AMPDB_114 | Chromogranin-A
PEPTIDE SUMMARY
Chromogranin-A
1 General Description
AMPDB ID: AMPDB_114
Protein Names: Chromogranin-A (CgA) (Pituitary secretory protein I) (SP-I) [Cleaved into: Vasostatin-1; Chromofungin; Chromostatin; Chromacin; Pancreastatin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor]
Protein Family: Chromogranin secretogranin protein family
Gene Name: CHGA
Source Organism: Bos taurus (Bovine)
Protein Length: 449 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 40, 'R': 31, 'N': 9, 'D': 22, 'C': 3, 'Q': 23, 'E': 82, 'G': 34, 'H': 6, 'I': 6, 'L': 36, 'K': 34, 'M': 8, 'F': 6, 'P': 38, 'S': 35, 'T': 9, 'W': 6, 'Y': 4, 'V': 17
Frequencies of Amino Acids
'A': 8.91%, 'R': 6.9%, 'N': 2%, 'D': 4.9%, 'C': 0.67%, 'Q': 5.12%, 'E': 18.26%, 'G': 7.57%, 'H': 1.34%, 'I': 1.34%, 'L': 8.02%, 'K': 7.57%, 'M': 1.78%, 'F': 1.34%, 'P': 8.46%, 'S': 7.8%, 'T': 2%, 'W': 1.34%, 'Y': 0.89%, 'V': 3.79%
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
191
Hydrophilic Amino Acid(s) Count
258
Basic Amino Acid(s) Count
104
Acidic Amino Acid(s) Count
71
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 50014.9 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 56.37 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 73.936 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) -1.202 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.804 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 4.395 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) -38.501 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.167, 0.258, 0.37 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.036 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 38960, 39085 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
A.benhamiae, A.brassicicola, A.fumigatus, B.cereus (Gram-positive), B.megaterium, B.subtilis (Gram-positive), C.albicans, C.glabrata, C.neoformans, C.tropicalis (Gram-negative), E.cloacae (Gram-negative), E.coli (Gram-negative), F.culmorum, K.pneumoniae (Gram-negative), L.monocytogenes (Gram-positive), M.fortuitum (Gram-positive), M.luteus (Gram-negative), N.crassa, S.aureus (Gram-positive), S.cerevisiae, S.pyogenes (Gram-positive), S.typhimurium
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Fungicide, Anti-candida, Anti-yeast, 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: Iacangelo AL, Grimes M, Eiden LE, et al. The bovine chromogranin A gene: structural basis for hormone regulation and generation of biologically active peptides. Mol Endocrinol. 1991;5(11):1651-60. Published 1991 Nov. doi:10.1210/mend-5-11-1651
PMID: 1779968
Citation 2: Benedum UM, Baeuerle PA, Konecki DS, et al. The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells. EMBO J. 1986;5(7):1495-502. Published 1986 Jul. doi:10.1002/j.1460-2075.1986.tb04388.x
PMID: 3755681
Citation 3: Iacangelo A, Affolter HU, Eiden LE, et al. Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues. Nature. 1986;323(6083):82-6. Published 1986 Sep 4-10. doi:10.1038/323082a0
PMID: 3018587
Citation 4: Ahn TG, Cohn DV, Gorr SU, et al. Primary structure of bovine pituitary secretory protein I (chromogranin A) deduced from the cDNA sequence. Proc Natl Acad Sci U S A. 1987;84(14):5043-7. Published 1987 Jul. doi:10.1073/pnas.84.14.5043
PMID: 3474638
Citation 5: Kang YK, Yoo SH, Yoo SH. Identification of the secretory vesicle membrane binding region of chromogranin A. FEBS Lett. 1997;404(1):87-90. Published 1997 Mar 3. doi:10.1016/s0014-5793(97)00099-9
PMID: 9074643
Citation 6: Lee JC, Taylor CV, Gaucher SP, et al. Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin a into active catestatin secreted from neuroendocrine chromaffin cells. Biochemistry. 2003;42(23):6938-46. Published 2003 Jun 17. doi:10.1021/bi0300433
PMID: 12795588
Citation 7: Barbosa JA, Gill BM, Takiyyuddin MA, et al. Chromogranin A: posttranslational modifications in secretory granules. Endocrinology. 1991;128(1):174-90. Published 1991 Jan. doi:10.1210/endo-128-1-174
PMID: 1986917
Citation 8: Yoo SH, Albanesi JP, Albanesi JP. Ca2(+)-induced conformational change and aggregation of chromogranin A. J Biol Chem. 1990;265(24):14414-21. Published 1990 Aug 25. doi:
PMID: 2387861
Citation 9: Yoo SH, Ferretti JA, Ferretti JA. Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A. FEBS Lett. 1993;334(3):373-7. Published 1993 Nov 22. doi:10.1016/0014-5793(93)80715-7
PMID: 8243650
Citation 10: Galindo E, Rill A, Bader MF, et al. Chromostatin, a 20-amino acid peptide derived from chromogranin A, inhibits chromaffin cell secretion. Proc Natl Acad Sci U S A. 1991;88(4):1426-30. Published 1991 Feb 15. doi:10.1073/pnas.88.4.1426
