Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9WV54

- ASAH1_MOUSE

UniProt

Q9WV54 - ASAH1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acid ceramidase

Gene

Asah1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.

Catalytic activityi

N-acylsphingosine + H2O = a carboxylate + sphingosine.

GO - Molecular functioni

  1. ceramidase activity Source: MGI

GO - Biological processi

  1. lipid metabolic process Source: InterPro
  2. lung development Source: Ensembl
  3. response to organic substance Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

ReactomeiREACT_199008. Glycosphingolipid metabolism.

Protein family/group databases

MEROPSiC89.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid ceramidase (EC:3.5.1.23)
Short name:
AC
Short name:
ACDase
Short name:
Acid CDase
Alternative name(s):
Acylsphingosine deacylase
N-acylsphingosine amidohydrolase
Cleaved into the following 2 chains:
Gene namesi
Name:Asah1
Synonyms:Asah
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1277124. Asah1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 141123Acid ceramidase subunit alphaPRO_0000002316Add
BLAST
Chaini142 – 394253Acid ceramidase subunit betaPRO_0000002317Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)1 Publication
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9WV54.
PaxDbiQ9WV54.
PRIDEiQ9WV54.

PTM databases

PhosphoSiteiQ9WV54.

Expressioni

Gene expression databases

BgeeiQ9WV54.
CleanExiMM_ASAH1.
ExpressionAtlasiQ9WV54. baseline and differential.
GenevestigatoriQ9WV54.

Interactioni

Subunit structurei

Heterodimer of one alpha and one beta subunit.

Protein-protein interaction databases

IntActiQ9WV54. 1 interaction.
MINTiMINT-4088419.

Structurei

3D structure databases

ProteinModelPortaliQ9WV54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acid ceramidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG84249.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
HOVERGENiHBG050586.
InParanoidiQ9WV54.
KOiK12348.
OMAiYTINLDL.
OrthoDBiEOG7TTQ7P.
PhylomeDBiQ9WV54.
TreeFamiTF313219.

Family and domain databases

InterProiIPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view]
PfamiPF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view]
PIRSFiPIRSF017632. Acid_ceramidase-like. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WV54-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRGQSLLTWV LAAAVTCAQA QDVPPWTEDC RKSTYPPSGP TYRGPVPWHT
60 70 80 90 100
INLDLPPYKR WHELLAQKAP ALRILVNSIT SLVNTFVPSG KLMKMVDQKL
110 120 130 140 150
PGMIGSLPDP FGEEMRGIAD VTGIPLGEII SFNIFYELFT MCTSIITEDE
160 170 180 190 200
KGHLLHGRNM DFGIFLGWNI NNNTWVVTEE LKPLTVNLDF QRNNKTVFKA
210 220 230 240 250
TSFVGYVGML TGFKPGLFSL SLNERFSING GYLGILEWMF GRKDAQWVGF
260 270 280 290 300
ITRSVLENTT SYEEAKNTLT KTKIMAPVYF ILGGKKSGEG CVITRERKES
310 320 330 340 350
LDVYELDPKH GRWYVVQTNY DRWKNTLFID DRRTPAKKCL NHTTQKNLSF
360 370 380 390
ATIYDVLSTK PVLNKLTVFT TLMDVTKGQF ESHLRDCPDP CIGW
Length:394
Mass (Da):44,670
Last modified:November 1, 1999 - v1
Checksum:iDA7BFBFDC45C9F65
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157500 mRNA. Translation: AAD39551.1.
AK075666 mRNA. Translation: BAC35884.1.
BC003204 mRNA. Translation: AAH03204.1.
CCDSiCCDS22262.1.
RefSeqiNP_062708.1. NM_019734.2.
UniGeneiMm.22547.

Genome annotation databases

EnsembliENSMUST00000034000; ENSMUSP00000034000; ENSMUSG00000031591.
GeneIDi11886.
KEGGimmu:11886.
UCSCiuc009lnw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157500 mRNA. Translation: AAD39551.1 .
AK075666 mRNA. Translation: BAC35884.1 .
BC003204 mRNA. Translation: AAH03204.1 .
CCDSi CCDS22262.1.
RefSeqi NP_062708.1. NM_019734.2.
UniGenei Mm.22547.

3D structure databases

ProteinModelPortali Q9WV54.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9WV54. 1 interaction.
MINTi MINT-4088419.

Protein family/group databases

MEROPSi C89.001.

PTM databases

PhosphoSitei Q9WV54.

Proteomic databases

MaxQBi Q9WV54.
PaxDbi Q9WV54.
PRIDEi Q9WV54.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034000 ; ENSMUSP00000034000 ; ENSMUSG00000031591 .
GeneIDi 11886.
KEGGi mmu:11886.
UCSCi uc009lnw.2. mouse.

Organism-specific databases

CTDi 427.
MGIi MGI:1277124. Asah1.

Phylogenomic databases

eggNOGi NOG84249.
GeneTreei ENSGT00530000063548.
HOGENOMi HOG000007253.
HOVERGENi HBG050586.
InParanoidi Q9WV54.
KOi K12348.
OMAi YTINLDL.
OrthoDBi EOG7TTQ7P.
PhylomeDBi Q9WV54.
TreeFami TF313219.

Enzyme and pathway databases

Reactomei REACT_199008. Glycosphingolipid metabolism.

Miscellaneous databases

ChiTaRSi Asah1. mouse.
NextBioi 279921.
PROi Q9WV54.
SOURCEi Search...

Gene expression databases

Bgeei Q9WV54.
CleanExi MM_ASAH1.
ExpressionAtlasi Q9WV54. baseline and differential.
Genevestigatori Q9WV54.

Family and domain databases

InterProi IPR016699. Acid_ceramidase-like.
IPR029130. Acid_ceramidase_N.
IPR029132. CBAH/NAAA_C.
[Graphical view ]
Pfami PF02275. CBAH. 1 hit.
PF15508. NAAA-beta. 1 hit.
[Graphical view ]
PIRSFi PIRSF017632. Acid_ceramidase-like. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the full-length cDNA and genomic sequences encoding murine acid ceramidase."
    Li C.-M., Hong S.-B., Kopal G., He X., Linke T., Hou W.-S., Koch J., Gatt S., Sandhoff K., Schuchman E.H.
    Genomics 50:267-274(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Brain.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-258.

Entry informationi

Entry nameiASAH1_MOUSE
AccessioniPrimary (citable) accession number: Q9WV54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3