| IED ID | IndEnz0002014308 |
| Enzyme Type ID | protease014308 |
| Protein Name |
Chromogranin-A CgA Cleaved into: Pancreastatin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor |
| Gene Name | CHGA |
| Organism | Equus caballus (Horse) |
| 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 Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | MRSAVVLALLLCAGQVIALPVNSPMDTGDTEVMKCIVEVISDTLSKPSPVPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAPQQKHSRLEDELAEVLEKQNHQAELKEVTEEALSEDAAEARGDSKEVEENGEDADGARPQAALEPEQESRVEDAQAPGEEKEAINTHSPTRLPSQKHPDPQAEGDSDSPSQGLVDREKGLGAERGQQAKREEEEDEAGEKADAEEEGPTAAFNPHPSLSYKIRKGESWSEALVVDGARKTGAEEAQPPEGQGEREHSRQEEEEEEETAGASRGLFRGGKSRELEQEKEQERLSKEWEDAKRWSKMDQLAKELTAEKRLEGEDEEEDDPDRSMKLSFRARAYGFRGPGLQLRRGWRPSSREDSIEAGLPPPVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG |
| Enzyme Length | 448 |
| Uniprot Accession Number | Q9XS63 |
| 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. {ECO:0000250|UniProtKB:P26339}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (6); Disulfide bond (1); Modified residue (12); Peptide (7); Region (2); Signal peptide (1) |
| Keywords | Amidation;Calcium;Cleavage on pair of basic residues;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Oxidation;Phosphoprotein;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | 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}.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P10354}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted {ECO:0000250|UniProtKB:P10354}. 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 197; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 258; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 288; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 308; /note=Glycine amide; /evidence=ECO:0000250; MOD_RES 311; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 324; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 362; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 363; /note=Methionine sulfoxide; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 389; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 393; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 415; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 429; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354 |
| Post Translational Modification | PTM: O-glycosylated. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,861 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |