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Showing Protein Chromogranin-A (HMDBP14018)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14018
Secondary Accession Numbers None
Name Chromogranin-A
Synonyms
  1. CgA
  2. Pituitary secretory protein I
  3. SP-I
Gene Name CHGA
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Strongly inhibits glucose induced insulin release from the pancreas.Completely inhibits catecholamine release from chromaffin cells.Has antibacterial activity against M.luteus. Not active against E.coli.Inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist (PubMed:9294131 and PubMed:9786174). Displays antibacterial activity against Gram-positive bacteria M.luteus and B.megaterium, and Gram-negative bacteria E.coli, and antifungal activity against a variety of filamentous fungi including A.fumigatus, N.hematococca, F.culmorum, F.oxyporum, T. mentagrophytes and several forms of Candida: C.albicans, C.tropicalis, C.glabrata and C.neoform (PubMed:15723172). Can induce mast cell migration, degranulation and production of cytokines and chemokines (By similarity).Has antibacterial activity against Gram-positive bacteria M.luteus, B.megaterium. Not active against Gram-positive bacteria B.cereus, B.subtilis, S.pyogenes, M.fortuitum, S.aureus and L.monocytogenes and against Gram-negative bacteria E.coli, E.cloacae, S.typhimurium, K.pneumoniae and P.aeruginosa. Possesses antifungal activity against N.crassa, A.fumigatus, A.brassicicola, N.hematococca, F.culmorum and F.oxyporum and against the yeast S.cerevisiae and C.albicans. Inactive against A.benhamiae.Has antifungal activity against N.crassa, A.fumigatus, A.brassicicola, N.hematococca, F.culmorum, F.oxyporum, A.benhamiae, C.neoformans, as well as against yeasts C.albicans, and C.tropicalis. Seems to be inactive against C.glabrata. Interacts with the fungal cell wall, crosses the plasma membrane and accumulates in fungal cells where it inhibits calcineurin activity.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 (PubMed:21436258).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
defense response to bacterium
adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation
disruption by host of symbiont cell wall
mast cell activation
mast cell chemotaxis
negative regulation of catecholamine secretion
negative regulation of hormone secretion
negative regulation of protein serine/threonine phosphatase activity
positive regulation of dense core granule biogenesis
defense response to Gram-positive bacterium
antifungal humoral response
antimicrobial humoral immune response mediated by antimicrobial peptide
negative regulation of insulin secretion
innate immune response
negative regulation of angiogenesis
mast cell degranulation
killing of cells of other organism
defense response to Gram-negative bacterium
regulation of cell adhesion
defense response to fungus
Cellular Component
chromaffin granule
neuronal dense core vesicle
secretory granule
extracellular region
extracellular space
transport vesicle
Molecular Function
calcium ion binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 449
Molecular Weight 50014.54
Theoretical pI 4.731
Pfam Domain Function
Signals
  • 1-18;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P05059
UniProtKB/Swiss-Prot Entry Name CMGA_BOVIN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Preece NE, Nguyen M, Mahata M, Mahata SK, Mahapatra NR, Tsigelny I, O'Connor DT: Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A. Regul Pept. 2004 Apr 15;118(1-2):75-87. [PubMed:14759560 ]
  2. Iacangelo AL, Grimes M, Eiden LE: The bovine chromogranin A gene: structural basis for hormone regulation and generation of biologically active peptides. Mol Endocrinol. 1991 Nov;5(11):1651-60. doi: 10.1210/mend-5-11-1651. [PubMed:1779968 ]
  3. Benedum UM, Baeuerle PA, Konecki DS, Frank R, Powell J, Mallet J, Huttner WB: 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 Jul;5(7):1495-502. [PubMed:3755681 ]
  4. Iacangelo A, Affolter HU, Eiden LE, Herbert E, Grimes M: Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues. Nature. 1986 Sep 4-10;323(6083):82-6. doi: 10.1038/323082a0. [PubMed:3018587 ]
  5. Ahn TG, Cohn DV, Gorr SU, Ornstein DL, Kashdan MA, Levine MA: Primary structure of bovine pituitary secretory protein I (chromogranin A) deduced from the cDNA sequence. Proc Natl Acad Sci U S A. 1987 Jul;84(14):5043-7. doi: 10.1073/pnas.84.14.5043. [PubMed:3474638 ]
