Neutral ceramidase - Danio rerio (Zebrafish)

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Q5W7F1 (ASAH2_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 49. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Neutral ceramidase
Short name=N-CDase
Short name=NCDase
EC=3.5.1.23

Alternative name(s):
Acylsphingosine deacylase 2
N-acylsphingosine amidohydrolase 2
Short name=znCD

Gene names

Name:

asah2

Organism

Danio rerio (Zebrafish) (Brachydanio rerio)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	743 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 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Essential for the metabolism of ceramide and the early development. Ref.1
Catalytic activity	N-acylsphingosine + H₂O = a carboxylate + sphingosine.
Subcellular location	Cell membrane; Single-pass type II membrane protein Ref.1.
Post-translational modification	N-glycosylated. Ref.1 O-glycosylated. Ref.1
Disruption phenotype	Fishes display severe embryonic morphological and cellular abnormalities such as abnormal morphogenesis in the head and tail, pericardiac edema, defect of blood cell circulation, and an increase of apoptotic cells, especially in the head and neural tube regions, at 36 hours post-fertilization. Ref.1
Sequence similarities	Belongs to the neutral ceramidase family.

Ontologies

Keywords
Biological process	Lipid metabolism Sphingolipid metabolism
Cellular component	Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Developmental protein Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ceramide metabolic process Inferred from direct assay Ref.1. Source: ZFIN multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi membrane Inferred from direct assay Ref.1. Source: ZFIN apical plasma membrane Inferred from direct assay Ref.1. Source: ZFIN endoplasmic reticulum membrane Inferred from direct assay Ref.1. Source: ZFIN integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ceramidase activity Inferred from direct assay Ref.1. Source: ZFIN
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

743

Neutral ceramidase

PRO_0000247105

Regions

Topological domain

14

Cytoplasmic Potential

Transmembrane

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

708

Lumenal Potential

Sites

Active site

1

Nucleophile By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q5W7F1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 7D2DC7395BA8CF70
Show »

743

82,069

        10         20         30         40         50         60 
MASKSRRLSG LEISLIVLFL LMTAVSVALI TVLALKQESD KKEEVTPEEP SPSVTPPEKP 

        70         80         90        100        110        120 
YLIGVGRADC TGPVADLPMM GYANTDQTAR GLHTRLFSRA FIVDDGNKRV VFVTSDIGMV 

       130        140        150        160        170        180 
SQRLRLEVFQ ALKEKYGDLY RQDNVVLSGT HTHSGVGGYF QYTLFMITSK GYIKPSIQAI 

       190        200        210        220        230        240 
VSGIVKSIDI AHRNLRPGRI FINKGQVADS NFNRSPHSYM NNPEEERNRY EFNTDKQIVV 

       250        260        270        280        290        300 
LKFTDLDGDG IGLLSWFAVH PVSMNYTNRM VSSDNLGYAS YIFEQEKNIG FLPGEKGPFV 

       310        320        330        340        350        360 
AGFSSSNLGD SSPNIRGPVC VNTGLKCDYI NSSCPVGGKK ACIAFGPGED MFESTRIIGE 

       370        380        390        400        410        420 
NMFKIAKELY GSAKQELHGP VYGAHQWVNM TDETVQFNST HTGRTCKPAL GHSFAAGTTD 

       430        440        450        460        470        480 
GGGEFNFLQG DTEGDPFWDG IRDAVLGPPS NETKACHQPK PILFSTGEMD SPLPWHPAIV 

       490        500        510        520        530        540 
DVQIITIGSL AVVAVPGEFT TMSGRRIREA VKRELEVKEP FTNAEVVVAG LCNIYTHYIT 

       550        560        570        580        590        600 
TYEEYQIQRY EGASTIFGPH TLSAYIQRYR GLAKAIAHGT IGELPKGPEP PFFDEDKLFN 

       610        620        630        640        650        660 
QVRDPVADVA PVGTTFGDVL QEVNPVYKVG EIASVTFVSG NPRHSGDIRD TTLVTVERFH 

       670        680        690        700        710        720 
NDTGSWEIIH NDASWETRFH WIKGLAGRSQ AKVEWHIPQT AQAGTYQIQY FGHYKQTTEN 

       730        740 
TTVITPYVGT SAAFKVARSF YYF

References

[1]

"Molecular cloning and functional analysis of zebrafish neutral ceramidase."
Yoshimura Y., Tani M., Okino N., Iida H., Ito M.
J. Biol. Chem. 279:44012-44022(2004) [PubMed: 15271994] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB194413 mRNA. Translation: BAD69590.1.
IPI	IPI00481782.
RefSeq	NP_001007764.1. NM_001007763.1.
UniGene	Dr.37168.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5W7F1.
Proteomic databases
PRIDE	Q5W7F1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSDART00000027793; ENSDARP00000024847; ENSDARG00000012829. ENSDART00000146650; ENSDARP00000119244; ENSDARG00000012829.
GeneID	493602.
KEGG	dre:493602.
Organism-specific databases
CTD	56624.
ZFIN	ZDB-GENE-041112-1. asah2.
Phylogenomic databases
eggNOG	fiNOG13161.
GeneTree	ENSGT00390000015792.
HOGENOM	HBG315824.
HOVERGEN	HBG080870.
InParanoid	Q5W7F1.
OMA	SWFAVHP.
OrthoDB	EOG4G4GPW.
Gene expression databases
Bgee	Q5W7F1.
Family and domain databases
InterPro	IPR006823. Ceramidase_alk. [Graphical view]
KO	K12349.
PANTHER	PTHR12670. Ceramidase_alk. 1 hit.
Pfam	PF04734. Ceramidase_alk. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ASAH2_DANRE

Accession

Primary (citable) accession number: Q5W7F1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	December 7, 2004
Last modified:	November 16, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents