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UniProtKB/Swiss-Prot entry P05059


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CMGA_BOVIN
Primary accession number P05059
Secondary accession numbers P79392 Q2KJ52
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on November 1, 1988 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 96)
Name and origin of the protein
Protein name Chromogranin-A [Precursor]
Synonyms CgA
Pituitary secretory protein I
SP-I
Contains Vasostatin-1
Chromostatin
Chromacin
Pancreastatin
WE-14
Catestatin
Gene name
Name: CHGA
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1779968 [NCBI, ExPASy, EBI, Israel, Japan]
Iacangelo A.L., Grimes M., Eiden L.E.;
"The bovine chromogranin A gene: structural basis for hormone regulation and generation of biologically active peptides.";
Mol. Endocrinol. 5:1651-1660(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3755681 [NCBI, ExPASy, EBI, Israel, Japan]
Benedum U.M., Baeuerle P.A., Konecki D.S., Frank R., Powell J., Mallet J., Huttner W.B.;
"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. 5:1495-1502(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/323082a0; PubMed=3018587 [NCBI, ExPASy, EBI, Israel, Japan]
Iacangelo A.L., Affolter H.-U., Eiden L.E., Herbert E., Grimes M.;
"Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues.";
Nature 323:82-86(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3474638 [NCBI, ExPASy, EBI, Israel, Japan]
Ahn T.G., Cohn D.V., Gorr S.U., Ornstein D.L., Kashdan M.A., Levine M.A.;
"Primary structure of bovine pituitary secretory protein I (chromogranin A) deduced from the cDNA sequence.";
Proc. Natl. Acad. Sci. U.S.A. 84:5043-5047(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0014-5793(97)00099-9; PubMed=9074643 [NCBI, ExPASy, EBI, Israel, Japan]
Kang Y.K., Yoo S.H.;
"Identification of the secretory vesicle membrane binding region of chromogranin A.";
FEBS Lett. 404:87-90(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 19-28; 97-106; 134-143; 266-275 AND 350-359, AND MASS SPECTROMETRY.
TISSUE=Chromaffin cell;
DOI=10.1021/bi0300433; PubMed=12795588 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.C., Taylor C.V., Gaucher S.P., Toneff T., Taupenot L., Yasothornsrikul S., Mahata S.K., Sei C., Parmer R.J., Neveu J.M., Lane W.S., Gibson B.W., O'Connor D.T., Hook V.Y.H.;
"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 42:6938-6946(2003).
[8]
PROTEIN SEQUENCE OF 19-38; 97-111 AND 134-139.
PubMed=1986917 [NCBI, ExPASy, EBI, Israel, Japan]
Barbosa J.A., Gill B.M., Takiyyuddin M.A., O'Connor D.T.;
"Chromogranin A: posttranslational modifications in secretory granules.";
Endocrinology 128:174-190(1991).
[9]
PROTEIN SEQUENCE OF 19-45, AND CALCIUM-BINDING.
PubMed=2387861 [NCBI, ExPASy, EBI, Israel, Japan]
Yoo S.H., Albanesi J.P.;
"Ca2(+)-induced conformational change and aggregation of chromogranin A.";
J. Biol. Chem. 265:14414-14421(1990).
[10]
PROTEIN SEQUENCE OF 19-26 AND 266-272.
DOI=10.1016/0014-5793(93)80715-7; PubMed=8243650 [NCBI, ExPASy, EBI, Israel, Japan]
Yoo S.H., Ferretti J.A.;
"Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A.";
FEBS Lett. 334:373-377(1993).
[11]
PROTEIN SEQUENCE OF 142-161, AND SYNTHESIS OF CHROMOSTATIN.
PubMed=1996343 [NCBI, ExPASy, EBI, Israel, Japan]
Galindo E., Rill A., Bader M.-F., Aunis D.;
"Chromostatin, a 20-amino acid peptide derived from chromogranin A, inhibits chromaffin cell secretion.";
Proc. Natl. Acad. Sci. U.S.A. 88:1426-1430(1991).
[12]
ERRATUM.
Galindo E., Rill A., Bader M.-F., Aunis D.;
Proc. Natl. Acad. Sci. U.S.A. 91:832-832(1994).
[13]
PROTEIN SEQUENCE OF 266-331.
PubMed=1710890 [NCBI, ExPASy, EBI, Israel, Japan]
Watkinson A., Jonsson A.C., Davison M., Young J., Lee C.M., Moore S., Dockray G.J.;
"Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla.";
Biochem. J. 276:471-479(1991).
[14]
PROTEIN SEQUENCE OF 266-312.
DOI=10.1016/0167-0115(89)90262-0; PubMed=2756155 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano I., Funakoshi A., Miyasaka K., Ishida K., Makk G., Angwin P., Chang D., Tatemoto K.;
"Isolation and characterization of bovine pancreastatin.";
Regul. Pept. 25:207-213(1989).
[15]
PROTEIN SEQUENCE OF 303-331.
PubMed=8240272 [NCBI, ExPASy, EBI, Israel, Japan]
Watkinson A., Rogers M., Dockray G.J.;
"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. 295:649-654(1993).
[16]
