HORDB

General Information

ID: hor006113
Uniprot ID: P10645
Protein name: GV-19
Gene name: CHGA
Organism: Homo sapiens (Human)
Family: Chromogranin/secretogranin protein family
Source: Human
Expression: GE-25 is found in the brain.
Disease: Diseases associated with CHGA include Acinar Cell Carcinoma and Neuroendocrine Carcinoma.
Comments: NA
Taxonomy: Homo (genus), Homininae (subfamily), Hominidae (family), Hominoidea (superfamily), Catarrhini (parvorder), Simiiformes (infraorder), Haplorrhini (suborder), Primates (order), Euarchontoglires (superorder), Boreoeutheria, Eutheria, Theria, Mammalia (class), Amniota, Tetrapoda, Dipnotetrapodomorpha, Sarcopterygii (superclass), Euteleostomi, Teleostomi, Gnathostomata, Vertebrata, Craniata (subphylum), Chordata (phylum), Deuterostomia, Bilateria, Eumetazoa, Metazoa (kingdom), Opisthokonta, Eukaryota (superkingdom), cellular organisms
GO MF: NA
GO BP: GO:0002026 regulation of the force of heart contraction; GO:0002551 mast cell chemotaxis; GO:0006996 organelle organization; GO:0008217 regulation of blood pressure; GO:0031640 killing of cells of another organism; GO:0033366 protein localization to secretory granule; GO:0033604 negative regulation of catecholamine secretion; GO:0042742 defense response to bacterium; GO:0043303 mast cell degranulation; GO:0045087 innate immune response; GO:0045576 mast cell activation; GO:0046676 negative regulation of insulin secretion; GO:0050829 defense response to Gram-negative bacterium; GO:0050830 defense response to Gram-positive bacterium; GO:0050832 defense response to fungus; GO:0060452 positive regulation of cardiac muscle contraction; GO:0071880 adenylate cyclase-activating adrenergic receptor signaling pathway; GO:0086030 adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation; GO:1900738 positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; GO:1901899 positive regulation of relaxation of cardiac muscle; GO:2000707 positive regulation of dense core granule biogenesis
GO CC: GO:0005576 extracellular region; GO:0005615 extracellular space; GO:0030133 transport vesicle; GO:0030141 secretory granule; GO:0031410 cytoplasmic vesicle; GO:0042583 chromaffin granule; GO:0048471 perinuclear region of cytoplasm; GO:0098992 neuronal dense core vesicle

Sequence Information

Sequence: GWRPSSREDSLEAGLPLQV
Length: 19
Propeptide: MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG
Signal peptide: MRSAAVLALLLCAGQVTA
Modification: T6 Phosphoserine;T10 Phosphoserine
Glycosylation: NA
Mutagenesis: NA

Activity

Function: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; [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, 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).
Mechanism: Binds calcium with a low-affinity.
Cross BBB: NA
Target: NA
Target Unid: NA
IC50: NA
EC50: NA
ED50: NA
kd: NA
Half life: NA

Structure

Disulfide bond: NA
Structure ID: AF-P10645-F1(AlphaFold_DB_ID)

Structure: (PDB_ID-from https://www.rcsb.org/; AlphaFold_DB_ID-from https://alphafold.ebi.ac.uk/; hordbxxxxxx_AF2.pdb was predicted structure by AlphaFold2; hordbxxxxxx_ESM.pdb was predicted structure by ESMFold)

hor006113_AF2.pdb

hor006113_ESM.pdb

Physical Information

Mass:	241855	Formula:	C91H145N27O30
Absent amino acids:	CFHIKMNTY	Common amino acids:	LS
pI:	4.43	Basic residues:	2
Polar residues:	5	Hydrophobic residues:	6
Hydrophobicity:	-67.89	Boman Index:	-4310
Half-Life:	30 hour	Half-Life Yeast:	>20 hour
Half-Life E.Coli:	>10 hour	Aliphatic Index	82.11
Instability Index:	10011.58	Extinction Coefficient cystines:	5500
Absorbance 280nm:	305.56

Literature

PubMed ID: 2445752
Title: The primary structure of human chromogranin A and pancreastatin.
PubMed ID: 3403545
Title: Molecular cloning and primary structure of human chromogranin A (secretory protein I) cDNA.
PubMed ID: 8120054
Title: Human chromogranin A gene. Molecular cloning, structural analysis, and neuroendocrine cell-specific expression.
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 12508121
Title: The DNA sequence and analysis of human chromosome 14.
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 3704195
Title: Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence.
PubMed ID: 2165909
Title: Isolation and characterization of a tumor-derived human protein related to chromogranin A and its in vitro conversion to human pancreastatin-48.
PubMed ID: 2830133
Title: Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma.
PubMed ID: 1577173
Title: Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour.
PubMed ID: 12442257
Title: The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy.
PubMed ID: 7535395
Title: Molecular characterization of immunoreactivities of peptides derived from chromogranin A (GE-25) and from secretogranin II (secretoneurin) in human and bovine cerebrospinal fluid.
PubMed ID: 9852066
Title: Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
PubMed ID: 10781584
Title: Formation of the catecholamine release-inhibitory peptide catestatin from chromogranin A. Determination of proteolytic cleavage sites in hormone storage granules.
PubMed ID: 14997482
Title: Identification and characterization of phosphorylated proteins in the human pituitary.
PubMed ID: 15723172
Title: New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A.
PubMed ID: 16807684
Title: Phosphoproteomic analysis of the human pituitary.
PubMed ID: 18541522
Title: Catestatin is a novel endogenous peptide that regulates cardiac function and blood pressure.
PubMed ID: 19838169
Title: Enrichment of glycopeptides for glycan structure and attachment site identification.
PubMed ID: 20116404
Title: Catestatin: a multifunctional peptide from chromogranin A.
PubMed ID: 21214543
Title: Catestatin, a neuroendocrine antimicrobial peptide, induces human mast cell migration, degranulation and production of cytokines and chemokines.
PubMed ID: 23234360
Title: LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
PubMed ID: 24723458
Title: Antioxidant properties of a human neuropeptide and its protective effect on free radical-induced DNA damage.
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome
PubMed ID: 14759560
Title:
PubMed ID: 14740315
Title:
PubMed ID: 1532
Title: