| IED ID | IndEnz0002019190 |
| Enzyme Type ID | protease019190 |
| Protein Name |
Chromogranin-A CgA Pituitary secretory protein I SP-I Cleaved into: Vasostatin-1; Chromofungin; Chromostatin; Chromacin; Pancreastatin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor |
| Gene Name | CHGA |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG |
| Enzyme Length | 449 |
| Uniprot Accession Number | P05059 |
| 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. {ECO:0000269|PubMed:2756155}.; FUNCTION: [Chromostatin]: Completely inhibits catecholamine release from chromaffin cells. {ECO:0000269|PubMed:1996343}.; FUNCTION: [Chromacin]: Has antibacterial activity against M.luteus. Not active against E.coli. {ECO:0000269|PubMed:8910482}.; FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:9294131 and PubMed:9786174). Displays antibacterial activity against Gram-positive bacteria M.luteus and B.megaterium, and Gram-negative bacteria E.coli, and antifungal activity against a variety of filamentous fungi including A.fumigatus, N.hematococca, F.culmorum, F.oxyporum, T. mentagrophytes and several forms of Candida: C.albicans, C.tropicalis, C.glabrata and C.neoform (PubMed:15723172). Can induce mast cell migration, degranulation and production of cytokines and chemokines (By similarity). {ECO:0000250|UniProtKB:P10645, ECO:0000269|PubMed:15723172, ECO:0000269|PubMed:9294131, ECO:0000269|PubMed:9786174}.; FUNCTION: [Vasostatin-1]: Has antibacterial activity against Gram-positive bacteria M.luteus, B.megaterium. Not active against Gram-positive bacteria B.cereus, B.subtilis, S.pyogenes, M.fortuitum, S.aureus and L.monocytogenes and against Gram-negative bacteria E.coli, E.cloacae, S.typhimurium, K.pneumoniae and P.aeruginosa. Possesses antifungal activity against N.crassa, A.fumigatus, A.brassicicola, N.hematococca, F.culmorum and F.oxyporum and against the yeast S.cerevisiae and C.albicans. Inactive against A.benhamiae. {ECO:0000269|PubMed:10753865}.; FUNCTION: [Chromofungin]: Has antifungal activity against N.crassa, A.fumigatus, A.brassicicola, N.hematococca, F.culmorum, F.oxyporum, A.benhamiae, C.neoformans, as well as against yeasts C.albicans, and C.tropicalis. Seems to be inactive against C.glabrata. Interacts with the fungal cell wall, crosses the plasma membrane and accumulates in fungal cells where it inhibits calcineurin activity. {ECO:0000269|PubMed:11451958}.; 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). {ECO:0000269|PubMed:21436258}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (1); Chain (1); Compositional bias (5); Disulfide bond (1); Glycosylation (3); Modified residue (15); Peptide (11); Region (1); Sequence conflict (17); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Amidation;Antibiotic;Antimicrobial;Calcium;Cleavage on pair of basic residues;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Fungicide;Glycoprotein;Oxidation;Phosphoprotein;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000269|PubMed:10781584}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P10354}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted {ECO:0000269|PubMed:11451958}. 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. {ECO:0000250|UniProtKB:P10354}. |
| Modified Residue | MOD_RES 99; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10527498; MOD_RES 142; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10527498; MOD_RES 191; /note=Phosphotyrosine; /evidence=ECO:0000269|PubMed:8910482; MOD_RES 200; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 215; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 295; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 312; /note=Glycine amide; /evidence=ECO:0000269|PubMed:2756155; MOD_RES 315; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10527498; MOD_RES 325; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 363; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 364; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:10781584; MOD_RES 390; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10527498; MOD_RES 394; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:10527498; MOD_RES 416; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 430; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354 |
| Post Translational Modification | PTM: In secretory granules, is attacked at both N- and C-terminal sides by proteolytic enzymes generating numerous peptides of various activities. Proteolytic processing can give rise to additional longer forms of catestatin peptides which display a less potent catecholamine release-inhibitory activity (PubMed:10781584). {ECO:0000269|PubMed:10781584, ECO:0000269|PubMed:8240272, ECO:0000305|PubMed:11451958}. |
| Signal Peptide | SIGNAL 1..18; /evidence="ECO:0000269|PubMed:12795588, ECO:0000269|PubMed:1986917, ECO:0000269|PubMed:2387861, ECO:0000269|PubMed:8243650" |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 1N2Y; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,015 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |