Q8R4X1 (ACER1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkaline ceramidase 1
Short name=AlkCDase 1
Short name=Alkaline CDase 1
Short name=maCER1
EC=3.5.1.23

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

Gene names

Name:	Acer1
Synonyms:	Asah3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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. Ref.1
Catalytic activity	N-acylsphingosine + H2O = a carboxylate + sphingosine.
Enzyme regulation	Inhibited by sphingosine. Inhibited by Mn2+, Zn2+, and Cu2+ in a dose-dependent manner. Slightly activated by Ca2+ in a dose-dependent manner. Ref.1
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Highly expressed in skin. Weakly or not expressed in other tissues. Ref.1
Sequence similarities	Belongs to the alkaline ceramidase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.0. Ref.1

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)
Biological process	ceramide catabolic process Inferred from direct assay Ref.1. Source: MGI regulation of lipid metabolic process Inferred from direct assay Ref.1. Source: MGI
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ceramidase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 273	273	Alkaline ceramidase 1		PRO_0000247746
Regions
	Topological domain	1 – 36	36	Lumenal Potential
	Transmembrane	37 – 57	21	Helical; Potential
	Topological domain	58 – 72	15	Cytoplasmic Potential
	Transmembrane	73 – 93	21	Helical; Potential
	Transmembrane	94 – 114	21	Helical; Potential
	Topological domain	115 – 126	12	Cytoplasmic Potential
	Transmembrane	127 – 147	21	Helical; Potential
	Topological domain	148 – 149	2	Lumenal Potential
	Transmembrane	150 – 167	18	Helical; Potential
	Topological domain	168 – 177	10	Cytoplasmic Potential
	Transmembrane	178 – 198	21	Helical; Potential
	Topological domain	199 – 215	17	Lumenal Potential
	Transmembrane	216 – 236	21	Helical; Potential
	Topological domain	237 – 273	37	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8R4X1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 0B84D015D7870219	FASTA	273	32,082
	10 20 30 40 50 60 MHVPGTRAKM SSIFAYQSSE VDWCESNFQH SELVAEFYNT FSNVFFLIFG PLMMFLMHPY 70 80 90 100 110 120 AQKRTRCFYG VSVLFMLIGL FSMYFHMTLS FLGQLLDEIS ILWLLASGYS VWLPRCYFPK 130 140 150 160 170 180 FVKGNRFYFS CLVTITTIIS TFLTFVKPTV NAYALNSIAI HILYIVRTEY KKIRDDDLRH 190 200 210 220 230 240 LIAVSVVLWA AALTSWISDR VLCSFWQRIH FYYLHSIWHV LISITFPYGI VTMALVDAKY 250 260 270 EMPDKTLKVH YWPRDSWVIG LPYVEIQEND KNC

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], FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Skin and Tongue.
[3]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF347023 mRNA. Translation: AAL83821.1. AK028901 mRNA. Translation: BAC26186.1. AK075884 mRNA. Translation: BAC36029.1. BC130254 mRNA. Translation: AAI30255.1.
IPI	IPI00153946.
RefSeq	NP_783858.1. NM_175731.4.
UniGene	Mm.218784.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8R4X1.
Proteomic databases
PRIDE	Q8R4X1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000056113; ENSMUSP00000062037; ENSMUSG00000045019.
GeneID	171168.
KEGG	mmu:171168.
UCSC	uc008ddl.1. mouse.
Organism-specific databases
CTD	125981.
MGI	MGI:2181962. Acer1.
Phylogenomic databases
GeneTree	ENSGT00390000004916.
HOGENOM	HBG446871.
InParanoid	Q8R4X1.
OMA	FQYSELV.
OrthoDB	EOG4XD3RW.
PhylomeDB	Q8R4X1.
Enzyme and pathway databases
BRENDA	3.5.1.23. 3474.
Gene expression databases
ArrayExpress	Q8R4X1.
Bgee	Q8R4X1.
Genevestigator	Q8R4X1.
GermOnline	ENSMUSG00000045019. Mus musculus.
Family and domain databases
InterPro	IPR008901. Ceramidase. [Graphical view]
KO	K01441.
Pfam	PF05875. Ceramidase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	370572.
SOURCE	Search...

Entry information

Entry name

ACER1_MOUSE

Accession

Primary (citable) accession number: Q8R4X1
Secondary accession number(s): A1L3S2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 2002
Last modified:	November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program