AMPDB_148 | Chromogranin-A
PEPTIDE SUMMARY
Chromogranin-A
1 General Description
AMPDB ID: AMPDB_148
Protein Names: 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]
Protein Family: Chromogranin secretogranin protein family
Gene Name: CHGA
Source Organism: Homo sapiens (Human)
Protein Length: 457 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSQECFETLRGDERILSILRHQNLLKELQDLALQGAKERAHQQKKHSGFEDELSEVLENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKSGEATDGARPQALPEPMQESKAEGNNQAPGEEEEEEEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLVDREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVPEEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGAGKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQGLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQLAKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGFRGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQALRRG
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 40, 'R': 28, 'N': 10, 'D': 18, 'C': 3, 'Q': 29, 'E': 90, 'G': 37, 'H': 7, 'I': 6, 'L': 41, 'K': 31, 'M': 9, 'F': 5, 'P': 29, 'S': 38, 'T': 9, 'W': 4, 'Y': 4, 'V': 19
Frequencies of Amino Acids
'A': 8.75%, 'R': 6.13%, 'N': 2.19%, 'D': 3.94%, 'C': 0.66%, 'Q': 6.35%, 'E': 19.69%, 'G': 8.1%, 'H': 1.53%, 'I': 1.31%, 'L': 8.97%, 'K': 6.78%, 'M': 1.97%, 'F': 1.09%, 'P': 6.35%, 'S': 8.32%, 'T': 1.97%, 'W': 0.88%, 'Y': 0.88%, 'V': 4.16%
Missing Amino Acid(s)
No Amino Acid(s) are missing in this protein
Most Occurring Amino Acid(s)
E
Less Occurring Amino Acid(s)
C
Hydrophobic Amino Acid(s) Count
190
Hydrophilic Amino Acid(s) Count
267
Basic Amino Acid(s) Count
108
Acidic Amino Acid(s) Count
66
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 50688.4 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 60.919 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 76.709 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -1.132 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.858 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 4.267 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) -48.396 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.173, 0.249, 0.394 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.028 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 27960, 28085 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
E.coli (Gram-negative), M.luteus (Gram-negative), P.aeruginosa (Gram-negative), S.aureus (Gram-positive)
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Fungicide, Anti-gram-negative, Anti-gram-Positive
4.3 Enzymatic Activity
Not found
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Non-hemolytic, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Konecki DS, Benedum UM, Gerdes HH, et al. The primary structure of human chromogranin A and pancreastatin. J Biol Chem. 1987;262(35):17026-30. Published 1987 Dec 15. doi:
PMID: 2445752
Citation 2: Helman LJ, Ahn TG, Levine MA, et al. Molecular cloning and primary structure of human chromogranin A (secretory protein I) cDNA. J Biol Chem. 1988;263(23):11559-63. Published 1988 Aug 15. doi:
PMID: 3403545
Citation 3: Mouland AJ, Bevan S, White JH, et al. Human chromogranin A gene. Molecular cloning, structural analysis, and neuroendocrine cell-specific expression. J Biol Chem. 1994;269(9):6918-26. Published 1994 Mar 4. doi:
PMID: 8120054
Citation 4: Ota T, Suzuki Y, Nishikawa T, et al. Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004;36(1):40-5. Published 2004 Jan. doi:10.1038/ng1285
PMID: 14702039
