| IED ID |
IndEnz0005001141 |
| Enzyme Type ID |
lipase001141 |
| Protein Name |
Helix-loop-helix protein 30
|
| Gene Name |
hlh-30 W02C12.3 |
| 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 |
MIRQLNSPGGGGGLGLNNPRAQQPPGAQQQQQPQQAQQQFYDDEPYQANASQFRFGAGKSMEQRRETGNLIPIAQRSMGSTSTPFGSAPTQSYFGGGSSGAALSSPRKMQQTHQMLFGNIQPPRGSPPSDGSDKIHRFGESPTPGGVGGVFGTELDDLIIDELMGMEDDQRMRPGATRPMTIGGEKTMSMARPIPGASSRAGSGHSGSPITIPNAMSNNFRQVVSSSAPTSSIDIEKMIGAVSNGGGNSGGDNDPEDYYRDRRKKDIHNMIERRRRYNINDRIKELGQMLPKNTSEDMKLNKGTILKASCDYIRVLQKDREQAMKTQQQQKSLESTAHKYADRVKELEEMLARQGVQVPPSHLPPIPKVIERPIKQEIDESPPNHTPTGSFVSSSGFLSEVTNNTAAMQITSPNDSRPNNFMNNSAPSDSFFSVGSASPPDYRTSSGTASWKLPGSNAFSDLMMDDLNPMMNGDPLISSAGAHPSPHFHSSQMSPDIHWDASGFSPDPINTQQSNSGHYHMDFS |
| Enzyme Length |
524 |
| Uniprot Accession Number |
H2KZZ2 |
| Absorption |
|
| Active Site |
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| Activity Regulation |
|
| Binding Site |
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| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
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| Enzyme Function |
FUNCTION: Transcription factor which regulates the expression of genes involved in lipid metabolism and autophagy in response to nutrient availability, bacterial pore-forming toxins or heat shock (PubMed:23604316, PubMed:23925298, PubMed:27001890, PubMed:27875098, PubMed:28198373). Binds to the E-box motif 5'-CACGTG-3' (PubMed:19632181). Under fasting conditions, binds to the promoter and activates the expression of lipase genes lipl-2, lipl-3 and lipl-5, and to a lesser extent, lipl-1, thereby regulating lipolysis (PubMed:23604316). Involved in modulating longevity in response to TOR signaling, dietary restriction, germline signaling, heat shock and the insulin-like signaling pathway (PubMed:23925298, PubMed:27001890, PubMed:24882217, PubMed:28198373). Involved in the immune response to infection by the S.aureus bacterium, probably acting downstream of the protein kinase dkf-1, leading to the transcriptional activation of host defense genes (PubMed:24882217, PubMed:27184844). May also play a role in lysosomal biogenesis in response to nutrient availability (PubMed:23604316). {ECO:0000269|PubMed:19632181, ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:23925298, ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27184844, ECO:0000269|PubMed:27875098}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
|
| nucleotide Binding |
|
| Features |
Alternative sequence (7); Chain (1); Coiled coil (1); Compositional bias (2); Domain (1); Region (5) |
| Keywords |
Alternative splicing;Coiled coil;Cytoplasm;DNA-binding;Nucleus;Reference proteome;Transcription;Transcription regulation |
| Interact With |
|
| Induction |
INDUCTION: Up-regulated by fasting. {ECO:0000269|PubMed:23604316}. |
| Subcellular Location |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:28198373}. Cytoplasm {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:28198373}. Note=Localization to nucleus enhanced during fasting and on mutant backgrounds involved in modulating longevity: glp-1, let-363 (tor), eat-2, daf-2, clk-1 or rsks-1 (PubMed:23604316, PubMed:23925298). Nuclear localization abolished on mml-1;glp-1 or mxl-2;glp-1 mutant backgrounds (PubMed:27001890). Localization to nucleus enhanced as a result of bacterial pore-forming toxin treatment, or heat shock (PubMed:27875098, PubMed:28198373). {ECO:0000269|PubMed:23604316, ECO:0000269|PubMed:23925298, ECO:0000269|PubMed:27001890, ECO:0000269|PubMed:27875098}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27184844}. Note=(Microbial infection) Localization to nucleus enriched rapidly after Staphylococcus aureus infection. {ECO:0000269|PubMed:24882217, ECO:0000269|PubMed:27184844}. |
| Modified Residue |
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| Post Translational Modification |
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| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
10778742;
12097347;
12529643;
15338614;
16507136;
16809667;
16845399;
17164286;
17486083;
17513831;
17850180;
18794350;
19123269;
19343510;
19922876;
20439776;
20461074;
21177967;
21367940;
21849976;
21938618;
22267497;
22286215;
22347378;
22396654;
22560298;
23533643;
23549480;
23586691;
23604319;
23791784;
23800452;
24068555;
24884423;
25487147;
26759963;
27420916;
28355222;
29600279;
29768192;
30299269;
30353013;
31086360;
31398187;
32259199;
33314217;
33683370;
6593563;
|
| Motif |
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| Gene Encoded By |
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| Mass |
56,857 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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