Record in detail


General Info

  • lamp_id:L03A000270
  • Name:CMGA_BOVIN
  • FullName:Chromogranin-A
  • Source:Bos taurus
  • Mass:10368.1 Da
  • Sequence Length:94 aa
  • Isoelectric Point:7.35
  • Activity:Antimicrobial
  • Sequence
        MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQ
  • Function:Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.

Cross-Linking

  •   Cross-linking
  •   1  Database:Uniprot  P05059
  •   2  Database:AMD  VSTN_BOVIN

Top similar AMPs

  • Top similar AMPs on LAMP
  • 1. L03A000270    From 1 To 94 E-value: 0 Score: 192
        MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQ
  • 2. L01A003291    From 1 To 76 E-value: 4.00001e-41 Score: 158
        LPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQ
  • 3. L12A09956|    From 1 To 46 E-value: 7e-21 Score: 90.9
        PMPVSQECFETLRGHERILSILRHQNLLKELQDLALQGAKERAHQQ
  • 4. L01A003294    From 1 To 30 E-value: 0.000000000005 Score: 61.6
        TLRGDERILSILRHQNLLKELQDLALQGAK
  • 5. L01A003295    From 1 To 24 E-value: 0.00000003 Score: 48.9
        RILSILRHQNLLKELQDLALQGAK

Structure

  •   Domains
  •   1  Name:Chromogranin_AB    Interpro Link:IPR001819
  •   2  Name:Chromogranin_CS    Interpro Link:IPR018054
  •   3  Name:Granin    Interpro Link:IPR001990
  •   Structures
  •   1
    PDB:1CFK
    Method:Model
    Chains:A=359-389
  •   2
    PDB:1N2Y
    Method:NMR
    Chains:A=368-380

Activity

  •   Antibacterial Activities

    •     No MICs found on LAMP database

Toxicity

  •   Toxicity

    •     No toxicity records found on LAMP database

Reference

  •   Reference
  •   [1]  Aunis D.,Bader M.-F.,Rill A.,Galindo E.,
  •   Title:
  •   Journal:Proc. Natl. Acad. Sci. U.S.A., 1994, 91, 832-832  [:]
  •   [2]  Grimes M.,Herbert E.,Eiden L.E.,Affolter H.-U.,Iacangelo A.L.,
  •   Title:Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues.
  •   Journal:Nature, 1986, 323, 82-86  [MEDLINE:86311345]
  •   [3]  Powell J.,Frank R.,Konecki D.S.,Baeuerle P.A.,Benedum U.M.,
  •   Title:The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells.
  •   Journal:EMBO J., 1986, 5, 1495-1502  [MEDLINE:86300648]
  •   [4]  Kashdan M.A.,Ornstein D.L.,Gorr S.U.,Cohn D.V.,Ahn T.G.,
  •   Title:Primary structure of bovine pituitary secretory protein I (chromogranin A) deduced from the cDNA sequence.
  •   Journal:Proc. Natl. Acad. Sci. U.S.A., 1987, 84, 5043-5047  [MEDLINE:87260925]
  •   [5]  Makk G.,Ishida K.,Miyasaka K.,Funakoshi A.,Nakano I.,
  •   Title:Isolation and characterization of bovine pancreastatin.
  •   Journal:Regul. Pept., 1989, 25, 207-213  [MEDLINE:89331945]
  •   [6]  Albanesi J.P.,Yoo S.H.,
  •   Title:Ca2(+)-induced conformational change and aggregation of chromogranin A.
  •   Journal:J. Biol. Chem., 1990, 265, 14414-14421  [MEDLINE:90354431]
  •   [7]  O"Connor D.T.,Takiyyuddin M.A.,Gill B.M.,Barbosa J.A.,
  •   Title:Chromogranin A: posttranslational modifications in secretory granules.
  •   Journal:Endocrinology, 1991, 128, 174-190  [MEDLINE:91099142]
  •   [8]  Aunis D.,Bader M.-F.,Rill A.,Galindo E.,
  •   Title:Chromostatin, a 20-amino acid peptide derived from chromogranin A, inhibits chromaffin cell secretion.
  •   Journal:Proc. Natl. Acad. Sci. U.S.A., 1991, 88, 1426-1430  [MEDLINE:91142185]
  •   [9]  Lee C.M.,Young J.,Davison M.,Jonsson A.C.,Watkinson A.,
  •   Title:Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla.
  •   Journal:Biochem. J., 1991, 276, 471-479  [MEDLINE:91264803]
  •   [10]  Eiden L.E.,Grimes M.,Iacangelo A.L.,
  •   Title:The bovine chromogranin A gene: structural basis for hormone regulation and generation of biologically active peptides.
  •   Journal:Mol. Endocrinol., 1991, 5, 1651-1660  [MEDLINE:92140395]
  •   [11]  Ferretti J.A.,Yoo S.H.,
  •   Title:Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A.
  •   Journal:FEBS Lett., 1993, 334, 373-377  [MEDLINE:94063061]
  •   [12]  Dockray G.J.,Rogers M.,Watkinson A.,
  •   Title: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.
  •   Journal:Biochem. J., 1993, 295, 649-654  [MEDLINE:94059013]
  •   [13]  Lopez M.,Capon C.,Lugardon K.,Goumon Y.,Strub J.-M.,
  •   Title:Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules.
  •   Journal:J. Biol. Chem., 1996, 271, 28533-28540  [MEDLINE:97067080]
  •   [14]  Yoo S.H.,Kang Y.K.,
  •   Title:Identification of the secretory vesicle membrane binding region of chromogranin A.
  •   Journal:FEBS Lett., 1997, 404, 87-90  [MEDLINE:97228583]
  •   [15]  Taupenot L.,Yoo S.H.,Mahata M.,O"Connor D.T.,Mahata S.K.,
  •   Title:Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist.
  •   Journal:J. Clin. Invest., 1997, 100, 1623-1633  [MEDLINE:97439785]
  •   [16]  Mahata M.,Preece N.E.,Taupenot L.,Mahata S.K.,Tsigelny I.,
  •   Title: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.
  •   Journal:Regul. Pept., 1998, 77, 43-53  [MEDLINE:99025667]
  •   [17]  Ziegler M.G.,O"Connor D.T.,Mahata S.K.,Kennedy B.P.,
  •   Title:Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo.
  •   Journal:Peptides, 1998, 19, 1241-1248  [MEDLINE:99000113]
  •   [18]  Przybylski M.,Claeys M.,Van Dongen W.,Zhang X.Y.,Bauer S.H.,
  •   Title:Chromogranin A from bovine adrenal medulla: molecular characterization of glycosylations, phosphorylations, and sequence heterogeneities by mass spectrometry.
  •   Journal:Anal. Biochem., 1999, 274, 69-80  [MEDLINE:99459228]
  •   [19]  Delmas A.,Corti A.,Goumon Y.,Raffner R.,Lugardon K.,
  •   Title:Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A.
  •   Journal:J. Biol. Chem., 2000, 275, 10745-10753  [MEDLINE:20219105]
  •   [20]  Taupenot L.,Toneff T.,Gaucher S.P.,Taylor C.V.,Lee J.C.,
  •   Title: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.
  •   Journal:Biochemistry, 2003, 42, 6938-6946  [MEDLINE:22680607]
  •   [21]  Mahapatra N.R.,Mahata S.K.,Mahata M.,Nguyen M.,Preece N.E.,
  •   Title:Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A.
  •   Journal:Regul. Pept., 2004, 118, 75-87  [PubMed:14759560]

Comments

  •   Comments

    •     No comments found on LAMP database



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