| IED ID | IndEnz0002014318 |
| Enzyme Type ID | protease014318 |
| Protein Name |
Chromogranin-A CgA Cleaved into: Pancreastatin; Beta-granin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor |
| Gene Name | Chga |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MRSSAALALLLCAGQVFALPVNSPMTKGDTKVMKCVLEVISDSLSKPSPMPVSPECLETLQGDERVLSILRHQNLLKELQDLALQGAKERAQQQQQQQQQQQQQQQQQQQQHSSFEDELSEVFENQSPAAKHGDAASEAPSKDTVEKREDSDKGQQDAFEGTTEGPRPQAFPEPKQESSMMGNSQSPGEDTANNTQSPTSLPSQEHGIPQTTEGSERGPSAQQQARKAKQEEKEEEEEEKEEEEEEKEEKAIAREKAGPKEVPTAASSSHFYSGYKKIQKDDDGQSESQAVNGKTGASEAVPSEGKGELEHSQQEEDGEEAMAGPPQGLFPGGKGQELERKQQEEEEEEERLSREWEDKRWSRMDQLAKELTAEKRLEGEDDPDRSMKLSFRARAYGFRDPGPQLRRGWRPSSREDSVEARGDFEEKKEEEGSANRRAEDQELESLSAIEAELEKVAHQLQALRRG |
| Enzyme Length | 466 |
| Uniprot Accession Number | P10354 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: Catestatin inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist. Can induce mast cell migration, degranulation and production of cytokines and chemokines. {ECO:0000250|UniProtKB:P10645}.; FUNCTION: Serpinin regulates granule biogenesis in endocrine cells by up-regulating the transcription of protease nexin 1 (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein degradation in the Golgi complex which in turn promotes granule formation (By similarity). Serpinin and pGlu-serpinin can enhance both myocardial contractility (inotropy) and relaxation (lusitropy) and this cardio-stimulation requires a beta 1-adrenergic receptor/adenylate cyclase/cAMP/PKA pathway (PubMed:22459152). {ECO:0000250|UniProtKB:P26339, ECO:0000269|PubMed:22459152}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (6); Disulfide bond (1); Modified residue (13); Peptide (8); Region (1); Signal peptide (1) |
| Keywords | Amidation;Calcium;Cleavage on pair of basic residues;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Glycoprotein;Oxidation;Phosphoprotein;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744, ECO:0000269|PubMed:3896848}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000269|PubMed:29166604}. Secreted. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions. In pituitary gonadotropes, located in large secretory granules.; SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}. |
| Modified Residue | MOD_RES 114; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P05059"; MOD_RES 215; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P10645"; MOD_RES 288; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P26339"; MOD_RES 312; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 332; /note="Glycine amide"; /evidence="ECO:0000250|UniProtKB:P05059"; MOD_RES 353; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 386; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 387; /note="Methionine sulfoxide"; /evidence="ECO:0000250|UniProtKB:P10645"; MOD_RES 413; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P05059"; MOD_RES 417; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 433; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903"; MOD_RES 441; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000250|UniProtKB:P26339, ECO:0000303|PubMed:22459152"; MOD_RES 447; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:22673903" |
| Post Translational Modification | PTM: CgA is O-glycosylated. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:3896848 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10803489; 11257446; 11696168; 12242039; 12397377; 12438143; 12646581; 12873792; 12902350; 15544843; 17540723; 18483175; 18697842; 18802106; 19372204; 19800883; 21537909; 23674521; 23751870; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,024 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |