| IED ID | IndEnz0002014320 |
| Enzyme Type ID | protease014320 |
| Protein Name |
Chromogranin-A CgA Cleaved into: Pancreastatin; Beta-granin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin AL26 ; p-Glu serpinin precursor |
| Gene Name | Chga |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MRSTAVLALLLCAGQVFALPVNSPMTKGDTKVMKCVLEVISDSLSKPSPMPVSPECLETLQGDERILSILRHQNLLKELQDLALQGAKERAQQPLKQQQPPKQQQQQQQQQQQEQQHSSFEDELSEVFENQSPDAKHRDAAAEVPSRDTMEKRKDSDKGQQDGFEATTEGPRPQAFPEPNQESPMMGDSESPGEDTATNTQSPTSLPSQEHVDPQATGDSERGLSAQQQARKAKQEEKEEEEEEEAVAREKAGPEEVPTAASSSHFHAGYKAIQKDDGQSDSQAVDGDGKTEASEALPSEGKGELEHSQQEEDGEEAMVGTPQGLFPQGGKGRELEHKQEEEEEEEERLSREWEDKRWSRMDQLAKELTAEKRLEGEDDPDRSMKLSFRTRAYGFRDPGPQLRRGWRPSSREDSVEARSDFEEKKEEEGSANRRAEDQELESLSAIEAELEKVAHQLQALRRG |
| Enzyme Length | 463 |
| Uniprot Accession Number | P26339 |
| 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 (PubMed:21436258). Pyroglutaminated (pGlu)-serpinin exerts an antiapoptotic effect on cells exposed to oxidative stress (PubMed:21537909). {ECO:0000269|PubMed:21436258, ECO:0000269|PubMed:21537909}. |
| 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 | 3D-structure;Amidation;Calcium;Cleavage on pair of basic residues;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Oxidation;Phosphoprotein;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal |
| Interact With | P00441 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted {ECO:0000269|PubMed:12388744}. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions.; SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000269|PubMed:21436258, ECO:0000269|PubMed:21537909}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:21537909}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000269|PubMed:21537909}. |
| Modified Residue | MOD_RES 119; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 220; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 282; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 308; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 329; /note=Glycine amide; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 350; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 383; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 384; /note=Methionine sulfoxide; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 410; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 414; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 430; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 438; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:21537909; MOD_RES 444; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354 |
| Post Translational Modification | PTM: CgA is O-glycosylated. |
| Signal Peptide | SIGNAL 1..18 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 5DMK; |
| Mapped Pubmed ID | 10615124; 10662643; 11130978; 11739954; 12167613; 12372255; 12456641; 12902350; 14715936; 1491299; 14970313; 15100241; 15226823; 15492237; 15590741; 15820695; 16007257; 16049171; 16107537; 16141072; 16219686; 16230531; 16326147; 16369483; 16556729; 16618415; 16943277; 16951258; 16962573; 17024414; 17032746; 17196193; 17400205; 17537793; 17718510; 17974627; 18094025; 18173746; 18177855; 18367602; 18369314; 18554416; 18722481; 18973469; 18987169; 19235715; 19389805; 19394326; 19520754; 19706599; 19726564; 19793886; 19819970; 19952279; 20005907; 20009010; 20139771; 20139986; 20148032; 20364088; 20431921; 20534673; 20637749; 20668031; 20691176; 20875861; 20883684; 21052719; 21113154; 21220053; 21267068; 21383188; 21402740; 21508962; 21670299; 21677750; 21750033; 21820362; 21982232; 21990378; 22132122; 22185794; 22387004; 22406641; 22415354; 22452792; 22535963; 22689348; 22706340; 22766025; 22980982; 23090999; 23266329; 23471965; 23648511; 23831373; 23852729; 24227653; 24236044; 24367558; 24443235; 24821335; 24929016; 25048197; 25053427; 25063677; 25133424; 25257107; 25495347; 25652387; 2573279; 25918232; 25958206; 26023099; 26169832; 26209627; 26431380; 26450967; 26453556; 26552046; 26572539; 26608914; 26743624; 26771085; 26887806; 26944677; 26950855; 27019864; 27510977; 27799464; 27923395; 28071588; 28094771; 28209766; 28220294; 28576773; 28893946; 29178418; 29274006; 29389743; 29432123; 29445148; 29700203; 29976617; 30074235; 30135482; 30590051; 30912742; 30916783; 31092921; 31116975; 31196952; 31604927; 31668390; 31714338; 31781038; 31953387; 32350257; 32404350; 32562431; 32747435; 33028844; 33121008; 33220232; 33500353; 33505018; 33527355; 33658226; 34487921; 34497137; 7979162; 8040254; 8088780; 8275705; 8406464; 8597641; 8617499; 8910482; 8994386; 9063750; 9126746; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,789 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |