| IED ID |
IndEnz0005001347 |
| Enzyme Type ID |
lipase001347 |
| Protein Name |
Abhydrolase domain-containing protein abhd-5.2
|
| Gene Name |
abhd-5.2 cgi-58 C37H5.3 |
| Organism |
Caenorhabditis elegans |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Protostomia
Ecdysozoa
Nematoda (roundworms)
Chromadorea
Rhabditida
Rhabditina
Rhabditomorpha
Rhabditoidea
Rhabditidae
Peloderinae
Caenorhabditis
Caenorhabditis elegans
|
| Enzyme Sequence |
MFQKTDFLSKIFSSSSHPLTGSQNIVVKDPQTLDFAMQSQNEIVCSLRERSHMNTMSYAQTQMMAIDEIRAFQSEGHLHLKYISLIIAMMAETAVVTSRSWFPYFSCPSKSQRLAEAEGRILSALGIKYLARLIQIPFKNTEISTITVNCESEQPIVKAKYPIVLIHGFGAGVALWGSAIKRLAQFQTVHAFDLPGFGRSSRPKFSSDPETAETEMIDSIEQWRDKMNLEKMNLVGHSFGGYLATSYALKYPKRVENLILADPWGFNEMDPEFAQKLTSRQKNIFWVIQQFNPLAVLRLVGGYGPSLVRRLRPDLALKYSEDVYDYIYLANSRDPTGEEVFKCLSENLGWAKQPMSKRFHELDNTVPVTFIHGERSWIDWRTTRRLFGELEHVESHIMDSAGHHVYADDADKFVQLVIGSLKDGKTGELVPEEVNLEEEIVTPI |
| Enzyme Length |
444 |
| Uniprot Accession Number |
H2KZ86 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Acts coordinately with phospholipase atgl-1 within the lipolytic cascade to distribute stored energy to tissues to maintain energy levels during the dauer phase. Localizes atgl-1 to lipid droplets, possibly to facilitate triglyceride hydrolysis. Regulates lipid droplet size, lipid content, the exchange of lipids between lipid droplets and fusion of lipid droplets during the dauer phase. {ECO:0000269|PubMed:26083785}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Alternative sequence (1); Chain (1); Domain (1) |
| Keywords |
Alternative splicing;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Reference proteome |
| Interact With |
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| Induction |
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| Subcellular Location |
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26083785}. |
| Modified Residue |
|
| Post Translational Modification |
|
| Signal Peptide |
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| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
12529643;
16600994;
17164286;
19343510;
21177967;
22347378;
22560298;
23800452;
25487147;
|
| Motif |
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| Gene Encoded By |
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| Mass |
50,488 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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