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ORYSJ:NCASE
Contents
| Species (Taxon ID) | Oryza sativa subsp. japonica (Rice). (39947) | |
| Gene Name(s) | No Information Provided. | |
| Protein Name(s) | Neutral ceramidase
N-CDase NCDase OsCDase Acylsphingosine deacylase N-acylsphingosine amidohydrolase | |
| External Links | ||
| UniProt | Q0JL46 | |
| EMBL | EU422991 AP002819 AP008207 CM000138 AK099625 | |
| RefSeq | NP_001043618.1 | |
| UniGene | Os.23622 | |
| STRING | 39947.LOC_Os01g43520.2 | |
| PRIDE | Q0JL46 | |
| EnsemblPlants | OS01T0624000-01 OS01T0624000-02 | |
| GeneID | 4326680 | |
| KEGG | osa:4326680 | |
| Gramene | Q0JL46 | |
| eggNOG | NOG75118 | |
| HOGENOM | HOG000209915 | |
| InParanoid | Q0JL46 | |
| KO | K12349 | |
| OMA | GAFCESP | |
| BioCyc | MetaCyc:MONOMER-15591 | |
| Reactome | REACT_225825 | |
| Proteomes | UP000000763 | |
| GO | GO:0005783 GO:0005576 GO:0005794 GO:0017040 | |
| InterPro | IPR006823 | |
| PANTHER | PTHR12670 | |
| Pfam | PF04734 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0017040 |
ceramidase activity |
ECO:0000270 |
F |
In figure 4, it was observed that endogenous levels of phytoceramide with fatty acid chain lengths of C26 and C28 were elevated in Δypc1Δydc1 when expression of OsCDase was induced by growth in galactose. This suggests that OsCDase (ceramidase) may exhibit reverse ceramidase activity and catalyze the formation of phytoceramide with very long chain fatty acids |
complete | |||||
| GO:0005794 |
Golgi apparatus |
ECO:0000314 |
C |
Figure 5 shows the red-tagged CDase colocalizes with the GFP tagged golgi. |
complete | |||||
| GO:0005783 |
endoplasmic reticulum |
ECO:0000314 |
C |
Figure 5 shows the red-tagged CDase colocalizes with the GFP tagged ER. |
complete | |||||
|
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005794 |
Golgi apparatus |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0046514 |
ceramide catabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0039774 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0046512 |
sphingosine biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000975176 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0042759 |
long-chain fatty acid biosynthetic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000975176 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0017040 |
N-acylsphingosine amidohydrolase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0039774 |
F |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0039774 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0017040 |
N-acylsphingosine amidohydrolase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0102121 |
ceramidase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005794 |
Golgi apparatus |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005783 |
endoplasmic reticulum |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 1.4 Pata, MO et al. (2008) Molecular cloning and characterization of OsCDase, a ceramidase enzyme from rice. Plant J. 55 1000-9 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 2.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