PMID: 1996343
Citation 11: Watkinson A, Jönsson AC, Davison M, et al. Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla. Biochem J. 1991;276 ( Pt 2)(Pt 2):471-9. Published 1991 Jun 1. doi:10.1042/bj2760471
PMID: 1710890
Citation 12: Nakano I, Funakoshi A, Miyasaka K, et al. Isolation and characterization of bovine pancreastatin. Regul Pept. 1989;25(2):207-13. Published 1989 May. doi:10.1016/0167-0115(89)90262-0
PMID: 2756155
Citation 13: Watkinson A, Rogers M, Dockray GJ, et al. Post-translational processing of chromogranin A: differential distribution of phosphorylated variants of pancreastatin and fragments 248-313 and 297-313 in bovine pancreas and ileum. Biochem J. 1993;295 ( Pt 3)(Pt 3):649-54. Published 1993 Nov 1. doi:10.1042/bj2950649
PMID: 8240272
Citation 14: Strub JM, Goumon Y, Lugardon K, et al. Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. J Biol Chem. 1996;271(45):28533-40. Published 1996 Nov 8. doi:10.1074/jbc.271.45.28533
PMID: 8910482
Citation 15: 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 16: 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 17: Kirchmair R, Leitner B, Fischer-Colbrie R, et al. Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues. Biochem J. 1995;310 ( Pt 1)(Pt 1):331-6. Published 1995 Aug 15. doi:10.1042/bj3100331
PMID: 7646465
Citation 18: Mahata SK, O'Connor DT, Mahata M, et al. Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest. 1997;100(6):1623-33. Published 1997 Sep 15. doi:10.1172/JCI119686
PMID: 9294131
Citation 19: Kennedy BP, Mahata SK, O'Connor DT, et al. Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo. Peptides. 1998;19(7):1241-8. Published 1998. doi:10.1016/s0196-9781(98)00086-2
PMID: 9786174
Citation 20: Lugardon K, Raffner R, Goumon Y, et al. Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. J Biol Chem. 2000;275(15):10745-53. Published 2000 Apr 14. doi:10.1074/jbc.275.15.10745
PMID: 10753865
Citation 21: Bauer SH, Zhang XY, Van Dongen W, et al. Chromogranin A from bovine adrenal medulla: molecular characterization of glycosylations, phosphorylations, and sequence heterogeneities by mass spectrometry. Anal Biochem. 1999;274(1):69-80. Published 1999 Oct 1. doi:10.1006/abio.1999.4244
PMID: 10527498
Citation 22: 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 23: Koshimizu H, Cawley NX, Kim T, et al. Serpinin: a novel chromogranin A-derived, secreted peptide up-regulates protease nexin-1 expression and granule biogenesis in endocrine cells. Mol Endocrinol. 2011;25(5):732-44. Published 2011 May. doi:10.1210/me.2010-0124
PMID: 21436258
Citation 24: Tsigelny I, Mahata SK, Taupenot L, et al. Mechanism of action of chromogranin A on catecholamine release: molecular modeling of the catestatin region reveals a beta-strand/loop/beta-strand structure secured by hydrophobic interactions and predictive of activity. Regul Pept. 1998;77(1-3):43-53. Published 1998 Oct 16. doi:10.1016/s0167-0115(98)00040-8
PMID: 9809795
Citation 25: Lugardon K, Chasserot-Golaz S, Kieffer AE, et al. Structural and biological characterization of chromofungin, the antifungal chromogranin A-(47-66)-derived peptide. J Biol Chem. 2001;276(38):35875-82. Published 2001 Sep 21. doi:10.1074/jbc.M104670200
PMID: 11451958
Citation 26: 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
5.2 Protein Sequence Databases
UniProt: P05059
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P05059
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. S79270 GenBank || EMBL
2. S79256 GenBank || EMBL
3. S79258 GenBank || EMBL
4. S79260 GenBank || EMBL
5. S79262 GenBank || EMBL
6. S79264 GenBank || EMBL
7. S79266 GenBank || EMBL
8. S79268 GenBank || EMBL
9. X04012 GenBank || EMBL
10. X04298 GenBank || EMBL
11. M16971 GenBank || EMBL
12. U73523 GenBank || EMBL
13. BC105515 GenBank || EMBL
CCDS: Not found
RefSeq: NP_851348.1
5.5 Protein-Protein Interaction Databases
STRING: 9913.ENSBTAP00000012973
IntAct: Not found
MINT: P05059
DIP: Not found
BioGRID: Not found
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: Not found
5.7 Family & Domain Databases
InterPro: IPR001819, IPR018054, IPR001990
PANTHER: PTHR10583
PROSITE: PS00422, PS00423
5.8 Genome Annotation Databases
Ensembl: Not found
KEGG: bta:281070
5.9 Phylogenomic Databases
GeneTree: Not found
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: Not found




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