  6. Kang YK, Yoo SH: Identification of the secretory vesicle membrane binding region of chromogranin A. FEBS Lett. 1997 Mar 3;404(1):87-90. doi: 10.1016/s0014-5793(97)00099-9. [PubMed:9074643 ]
  7. Lee JC, Taylor CV, Gaucher SP, Toneff T, Taupenot L, Yasothornsrikul S, Mahata SK, Sei C, Parmer RJ, Neveu JM, Lane WS, Gibson BW, O'Connor DT, Hook VY: 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 Jun 17;42(23):6938-46. doi: 10.1021/bi0300433. [PubMed:12795588 ]
  8. Barbosa JA, Gill BM, Takiyyuddin MA, O'Connor DT: Chromogranin A: posttranslational modifications in secretory granules. Endocrinology. 1991 Jan;128(1):174-90. doi: 10.1210/endo-128-1-174. [PubMed:1986917 ]
  9. Yoo SH, Ferretti JA: Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A. FEBS Lett. 1993 Nov 22;334(3):373-7. doi: 10.1016/0014-5793(93)80715-7. [PubMed:8243650 ]
  10. Galindo E, Rill A, Bader MF, Aunis D: Chromostatin, a 20-amino acid peptide derived from chromogranin A, inhibits chromaffin cell secretion. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1426-30. doi: 10.1073/pnas.88.4.1426. [PubMed:1996343 ]
  11. Watkinson A, Jonsson AC, Davison M, Young J, Lee CM, Moore S, Dockray GJ: Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla. Biochem J. 1991 Jun 1;276 ( Pt 2):471-9. doi: 10.1042/bj2760471. [PubMed:1710890 ]
  12. Nakano I, Funakoshi A, Miyasaka K, Ishida K, Makk G, Angwin P, Chang D, Tatemoto K: Isolation and characterization of bovine pancreastatin. Regul Pept. 1989 May;25(2):207-13. doi: 10.1016/0167-0115(89)90262-0. [PubMed:2756155 ]
  13. Watkinson A, Rogers M, Dockray GJ: 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 Nov 1;295 ( Pt 3):649-54. doi: 10.1042/bj2950649. [PubMed:8240272 ]
  14. Strub JM, Goumon Y, Lugardon K, Capon C, Lopez M, Moniatte M, Van Dorsselaer A, Aunis D, Metz-Boutigue MH: Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. J Biol Chem. 1996 Nov 8;271(45):28533-40. doi: 10.1074/jbc.271.45.28533. [PubMed:8910482 ]
  15. Kirchmair R, Benzer A, Troger J, Miller C, Marksteiner J, Saria A, Gasser RW, Hogue-Angeletti R, Fischer-Colbrie R, Winkler H: 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 Dec;63(4):1179-87. doi: 10.1016/0306-4522(94)90582-7. [PubMed:7535395 ]
  16. Kirchmair R, Leitner B, Fischer-Colbrie R, Marksteiner J, Hogue-Angeletti R, Winkler H: Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues. Biochem J. 1995 Aug 15;310 ( Pt 1):331-6. doi: 10.1042/bj3100331. [PubMed:7646465 ]
  17. Mahata SK, O'Connor DT, Mahata M, Yoo SH, Taupenot L, Wu H, Gill BM, Parmer RJ: Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist. J Clin Invest. 1997 Sep 15;100(6):1623-33. doi: 10.1172/JCI119686. [PubMed:9294131 ]
  18. Kennedy BP, Mahata SK, O'Connor DT, Ziegler MG: Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo. Peptides. 1998;19(7):1241-8. doi: 10.1016/s0196-9781(98)00086-2. [PubMed:9786174 ]
  19. Lugardon K, Raffner R, Goumon Y, Corti A, Delmas A, Bulet P, Aunis D, Metz-Boutigue MH: Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A. J Biol Chem. 2000 Apr 14;275(15):10745-53. doi: 10.1074/jbc.275.15.10745. [PubMed:10753865 ]
  20. Bauer SH, Zhang XY, Van Dongen W, Claeys M, Przybylski M: Chromogranin A from bovine adrenal medulla: molecular characterization of glycosylations, phosphorylations, and sequence heterogeneities by mass spectrometry. Anal Biochem. 1999 Oct 1;274(1):69-80. doi: 10.1006/abio.1999.4244. [PubMed:10527498 ]
  21. Briolat J, Wu SD, Mahata SK, Gonthier B, Bagnard D, Chasserot-Golaz S, Helle KB, Aunis D, Metz-Boutigue MH: New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A. Cell Mol Life Sci. 2005 Feb;62(3):377-85. doi: 10.1007/s00018-004-4461-9. [PubMed:15723172 ]
  22. Koshimizu H, Cawley NX, Kim T, Yergey AL, Loh YP: Serpinin: a novel chromogranin A-derived, secreted peptide up-regulates protease nexin-1 expression and granule biogenesis in endocrine cells. Mol Endocrinol. 2011 May;25(5):732-44. doi: 10.1210/me.2010-0124. Epub 2011 Mar 24. [PubMed:21436258 ]
  23. Tsigelny I, Mahata SK, Taupenot L, Preece NE, Mahata M, Khan I, Parmer RJ, O'Connor DT: 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 Oct 16;77(1-3):43-53. doi: 10.1016/s0167-0115(98)00040-8. [PubMed:9809795 ]
  24. Lugardon K, Chasserot-Golaz S, Kieffer AE, Maget-Dana R, Nullans G, Kieffer B, Aunis D, Metz-Boutigue MH: Structural and biological characterization of chromofungin, the antifungal chromogranin A-(47-66)-derived peptide. J Biol Chem. 2001 Sep 21;276(38):35875-82. doi: 10.1074/jbc.M104670200. Epub 2001 Jul 12. [PubMed:11451958 ]