Citation 5: Heilig R, Eckenberg R, Petit JL, et al. The DNA sequence and analysis of human chromosome 14. Nature. 2003;421(6923):601-7. Published 2003 Feb 6. doi:10.1038/nature01348
PMID: 12508121
Citation 6: Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004;14(10B):2121-7. Published 2004 Oct. doi:10.1101/gr.2596504
PMID: 15489334
Citation 7: Wilson BS, Phan SH, Lloyd RV, et al. Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence. Regul Pept. 1986;13(3-4):207-23. Published 1986 Feb. doi:10.1016/0167-0115(86)90040-6
PMID: 3704195
Citation 8: Tamamura H, Ohta M, Yoshizawa K, et al. Isolation and characterization of a tumor-derived human protein related to chromogranin A and its in vitro conversion to human pancreastatin-48. Eur J Biochem. 1990;191(1):33-9. Published 1990 Jul 20. doi:10.1111/j.1432-1033.1990.tb19090.x
PMID: 2165909
Citation 9: Sekiya K, Ghatei MA, Minamino N, et al. Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma. FEBS Lett. 1988;228(1):153-6. Published 1988 Feb 8. doi:10.1016/0014-5793(88)80606-9
PMID: 2830133
Citation 10: Curry WJ, Shaw C, Johnston CF, et al. Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour. FEBS Lett. 1992;301(3):319-21. Published 1992 Apr 27. doi:10.1016/0014-5793(92)80266-j
PMID: 1577173
Citation 11: Orr DF, Chen T, Johnsen AH, et al. The spectrum of endogenous human chromogranin A-derived peptides identified using a modified proteomic strategy. Proteomics. 2002;2(11):1586-600. Published 2002 Nov. doi:10.1002/1615-9861(200211)2:11<1586::AID-PROT1586>3.0.CO;2-K
PMID: 12442257
Citation 12: Kirchmair R, Benzer A, Troger J, et al. Molecular characterization of immunoreactivities of peptides derived from chromogranin A (GE-25) and from secretogranin II (secretoneurin) in human and bovine cerebrospinal fluid. Neuroscience. 1994;63(4):1179-87. Published 1994 Dec. doi:10.1016/0306-4522(94)90582-7
PMID: 7535395
Citation 13: Gadroy P, Stridsberg M, Capon C, et al. Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors. J Biol Chem. 1998;273(51):34087-97. Published 1998 Dec 18. doi:10.1074/jbc.273.51.34087
PMID: 9852066
Citation 14: Taylor CV, Taupenot L, Mahata SK, et al. Formation of the catecholamine release-inhibitory peptide catestatin from chromogranin A. Determination of proteolytic cleavage sites in hormone storage granules. J Biol Chem. 2000;275(30):22905-15. Published 2000 Jul 28. doi:10.1074/jbc.M001232200
PMID: 10781584
Citation 15: Giorgianni F, Beranova-Giorgianni S, Desiderio DM, et al. Identification and characterization of phosphorylated proteins in the human pituitary. Proteomics. 2004;4(3):587-98. Published 2004 Mar. doi:10.1002/pmic.200300584
PMID: 14997482
Citation 16: Briolat J, Wu SD, Mahata SK, et al. New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A. Cell Mol Life Sci. 2005;62(3):377-85. Published 2005 Feb. doi:10.1007/s00018-004-4461-9
PMID: 15723172
Citation 17: Beranova-Giorgianni S, Zhao Y, Desiderio DM, et al. Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. Published 2006. doi:10.1007/s11102-006-8916-x
PMID: 16807684
Citation 18: Mahapatra NR, Mahapatra NR. Catestatin is a novel endogenous peptide that regulates cardiac function and blood pressure. Cardiovasc Res. 2008;80(3):330-8. Published 2008 Dec 1. doi:10.1093/cvr/cvn155
PMID: 18541522
Citation 19: Nilsson J, Rüetschi U, Halim A, et al. Enrichment of glycopeptides for glycan structure and attachment site identification. Nat Methods. 2009;6(11):809-11. Published 2009 Nov. doi:10.1038/nmeth.1392
PMID: 19838169
Citation 20: Mahata SK, Mahata M, Fung MM, et al. Catestatin: a multifunctional peptide from chromogranin A. Regul Pept. 2010;162(1-3):33-43. Published 2010 Jun 8. doi:10.1016/j.regpep.2010.01.006
PMID: 20116404
Citation 21: Aung G, Niyonsaba F, Ushio H, et al. Catestatin, a neuroendocrine antimicrobial peptide, induces human mast cell migration, degranulation and production of cytokines and chemokines. Immunology. 2011;132(4):527-39. Published 2011 Apr. doi:10.1111/j.1365-2567.2010.03395.x
PMID: 21214543
Citation 22: Halim A, Rüetschi U, Larson G, et al. LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins. J Proteome Res. 2013;12(2):573-84. Published 2013 Feb 1. doi:10.1021/pr300963h
PMID: 23234360
Citation 23: Mohseni S, Emtenani S, Emtenani S, et al. Antioxidant properties of a human neuropeptide and its protective effect on free radical-induced DNA damage. J Pept Sci. 2014;20(6):429-37. Published 2014 Jun. doi:10.1002/psc.2634
PMID: 24723458
Citation 24: Bian Y, Song C, Cheng K, et al. An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014;96:253-62. Published 2014 Jan 16. doi:10.1016/j.jprot.2013.11.014
PMID: 24275569
Citation 25: Preece NE, Nguyen M, Mahata M, et al. Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A. Regul Pept. 2004;118(1-2):75-87. Published 2004 Apr 15. doi:10.1016/j.regpep.2003.10.035
PMID: 14759560
Citation 26: Wen G, Mahata SK, Cadman P, et al. Both rare and common polymorphisms contribute functional variation at CHGA, a regulator of catecholamine physiology. Am J Hum Genet. 2004;74(2):197-207. Published 2004 Feb. doi:10.1086/381399
PMID: 14740315
Citation 27: Mahata SK, Mahata M, Wen G, et al. The catecholamine release-inhibitory 'catestatin' fragment of chromogranin a: naturally occurring human variants with different potencies for multiple chromaffin cell nicotinic cholinergic responses. Mol Pharmacol. 2004;66(5):1180-91. Published 2004 Nov. doi:10.1124/mol.104.002139
PMID: 15326220
Citation 28: Rao F, Wen G, Gayen JR, et al. Catecholamine release-inhibitory peptide catestatin (chromogranin A(352-372)): naturally occurring amino acid variant Gly364Ser causes profound changes in human autonomic activity and alters risk for hypertension. Circulation. 2007;115(17):2271-81. Published 2007 May 1. doi:10.1161/CIRCULATIONAHA.106.628859
PMID: 17438154
Citation 29: Biswas N, Vaingankar SM, Mahata M, et al. Proteolytic cleavage of human chromogranin a containing naturally occurring catestatin variants: differential processing at catestatin region by plasmin. Endocrinology. 2008;149(2):749-57. Published 2008 Feb. doi:10.1210/en.2007-0838
PMID: 17991725
5.2 Protein Sequence Databases
UniProt: P10645
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P10645
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. J03483 GenBank || EMBL
2. J03915 GenBank || EMBL
3. U03749 GenBank || EMBL
4. U03742 GenBank || EMBL
5. U03743 GenBank || EMBL
6. U03744 GenBank || EMBL
7. U03748 GenBank || EMBL
8. U03745 GenBank || EMBL
9. U03746 GenBank || EMBL
10. U03747 GenBank || EMBL
11. BT006869 GenBank || EMBL
12. AK223381 GenBank || EMBL
13. AL117192 GenBank || EMBL
14. AK313757 GenBank || EMBL
15. CH471061 GenBank || EMBL
16. BC001059 GenBank || EMBL
17. BC006459 GenBank || EMBL
18. BC009384 GenBank || EMBL
19. BC012755 GenBank || EMBL
5.5 Protein-Protein Interaction Databases
IntAct: P10645
MINT: P10645
DIP: Not found
BioGRID: 107538
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: Not found
5.7 Family & Domain Databases
PANTHER: PTHR10583
PROSITE: PS00422, PS00423
5.8 Genome Annotation Databases
KEGG: hsa:1113
5.9 Phylogenomic Databases
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: P10645




© 2023 B&BL, DoAS, IIIT-A, UP-211015, India