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Q8VD53 (ACER2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alkaline ceramidase 2
Short name=AlkCDase 2
Short name=Alkaline CDase 2
Short name=maCER2
EC=3.5.1.23
Alternative name(s):
Acylsphingosine deacylase 3-like
Cancer-related gene liver 1 protein
Short name=CRG-L1
N-acylsphingosine amidohydrolase 3-like
Gene names
Name:Acer2
Synonyms:Asah3l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid By similarity. Unsaturated long-chain ceramides are the best substrates, saturated long-chain ceramides and unsaturated very long-chain ceramides are good substrates, whereas saturated very long-chain ceramides and short-chain ceramides were poor substrates By similarity. Inhibits the maturation of protein glycosylation in the Golgi complex, including that of integrin beta-1 (ITGB1) and of LAMP1, by increasing the levels of sphingosine By similarity. Inhibits cell adhesion by reducing the level of ITGB1 in the cell surface By similarity. May have a role in cell proliferation and apoptosis that seems to depend on the balance between sphingosine and sphingosine-1-phosphate By similarity.

Catalytic activity

N-acylsphingosine + H2O = a carboxylate + sphingosine.

Enzyme regulation

Specifically activated by lumenal, but not cytosolic Ca2+ By similarity.

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein By similarity.

Miscellaneous

Up-regulated in hepatocellular carcinomas.

Sequence similarities

Belongs to the alkaline ceramidase family.

Sequence caution

The sequence BAC39416.1 differs from that shown. Reason: Chimera.

Ontologies

Keywords
   Biological processLipid metabolism
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processceramide metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionceramidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VD53-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8VD53-2)

The sequence of this isoform differs from the canonical sequence as follows:
     122-167: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Alkaline ceramidase 2
PRO_0000247749

Regions

Topological domain1 – 3232Lumenal Potential
Transmembrane33 – 5321Helical; Potential
Topological domain54 – 629Cytoplasmic Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 863Lumenal Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 12417Cytoplasmic Potential
Transmembrane125 – 14218Helical; Potential
Topological domain1431Lumenal Potential
Transmembrane144 – 16421Helical; Potential
Topological domain165 – 1739Cytoplasmic Potential
Transmembrane174 – 19421Helical; Potential
Topological domain195 – 21117Lumenal Potential
Transmembrane212 – 23221Helical; Potential
Topological domain233 – 27543Cytoplasmic Potential

Amino acid modifications

Glycosylation231N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence122 – 16746Missing in isoform 2.
VSP_020036

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 8FCC755B4949B9DF

FASTA27531,369
        10         20         30         40         50         60 
MGAPHWWDHL RAGSSEVDWC EDNYTIVPAI AEFYNTISNV LFFILPPICM CLFRQYATCF 

        70         80         90        100        110        120 
NSGIYLIWTL LVVVGIGSVY FHATLSFLGQ MLDELAILWV LMCALAMWFP RRYLPKIFRN 

       130        140        150        160        170        180 
DRGRFKAVVC VLSAITTCLA FIKPAINNIS LMILGLPCTA LLVAELKRCD NVRVFKLGLF 

       190        200        210        220        230        240 
SGLWWTLALF CWISDQAFCE LLSSFHFPYL HCVWHILICL ASYLGCVCFA YFDAASEIPE 

       250        260        270 
QGPVIRFWPS EKWAFIGVPY VSLLCAHKKS PVKIT

« Hide

Isoform 2 [UniParc].

Checksum: D396EFEA1F3B70A1
Show »

FASTA22926,500

References

« Hide 'large scale' references
[1]"Expression profiling and identification of novel genes in hepatocellular carcinomas."
Graveel C.R., Jatkoe T., Madore S.J., Holt A.L., Farnham P.J.
Oncogene 20:2704-2712(2001) [PubMed: 11420682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hepatoma.
[2]"Cloning and characterization of a Homo sapiens Golgi alkaline ceramidase: an enzyme that regulates the levels of sphingosine-1-P, and cell growth and survival."
Xu R., Hu W., Obeid L.M., Mao C.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[4]"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. expand/collapse author list , 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] OF 1-215.
Strain: C57BL/6J.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF282864 mRNA. Translation: AAL40408.1.
AY312515 mRNA. Translation: AAQ85131.1.
BC059819 mRNA. Translation: AAH59819.1.
AK085306 mRNA. Translation: BAC39416.1. Sequence problems.
IPIIPI00122593.
IPI00461271.
RefSeqNP_647467.1. NM_139306.2.
UniGeneMm.45019.
Mm.458684.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8VD53.

Proteomic databases

PRIDEQ8VD53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045224; ENSMUSP00000040048; ENSMUSG00000038007.
ENSMUST00000084433; ENSMUSP00000081473; ENSMUSG00000038007.
GeneID230379.
KEGGmmu:230379.

Organism-specific databases

CTD340485.
MGIMGI:1920932. Acer2.

Phylogenomic databases

GeneTreeENSGT00390000004916.
HOGENOMHBG446871.
InParanoidQ8VD53.
OMAKRCDNVR.
OrthoDBEOG41G34Q.
PhylomeDBQ8VD53.

Gene expression databases

ArrayExpressQ8VD53.
BgeeQ8VD53.
CleanExMM_ASAH3L.
GenevestigatorQ8VD53.
GermOnlineENSMUSG00000038007. Mus musculus.

Family and domain databases

InterProIPR008901. Ceramidase.
[Graphical view]
KOK01441.
PfamPF05875. Ceramidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379885.
SOURCESearch...

Entry information

Entry nameACER2_MOUSE
AccessionPrimary (citable) accession number: Q8VD53
Secondary accession number(s): Q6PB92, Q8BUG3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2002
Last modified: November 16, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents