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Protein

Acid ceramidase

Gene

asah-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid.By similarity

Catalytic activityi

N-acylsphingosine + H2O = a carboxylate + sphingosine.

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiR-CEL-1660662. Glycosphingolipid metabolism.
UniPathwayiUPA00222.

Protein family/group databases

MEROPSiC89.A02.

Names & Taxonomyi

Protein namesi
Recommended name:
Acid ceramidase (EC:3.5.1.23)
Alternative name(s):
Acylsphingosine amidohydrolase 1
Gene namesi
Name:asah-1
ORF Names:K11D2.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiK11D2.2; CE12120; WBGene00010769; asah-1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 393377Acid ceramidasePRO_0000002322Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO45686.

Interactioni

Subunit structurei

Heterodimer of one alpha and one beta subunit.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
lag-1Q9TYY11EBI-324508,EBI-324482
vps-39Q9XUQ41EBI-324508,EBI-318975

Protein-protein interaction databases

BioGridi38517. 2 interactions.
DIPiDIP-26864N.
IntActiO45686. 2 interactions.
MINTiMINT-1094668.
STRINGi6239.K11D2.2.1.

Structurei

3D structure databases

ProteinModelPortaliO45686.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acid ceramidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFSS. Eukaryota.
ENOG410XQ6Y. LUCA.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
InParanoidiO45686.
KOiK12348.
OMAiWYTINLD.
PhylomeDBiO45686.

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.

O45686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRELSVLLL VAVCAAKHVE LPAPFKDHCI LDDKQNLYDP SKQFDIKWYD
60 70 80 90 100
VNLDLPPSER WVQIATANKE HIADLIGVLI NLITPWFPNA IDFVDDVFGD
110 120 130 140 150
LAPKLAQPYR DEIFSIANAT GIPLGQITMY NIFYEIFTVC TSVIAQDKDG
160 170 180 190 200
HVFHARNLDF GLFMGWDPVL HDWQISQKLR KMIINVNWLK DGKLLYKSNN
210 220 230 240 250
FAGYIGIYNG LKPNAFSLTA DDRFQLVGGY YGILKWVFGL EADGKWMSWL
260 270 280 290 300
ARETLETKTT YLDAKEHLMN TPMLSPVYFI LGGSKKDEGC IIARSLDKTA
310 320 330 340 350
LLTEMATSPH GWYLLETNYD QGTEDLYLDD RDTPGFRCMD KLTQKNVGFE
360 370 380 390
GIFNVLSSRT NLNKLTTYTV LMSVETSRFE TILQSCPGEC YPW
Length:393
Mass (Da):44,823
Last modified:June 1, 1998 - v1
Checksum:i7545366601FDFFF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z83115 Genomic DNA. Translation: CAB05556.1.
PIRiT23602.
RefSeqiNP_493173.1. NM_060772.8.
UniGeneiCel.6266.

Genome annotation databases

EnsemblMetazoaiK11D2.2.1; K11D2.2.1; WBGene00010769.
K11D2.2.2; K11D2.2.2; WBGene00010769.
GeneIDi173120.
KEGGicel:CELE_K11D2.2.
UCSCiK11D2.2. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z83115 Genomic DNA. Translation: CAB05556.1.
PIRiT23602.
RefSeqiNP_493173.1. NM_060772.8.
UniGeneiCel.6266.

3D structure databases

ProteinModelPortaliO45686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38517. 2 interactions.
DIPiDIP-26864N.
IntActiO45686. 2 interactions.
MINTiMINT-1094668.
STRINGi6239.K11D2.2.1.

Protein family/group databases

MEROPSiC89.A02.

Proteomic databases

PaxDbiO45686.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiK11D2.2.1; K11D2.2.1; WBGene00010769.
K11D2.2.2; K11D2.2.2; WBGene00010769.
GeneIDi173120.
KEGGicel:CELE_K11D2.2.
UCSCiK11D2.2. c. elegans.

Organism-specific databases

CTDi173120.
WormBaseiK11D2.2; CE12120; WBGene00010769; asah-1.

Phylogenomic databases

eggNOGiENOG410IFSS. Eukaryota.
ENOG410XQ6Y. LUCA.
GeneTreeiENSGT00530000063548.
HOGENOMiHOG000007253.
InParanoidiO45686.
KOiK12348.
OMAiWYTINLD.
PhylomeDBiO45686.

Enzyme and pathway databases

UniPathwayiUPA00222.
ReactomeiR-CEL-1660662. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi878341.
PROiO45686.

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.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiASAH1_CAEEL
AccessioniPrimary (citable) accession number: O45686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 11, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.