| IED ID | IndEnz0005000328 |
| Enzyme Type ID | lipase000328 |
| Protein Name |
Protein glp-1 Cleaved into: glp-1/Notch intracellular domain |
| Gene Name | glp-1 emb-33 F02A9.6 |
| 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 | MRVLLILLAFFAPIASQLMGGECGREGACSVNGKCYNGKLIETYWCRCKKGFGGAFCERECDLDCKRGEKCIYDVYGENPTCICQDCEDETPPTERTQKGCEEGYGGPDCKTPLFSGVNPCDSDPCNNGLCYPFYGGFQCICNNGYGGSYCEEGIDHCAQNECAEGSTCVNSVYNYYCDCPIGKSGRYCERTECALMGNICNHGRCIPNRDEDKNFRCVCDSGYEGEFCNKDKNECLIEETCVNNSTCFNLHGDFTCTCKPGYAGKYCEEAIDMCKDYVCQNDGYCAHDSNQMPICYCEQGFTGQRCEIECPSGFGGIHCDLPLQRPHCSRSNGTCYNDGRCINGFCVCEPDYIGDRCEINRKDFKFPDIQSCKYNPCVNNATCIDLKNSGYSCHCPLGFYGLNCEQHLLCTPTTCANGGTCEGVNGVIRCNCPNGFSGDYCEIKDRQLCSRHPCKNGGVCKNTGYCECQYGYTGPTCEEVLVIEKSKETVIRDLCEQRKCMDLASNGICNPECNLEECNFDGGDCSGGQRPFSKCQYPARCADQFANGVCNQECNNEECLYDGLDCQSELFRCPAHIRKHCIERRGDGVCNLECSFIGCGFDGGDCNNGTEAIILSDIRIKVQIDPIEFQATGGETLMQISANLRATVRIQRDELGPLVFRWDGEHEMERVEMNSSKLEDQFVLSHHVRRYRQAVVTGIVLYLEVEEICKPEFCRFSTAQSVVDLIAAGLVKSDGRMSLGLPITEAMVAVPKRNEIDEGWSRSQVILFACIAFLAFGTVVAGVIAKNGPERSRKRKMVNATVWMPPMESTNEKGRRNQSNHSSQCSLLDNSAYYHPNTKRHCSDYSTGYNGEQYSQIYPQTLANGYPGDYNELNFDFQSETFAPADLPADEIPLHVQAAGPDAITAPITNESVNQVDSKYRRRVLHWLAANVRGKPEDVITTEAIRCLKAGADVNARDCDENTALMLAVRAHRVRLSVVLLREGANPTIFNNSERSALHEAVVNKDLRILRHLLTDKRLLKEIDELDRNGMTALMLVARELGKHQVEMAELLLSKGAKLDYDGAARKDSNKYKGRTALHYAAMHDNEEMVIMLVRRSSNKDKQDEDGRTPIMLAAKEGCEKTVQYLALNDASLGIVDSMDMTAAQVAEASYHHELAAFLRQVANERHRNDIMRQQIVKSGHGAKSGRQTVKNIKRAGSRKTPTSAASSRETNHLTPPPSDGSFSSPSPHYYPTTTSTPNRMETSPEYMFNHEMAPPVNAMWYTTPPPYQDPNYRHVPPNTAFQNAEQMNGSFYC |
| Enzyme Length | 1295 |
| Uniprot Accession Number | P13508 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Essential signaling protein which has a major role in germline and embryonic development; involved in cell fate decisions that require cell-cell interactions (PubMed:8156602, PubMed:16319922, PubMed:19379690). Probable membrane-bound receptor for putative ligands lag-2 and apx-1 (PubMed:8156602, PubMed:7607081). Upon ligand activation, and releasing from the cell membrane, the glp-1/Notch intracellular domain (NICD) probably forms a transcriptional activator complex with lag-1 and lag-3 and regulates expression of various genes; targets in the germline include lst-1 and sygl-1 (PubMed:9003776, PubMed:10884418, PubMed:16319922, PubMed:32196486, PubMed:16197940, PubMed:7566091, PubMed:19379690). Involved in the specification of the cell fates of the blastomeres, ABa and ABp (PubMed:8156602). Proper signaling by glp-1 induces ABa descendants to produce anterior pharyngeal cells, and ABp descendants to adopt a different fate (PubMed:8156602). Contributes to the establishment of the dorsal-ventral axis in early embryos (PubMed:8156602). Required in postmitotic neurons in order to maintain the developmentally arrested larval state known as dauer, probably in response to lag-2 (PubMed:18599512). Regulates germ cell mitotic proliferation probably by regulating MAP kinase phosphatase lip-1 expression (PubMed:16319922, PubMed:22278922). Required for oocyte growth control (PubMed:19502484). Plays a negative role in lifespan (PubMed:21906946, PubMed:24332851, PubMed:28853436). {ECO:0000269|PubMed:10884418, ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:16319922, ECO:0000269|PubMed:18599512, ECO:0000269|PubMed:19502484, ECO:0000269|PubMed:21906946, ECO:0000269|PubMed:22278922, ECO:0000269|PubMed:24332851, ECO:0000269|PubMed:28853436, ECO:0000269|PubMed:32196486, ECO:0000269|PubMed:7566091, ECO:0000269|PubMed:7607081, ECO:0000269|PubMed:8156602, ECO:0000269|PubMed:9003776, ECO:0000303|PubMed:19379690}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Compositional bias (1); Disulfide bond (37); Domain (10); Glycosylation (6); Mutagenesis (5); Region (1); Repeat (8); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | ANK repeat;Activator;Cell membrane;Cell projection;Developmental protein;Differentiation;Disulfide bond;EGF-like domain;Glycoprotein;Membrane;Notch signaling pathway;Nucleus;Reference proteome;Repeat;Signal;Transcription;Transcription regulation;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7607081}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:18599512}. Note=Localized to axons during dauer larval stage. {ECO:0000269|PubMed:18599512}.; SUBCELLULAR LOCATION: [glp-1/Notch intracellular domain]: Nucleus {ECO:0000269|PubMed:9003776}. Note=The glp-1/Notch intracellular domain (NICD) may become localized to the nucleus after ligand activation. {ECO:0000269|PubMed:9003776}. |
| Modified Residue | |
| Post Translational Modification | PTM: Upon binding its ligands, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain (By similarity). S2 cleavage is probably mediated by the metalloproteases adm-4 and sup-17 (PubMed:16197940). It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it from the cell membrane; S3 cleavage requires a multiprotein gamma-secretase complex, which may include presenilin sel-12 (PubMed:7566091). {ECO:0000250|UniProtKB:P07207, ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:7566091}. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10571181; 10615043; 10778742; 10830967; 11091073; 11099034; 11231151; 11463373; 11562350; 11904378; 12445391; 12529635; 12586701; 12679813; 12702662; 12871705; 12952888; 14551910; 1457827; 14704431; 15056620; 1516818; 15342467; 15791247; 15911573; 15935776; 16507136; 16530049; 16845399; 16884526; 17411345; 17472752; 1769331; 18023123; 18050450; 18501605; 18515547; 18571451; 18692475; 18706403; 18791239; 18828672; 18988854; 19460348; 19564624; 19596901; 19879883; 19923212; 20439776; 20620993; 20668681; 21085631; 21177967; 21367940; 21478858; 21549604; 21834846; 21893079; 22004469; 22209900; 22267497; 22286215; 22508763; 22520465; 22560298; 22718972; 22901814; 23034181; 23305862; 23555887; 23699393; 23788625; 23800452; 23975097; 24439388; 24671263; 24884423; 25487147; 25517099; 25552605; 25762526; 26120834; 26158953; 26483009; 26552888; 26780296; 27185398; 27566309; 2758467; 27705743; 28049659; 29507057; 29775245; 33077477; 33280816; 34795288; 3677168; 3677169; 6593563; 7585963; 7607073; 7607080; 7929443; 8168128; 8658178; 9015263; 9043073; 9307971; 9550713; 9872954; |
| Motif | |
| Gene Encoded By | |
| Mass | 144,079 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |