| IED ID | IndEnz0002004610 |
| Enzyme Type ID | protease004610 |
| Protein Name |
Chromogranin-A CgA Cleaved into: Pancreastatin; Parastatin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor Fragment |
| Gene Name | CHGA |
| Organism | Sus scrofa (Pig) |
| 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 Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | SAAALALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERSHQQKKQSSYEDELSEVLEKQNDQAELKEGTEEASSKEAAEKRGDSKEVEKNDEDADGAKPQASLEPPXXXEAEDQTPGEEEAASTHPLASLPSKKRPGAQAEEDHEGPSQGPVDREKGPSAEQGPQAEREEEEEAEAGEKAVPEEEGPRSEAFDSHPSLGYKEMQRGWPQAPAMDGAGKTGAEEAQPPEGKGAREHSRQEEEEETAGAPQGLFRGGKRGEPAQEEEERLSEEWENAKRWSKMDRLAKELTAEKRLQGEEEEEEEEEDPDRSMKLSFRAPAYGFRGPGLQLRRGWRPSSREDSVEAGLPLQVRXYLEEKKEEEGSANRRPEDQELESLSAIEAELEKVAPQLQSLRRG |
| Enzyme Length | 446 |
| Uniprot Accession Number | P04404 |
| 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: [Parastatin]: Inhibits low calcium-stimulated parathyroid cell secretion.; 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 (5); Disulfide bond (1); Modified residue (11); Non-terminal residue (1); 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;Reference proteome;Secreted;Signal;Sulfation |
| 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 97; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 209; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 286; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 304; /note=Glycine amide; /evidence=ECO:0000269|PubMed:3537810; MOD_RES 319; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 360; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 361; /note=Methionine sulfoxide; /evidence=ECO:0000250|UniProtKB:P10645; MOD_RES 387; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 391; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P05059; MOD_RES 413; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354; MOD_RES 427; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P10354 |
| Post Translational Modification | PTM: O-glycosylated.; PTM: Parathyroid CHGA is sulfated on tyrosine residues, whereas adrenal CHGA seems to be mainly sulfated on oligosaccharide residues. {ECO:0000269|PubMed:2105940}. |
| Signal Peptide | SIGNAL <1..16 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,328 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |