Q8TDN7 (ACER1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkaline ceramidase 1
Short name=AlkCDase 1
Short name=Alkaline CDase 1
EC=3.5.1.23

Alternative name(s):
Acylsphingosine deacylase 3
N-acylsphingosine amidohydrolase 3

Gene names

Name:	ACER1
Synonyms:	ASAH3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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.
Catalytic activity	N-acylsphingosine + H2O = a carboxylate + sphingosine.
Enzyme regulation	Inhibited by sphingosine By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Mainly expressed in epidermis. Ref.3
Sequence similarities	Belongs to the alkaline ceramidase family.

Ontologies

Keywords
Biological process	Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ceramidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 264	264	Alkaline ceramidase 1		PRO_0000247745
Regions
	Topological domain	1 – 27	27	Lumenal Potential
	Transmembrane	28 – 48	21	Helical; Potential
	Topological domain	49 – 57	9	Cytoplasmic Potential
	Transmembrane	58 – 78	21	Helical; Potential
	Topological domain	79 – 81	3	Lumenal Potential
	Transmembrane	82 – 102	21	Helical; Potential
	Topological domain	103 – 119	17	Cytoplasmic Potential
	Transmembrane	120 – 137	18	Helical; Potential
	Topological domain	138	1	Lumenal Potential
	Transmembrane	139 – 159	21	Helical; Potential
	Topological domain	160 – 176	17	Cytoplasmic Potential
	Transmembrane	177 – 197	21	Helical; Potential
	Topological domain	198 – 206	9	Lumenal Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Topological domain	228 – 264	37	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8TDN7 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: E16E5DB81D064F60	FASTA	264	31,095
	10 20 30 40 50 60 MPSIFAYQSS EVDWCESNFQ YSELVAEFYN TFSNIPFFIF GPLMMLLMHP YAQKRSRYIY 70 80 90 100 110 120 VVWVLFMIIG LFSMYFHMTL SFLGQLLDEI AILWLLGSGY SIWMPRCYFP SFLGGNRSQF 130 140 150 160 170 180 IRLVFITTVV STLLSFLRPT VNAYALNSIA LHILYIVCQE YRKTSNKELR HLIEVSVVLW 190 200 210 220 230 240 AVALTSWISD RLLCSFWQRI HFFYLHSIWH VLISITFPYG MVTMALVDAN YEMPGETLKV 250 260 RYWPRDSWPV GLPYVEIRGD DKDC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides." Mao C., Xu R., Szulc Z.M., Bielawski J., Becker K.P., Bielawska A., Galadari S.H., Hu W., Obeid L.M. J. Biol. Chem. 278:31184-31191(2003) [PubMed: 12783875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis." Houben E., Holleran W.M., Yaginuma T., Mao C., Obeid L.M., Rogiers V., Takagi Y., Elias P.M., Uchida Y. J. Lipid Res. 47:1063-1070(2006) [PubMed: 16477081] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF347024 mRNA. Translation: AAL83822.1. BC112122 mRNA. Translation: AAI12123.1. BC112124 mRNA. Translation: AAI12125.1.
IPI	IPI00152570.
RefSeq	NP_597999.1. NM_133492.2.
UniGene	Hs.352609.
3D structure databases
ProteinModelPortal	Q8TDN7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8TDN7.
Polymorphism databases
DMDM	74715919.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000301452; ENSP00000301452; ENSG00000167769.
GeneID	125981.
KEGG	hsa:125981.
UCSC	uc002mel.1. human.
Organism-specific databases
CTD	125981.
GeneCards	GC19M006261.
H-InvDB	HIX0039998.
HGNC	HGNC:18356. ACER1.
HPA	HPA042506.
MIM	613491. gene.
neXtProt	NX_Q8TDN7.
PharmGKB	PA134897634. PA164714838.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04896.
GeneTree	ENSGT00390000004916.
HOGENOM	HBG446871.
InParanoid	Q8TDN7.
OMA	FQYSELV.
OrthoDB	EOG4XD3RW.
PhylomeDB	Q8TDN7.
Enzyme and pathway databases
Reactome	REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q8TDN7.
Bgee	Q8TDN7.
CleanEx	HS_ACER1.
Genevestigator	Q8TDN7.
GermOnline	ENSG00000167769. Homo sapiens.
Family and domain databases
InterPro	IPR008901. Ceramidase. [Graphical view]
KO	K01441.
Pfam	PF05875. Ceramidase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	81606.
SOURCE	Search...

Entry information

Entry name

ACER1_HUMAN

Accession

Primary (citable) accession number: Q8TDN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.