| IED ID | IndEnz0002004779 |
| Enzyme Type ID | protease004779 |
| Protein Name |
Chromogranin-A CgA Pituitary secretory protein I SP-I Cleaved into: Vasostatin-1 Vasostatin I ; Vasostatin-2 Vasostatin II ; EA-92; ES-43; Pancreastatin; SS-18; WA-8; WE-14; LF-19; Catestatin SL21 ; AL-11; GV-19; GR-44; ER-37; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor |
| Gene Name | CHGA |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG |
| Enzyme Length | 457 |
| Uniprot Accession Number | P10645 |
| 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 (PubMed:15326220). Displays antibacterial activity against Gram-positive bacteria S.aureus and M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa (PubMed:15723172 and PubMed:24723458). Can induce mast cell migration, degranulation and production of cytokines and chemokines (PubMed:21214543). Acts as a potent scavenger of free radicals in vitro (PubMed:24723458). May play a role in the regulation of cardiac function and blood pressure (PubMed:18541522). {ECO:0000269|PubMed:15326220, ECO:0000269|PubMed:15723172, ECO:0000269|PubMed:21214543, ECO:0000269|PubMed:24723458, ECO:0000303|PubMed:18541522}.; 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 | Beta strand (2); Chain (1); Compositional bias (7); Disulfide bond (1); Glycosylation (3); Helix (1); Modified residue (16); Natural variant (12); Peptide (18); Region (3); Sequence conflict (14); Signal peptide (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;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 142; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P05059"; MOD_RES 194; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:P05059"; MOD_RES 203; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16807684"; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:9852066"; MOD_RES 270; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:9852066"; MOD_RES 300; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16807684"; MOD_RES 319; /note="Glycine amide"; /evidence="ECO:0000269|PubMed:2165909, ECO:0000269|PubMed:2830133"; MOD_RES 322; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:14997482, ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:24275569"; MOD_RES 333; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:9852066"; MOD_RES 371; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P10354"; MOD_RES 372; /note="Methionine sulfoxide"; /evidence="ECO:0000269|PubMed:17991725"; MOD_RES 398; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P05059"; MOD_RES 402; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16807684"; MOD_RES 424; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P10354"; MOD_RES 438; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P10354"; MOD_RES 456; /note="Arginine amide"; /evidence="ECO:0000269|PubMed:12442257" |
| Post Translational Modification | PTM: Sulfated on tyrosine residues and/or contains sulfated glycans.; PTM: O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:9852066}.; PTM: Proteolytic processing gives rise to an additional longer form of catestatin (residues 358-390) which displays a less potent catecholamine release-inhibitory activity (PubMed:10781584). Plasmin-mediated proteolytic processing can give rise to additional shorter and longer forms of catestatin peptides (PubMed:17991725). {ECO:0000269|PubMed:10781584, ECO:0000269|PubMed:17991725}. |
| Signal Peptide | SIGNAL 1..18; /evidence="ECO:0000269|PubMed:12442257, ECO:0000269|PubMed:3704195" |
| Structure 3D | NMR spectroscopy (2) |
| Cross Reference PDB | 1LV4; 6R2X; |
| Mapped Pubmed ID | 12091348; 12165659; 12397377; 12432071; 12438141; 12438152; 12456801; 12687271; 12692477; 12826904; 14734634; 14968443; 15337252; 15462496; 15542860; 15648545; 15788643; 15956083; 16007257; 16151967; 16330879; 16450720; 16504480; 17003646; 17032650; 17060047; 17126478; 17293489; 17379958; 17438105; 17438153; 17510497; 17578828; 17599769; 17718510; 17889508; 17929277; 17985422; 18046660; 18061980; 18158567; 18185531; 18235090; 18262756; 18271679; 18329114; 18374882; 18432188; 18549247; 18549351; 18591442; 18635750; 18721831; 18724010; 18771509; 18832606; 18981630; 19017515; 19058139; 19090560; 19321999; 19337629; 19366853; 19520754; 19652998; 19724850; 19747727; 19794299; 19855234; 19943077; 20033364; 20043075; 20087896; 20103720; 20113265; 20139771; 20172008; 20193177; 20213742; 20335134; 20550951; 20640434; 20663522; 20807312; 20833163; 20930149; 20965217; 21044118; 21046454; 21046455; 21061160; 21080056; 21115933; 21325453; 21349414; 21357258; 21362443; 21431800; 21463431; 21478104; 21483253; 21508845; 21551321; 21558123; 21825034; 21872447; 21884005; 21900206; 21918574; 21980038; 21994954; 22035982; 22343505; 22388654; 22449227; 22487376; 22524436; 22529895; 22674297; 22699394; 22720672; 23105094; 23153859; 23173843; 23206950; 23271036; 23292839; 23361940; 23418554; 23423580; 23426642; 23588348; 23688154; 23702300; 23939195; 23956349; 24210828; 24239002; 24260544; 24338022; 24375395; 24375481; 24523932; 24631953; 24741024; 24821335; 25012947; 25077558; 25099181; 25174455; 25220535; 25275071; 25392232; 25501094; 25532001; 25651748; 25810338; 25848973; 25894842; 25958206; 26186986; 26211667; 26299616; 26359267; 26403073; 26556564; 26608723; 26683597; 26684860; 26750135; 26850182; 27203389; 27304618; 27324226; 27683038; 27771336; 28095720; 28190616; 28209766; 28254729; 28334992; 28351413; 28397784; 28406540; 28501118; 28667172; 28685598; 28870943; 28886122; 29033257; 29274006; 29723285; 29737901; 29858590; 30074235; 30401690; 30467710; 30658195; 30702115; 30714297; 30768573; 30887724; 31091213; 31091854; 31207989; 31755501; 32436949; 32739447; 33121008; 33141811; 33485291; 33835984; 34453940; 34620125; 34647168; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,688 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |