Q8TDN7;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
27-SEP-2017, entry version 108.
RecName: Full=Alkaline ceramidase 1;
Short=AlkCDase 1;
Short=Alkaline CDase 1;
EC=3.5.1.23;
AltName: Full=Acylsphingosine deacylase 3;
AltName: Full=N-acylsphingosine amidohydrolase 3;
Name=ACER1; Synonyms=ASAH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12783875; DOI=10.1074/jbc.M303875200;
Mao C., Xu R., Szulc Z.M., Bielawski J., Becker K.P., Bielawska A.,
Galadari S.H., Hu W., Obeid L.M.;
"Cloning and characterization of a mouse endoplasmic reticulum
alkaline ceramidase: an enzyme that preferentially regulates
metabolism of very long chain ceramides.";
J. Biol. Chem. 278:31184-31191(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY.
PubMed=16477081; DOI=10.1194/jlr.M600001-JLR200;
Houben E., Holleran W.M., Yaginuma T., Mao C., Obeid L.M., Rogiers V.,
Takagi Y., Elias P.M., Uchida Y.;
"Differentiation-associated expression of ceramidase isoforms in
cultured keratinocytes and epidermis.";
J. Lipid Res. 47:1063-1070(2006).
-!- FUNCTION: Hydrolyzes the sphingolipid ceramide into sphingosine
and free fatty acid at an optimal pH of 8.0. Has a highly
restricted substrate specificity for the natural stereoisomer of
ceramide with D-erythro-sphingosine but not D-ribo-
phytosphingosine or D-erythro-dihydrosphingosine as a backbone.
May have a role in regulating the levels of bioactive lipids
ceramide and sphingosine 1-phosphate, as well as complex
sphingolipids (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: N-acylsphingosine + H(2)O = a carboxylate +
sphingosine.
-!- ENZYME REGULATION: Inhibited by sphingosine. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Mainly expressed in epidermis.
{ECO:0000269|PubMed:16477081}.
-!- SIMILARITY: Belongs to the alkaline ceramidase family.
{ECO:0000305}.
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EMBL; AF347024; AAL83822.1; -; mRNA.
EMBL; BC112122; AAI12123.1; -; mRNA.
EMBL; BC112124; AAI12125.1; -; mRNA.
CCDS; CCDS12161.1; -.
RefSeq; NP_597999.1; NM_133492.2.
UniGene; Hs.352609; -.
ProteinModelPortal; Q8TDN7; -.
IntAct; Q8TDN7; 1.
STRING; 9606.ENSP00000301452; -.
ChEMBL; CHEMBL3351194; -.
SwissLipids; SLP:000000165; -.
BioMuta; ACER1; -.
DMDM; 74715919; -.
PaxDb; Q8TDN7; -.
PeptideAtlas; Q8TDN7; -.
PRIDE; Q8TDN7; -.
Ensembl; ENST00000301452; ENSP00000301452; ENSG00000167769.
GeneID; 125981; -.
KEGG; hsa:125981; -.
UCSC; uc002mel.3; human.
CTD; 125981; -.
EuPathDB; HostDB:ENSG00000167769.4; -.
GeneCards; ACER1; -.
HGNC; HGNC:18356; ACER1.
MIM; 613491; gene.
neXtProt; NX_Q8TDN7; -.
OpenTargets; ENSG00000167769; -.
PharmGKB; PA164714838; -.
eggNOG; KOG2329; Eukaryota.
eggNOG; ENOG4111RPN; LUCA.
GeneTree; ENSGT00730000110920; -.
HOGENOM; HOG000220878; -.
InParanoid; Q8TDN7; -.
KO; K01441; -.
OMA; SGYSIWM; -.
OrthoDB; EOG091G0HT1; -.
PhylomeDB; Q8TDN7; -.
TreeFam; TF313019; -.
BRENDA; 3.5.1.23; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
ChiTaRS; ACER1; human.
GeneWiki; ACER1; -.
GenomeRNAi; 125981; -.
PRO; PR:Q8TDN7; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167769; -.
CleanEx; HS_ACER1; -.
Genevisible; Q8TDN7; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0017040; F:ceramidase activity; IDA:BHF-UCL.
GO; GO:0071633; F:dihydroceramidase activity; IDA:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IMP:BHF-UCL.
GO; GO:0071277; P:cellular response to calcium ion; IDA:BHF-UCL.
GO; GO:0046514; P:ceramide catabolic process; ISS:BHF-UCL.
GO; GO:0008544; P:epidermis development; IEP:BHF-UCL.
GO; GO:0030216; P:keratinocyte differentiation; IEP:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
GO; GO:0010446; P:response to alkaline pH; IDA:BHF-UCL.
GO; GO:0030148; P:sphingolipid biosynthetic process; IDA:BHF-UCL.
GO; GO:0006665; P:sphingolipid metabolic process; ISS:BHF-UCL.
GO; GO:0046512; P:sphingosine biosynthetic process; IDA:BHF-UCL.
InterPro; IPR008901; Ceramidase.
Pfam; PF05875; Ceramidase; 1.
2: Evidence at transcript level;
Complete proteome; Endoplasmic reticulum; Hydrolase; Lipid metabolism;
Membrane; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 264 Alkaline ceramidase 1.
/FTId=PRO_0000247745.
TOPO_DOM 1 27 Lumenal. {ECO:0000255}.
TRANSMEM 28 48 Helical. {ECO:0000255}.
TOPO_DOM 49 57 Cytoplasmic. {ECO:0000255}.
TRANSMEM 58 78 Helical. {ECO:0000255}.
TOPO_DOM 79 81 Lumenal. {ECO:0000255}.
TRANSMEM 82 102 Helical. {ECO:0000255}.
TOPO_DOM 103 119 Cytoplasmic. {ECO:0000255}.
TRANSMEM 120 137 Helical. {ECO:0000255}.
TOPO_DOM 138 138 Lumenal. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TOPO_DOM 160 176 Cytoplasmic. {ECO:0000255}.
TRANSMEM 177 197 Helical. {ECO:0000255}.
TOPO_DOM 198 206 Lumenal. {ECO:0000255}.
TRANSMEM 207 227 Helical. {ECO:0000255}.
TOPO_DOM 228 264 Cytoplasmic. {ECO:0000255}.
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


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