PROTEIN SEQUENCE OF 191-212 (CHROMACIN), PHOSPHORYLATION AT TYR-191, AND GLYCOSYLATION AT SER-204.
TISSUE=Chromaffin cell;
DOI=10.1074/jbc.271.45.28533; PubMed=8910482 [NCBI, ExPASy, EBI, Israel, Japan]
Strub J.-M., Goumon Y., Lugardon K., Capon C., Lopez M., Moniatte M., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
"Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules.";
J. Biol. Chem. 271:28533-28540(1996).
[17]
CHARACTERIZATION OF CATESTATIN.
PubMed=9294131 [NCBI, ExPASy, EBI, Israel, Japan]
Mahata S.K., O'Connor D.T., Mahata M., Yoo S.H., Taupenot L., Wu H., Gill B.M., Parmer R.J.;
"Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist.";
J. Clin. Invest. 100:1623-1633(1997).
[18]
CHARACTERIZATION OF CATESTATIN.
DOI=10.1016/S0196-9781(98)00086-2; PubMed=9786174 [NCBI, ExPASy, EBI, Israel, Japan]
Kennedy B.P., Mahata S.K., O'Connor D.T., Ziegler M.G.;
"Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo.";
Peptides 19:1241-1248(1998).
[19]
CHARACTERIZATION OF VASOSTATIN-1.
DOI=10.1074/jbc.275.15.10745; PubMed=10753865 [NCBI, ExPASy, EBI, Israel, Japan]
Lugardon K., Raffner R., Goumon Y., Corti A., Delmas A., Bulet P., Aunis D., Metz-Boutigue M.-H.;
"Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A.";
J. Biol. Chem. 275:10745-10753(2000).
[20]
GLYCOSYLATION AT SER-185 AND THR-249, PHOSPHORYLATION, AND DISULFIDE BOND.
DOI=10.1006/abio.1999.4244; PubMed=10527498 [NCBI, ExPASy, EBI, Israel, Japan]
Bauer S.H., Zhang X.Y., 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. 274:69-80(1999).
[21]
3D-STRUCTURE MODELING OF CATESTATIN.
DOI=10.1016/S0167-0115(98)00040-8; PubMed=9809795 [NCBI, ExPASy, EBI, Israel, Japan]
Tsigelny I., Mahata S.K., Taupenot L., Preece N.E., Mahata M., Khan I., Parmer R.J., O'Connor D.T.;
"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. 77:43-53(1998).
[22]
STRUCTURE BY NMR OF 368-380.
DOI=10.1016/j.regpep.2003.10.035; PubMed=14759560 [NCBI, ExPASy, EBI, Israel, Japan]
Preece N.E., Nguyen M., Mahata M., Mahata S.K., Mahapatra N.R., Tsigelny I., O'Connor D.T.;
"Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A.";
Regul. Pept. 118:75-87(2004).
Comments
  • FUNCTION: Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.
  • FUNCTION: Chromostatin completely inhibits catecholamine release from chromaffin cells.
  • FUNCTION: Chromacin has antibacterial activity against M.luteus. Not active against E.coli.
  • FUNCTION: Catestatin inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist.
  • FUNCTION: Vasostatin-1 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 T.mentagrophytes.
  • SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules.
  • MASS SPECTROMETRY: Mass=8584.9; Method=MALDI; Range=19-94; Source=PubMed:12795588;.
  • MASS SPECTROMETRY: Mass=2426; Method=MALDI; Range=362-382; Source=PubMed:12795588;.
  • MISCELLANEOUS: Binds calcium with a low-affinity.
  • SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S79270; AAB21297.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79256; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79258; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79260; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79262; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79264; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79266; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S79268; AAB21297.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04012; CAA27636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04298; CAA27841.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16971; AAA30765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U73523; AAC48700.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC105515; AAI05516.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41520; A41520.
RefSeq NP_851348.1; -.
UniGene Bt.49630
3D structure databases
PDB
1CFK; Model; -; A=359-389.[ExPASy / RCSB / EBI]
1N2Y; NMR; -; A=368-380.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CFK; -.
1N2Y; -.
DisProt DP00118; -.
ModBase P05059.
PTM databases
GlycoSuiteDB P05059; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from direct assay from UniProtKB).
GO:0030141; Cellular component: secretory granule (inferred from direct assay from UniProtKB).
GO:0050832; Biological process: defense response to fungus (inferred from direct assay from UniProtKB).
GO:0050829; Biological process: defense response to Gram-negative bacterium (inferred from direct assay from UniProtKB).
GO:0050830; Biological process: defense response to Gram-positive bacterium (inferred from direct assay from UniProtKB).
GO:0045087; Biological process: innate immune response (non-traceable author statement from UniProtKB).
GO:0016525; Biological process: negative regulation of angiogenesis (traceable author statement from UniProtKB).
GO:0046676; Biological process: negative regulation of insulin secretion (inferred from direct assay from UniProtKB).
GO:0030155; Biological process: regulation of cell adhesion (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001819; Chromogranin_AB.
IPR001990; Granin.
Graphical view of domain structure.
PANTHER PTHR10583; Chromogranin_AB; 1.
Pfam PF01271; Granin; 1.
Pfam graphical view of domain structure.
PRINTS PR00659; CHROMOGRANIN.
PROSITE PS00422; GRANINS_1; 1.
PS00423; GRANINS_2; 1.
BLOCKS P05059.
Genome annotation databases
Ensembl ENSBTAG00000009836; Bos taurus. [Contig view]
GeneID 281070; -.
KEGG bta:281070; -.
Phylogenomic databases
HOVERGEN P05059; -.
Other
ProtoNet P05059.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amidation; Antibiotic; Antimicrobial; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Fungicide; Glycoprotein; Phosphoprotein; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   449  431     Chromogranin-A. PRO_0000005398
PEPTIDE   19    94  76     Vasostatin-1. PRO_0000005399
PEPTIDE   142   161  20     Chromostatin. PRO_0000005400
PEPTIDE   191   212  22     Chromacin. PRO_0000005401
PEPTIDE   266   312  47     Pancreastatin. PRO_0000005402
PEPTIDE   334   347  14     WE-14. PRO_0000005403
PEPTIDE   362   382  21     Catestatin. PRO_0000005404
MOD_RES   99    99        Phosphoserine. 
MOD_RES   142   142        Phosphoserine. 
MOD_RES   191   191        Phosphotyrosine. 
MOD_RES   200   200        Phosphoserine (By similarity). 
MOD_RES   295   295        Phosphoserine (By similarity). 
MOD_RES   312   312        Glycine amide (Probable). 
MOD_RES   315   315        Phosphoserine. 
MOD_RES   390   390        Phosphoserine. 
MOD_RES   394   394        Phosphoserine. 
CARBOHYD   185   185        O-linked (GalNAc...) [GlycoSuiteDB]. CAR_000114
CARBOHYD   204   204        O-linked (GalNAc...) [GlycoSuiteDB]. CAR_000203
CARBOHYD   249   249        O-linked (GalNAc...) [GlycoSuiteDB]. CAR_000115
DISULFID   35    56         
CONFLICT   112   112        N -> T (in Ref. 4; AAA30765). 
CONFLICT   136   136        F -> S (in Ref. 2; CAA27636 and 6; AAI05516). 
CONFLICT   154   155        SP -> PQ (in Ref. 3; CAA27841). 
CONFLICT   159   159        P -> R (in Ref. 3; CAA27841). 
CONFLICT   191   191        Y -> H (in Ref. 1; AAB21297). 
CONFLICT   254   254        P -> A (in Ref. 1; AAB21297). 
CONFLICT   293   293        A -> S (in Ref. 5; AAC48700). 
CONFLICT   311   311        R -> H (in Ref. 2, 6; AAI05516 and 13). 
CONFLICT   319   319        E -> K (in Ref. 2, 6; AAI05516 and 13). 
CONFLICT   379   379        G -> R (in Ref. 4; AAA30765). 
CONFLICT   391   391        R -> Q (in Ref. 2; CAA27636 and 6; AAI05516). 
TURN   369   374  6      
STRAND   375   377  3      
Sequence information
Length: 449 AA [This is the length of the unprocessed precursor] Molecular weight: 50015 Da [This is the MW of the unprocessed precursor] CRC64: F304EDC587AA70A3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRSAAVLALL LCAGQVIALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM PVSKECFETL 

        70         80         90        100        110        120 
RGDERILSIL RHQNLLKELQ DLALQGAKER THQQKKHSSY EDELSEVLEK PNDQAEPKEV 

       130        140        150        160        170        180 
TEEVSSKDAA EKRDDFKEVE KSDEDSDGDR PQASPGLGPG PKVEEDNQAP GEEEEAPSNA 

       190        200        210        220        230        240 
HPLASLPSPK YPGPQAKEDS EGPSQGPASR EKGLSAEQGR QTEREEEEEK WEEAEAREKA 

       250        260        270        280        290        300 
VPEEESPPTA AFKPPPSLGN KETQRAAPGW PEDGAGKMGA EEAKPPEGKG EWAHSRQEEE 

       310        320        330        340        350        360 
EMARAPQVLF RGGKSGEPEQ EEQLSKEWED AKRWSKMDQL AKELTAEKRL EGEEEEEEDP 

       370        380        390        400        410        420 
DRSMRLSFRA RGYGFRGPGL QLRRGWRPNS REDSVEAGLP LQVRGYPEEK KEEEGSANRR 

       430        440 
PEDQELESLS AIEAELEKVA HQLEELRRG 

P05059 in FASTA format

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