Reviewed, UniProtKB/Swiss-Prot P05059 (CMGA_BOVIN)

Names and origin

Protein names

Recommended name:
    Chromogranin-A
      Short name=CgA
Alternative name(s):
    Pituitary secretory protein I
      Short name=SP-I
Cleaved into the following 6 chains:
    1- Recommended name:
            Vasostatin-1
    2- Recommended name:
            Chromostatin
    3- Recommended name:
            Chromacin
    4- Recommended name:
            Pancreastatin
    5- Recommended name:
            WE-14
    6- Recommended name:
            Catestatin

Gene names

Name:

CHGA

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Pancreastatin strongly inhibits glucose induced insulin release from the pancreas. Chromostatin completely inhibits catecholamine release from chromaffin cells. Chromacin has antibacterial activity against M.luteus. Not active against E.coli. Catestatin inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist. 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.
Miscellaneous	Binds calcium with a low-affinity.
Sequence similarities	Belongs to the chromogranin/secretogranin protein family.
Mass spectrometry	Molecular mass is 8584.9 Da from positions 19 - 94. Determined by MALDI. Ref.7 Molecular mass is 2426 Da from positions 362 - 382. Determined by MALDI. Ref.7

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium
Molecular function	Antibiotic Antimicrobial Fungicide
PTM	Amidation Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response to Gram-negative bacterium Ref.19 Inferred from direct assay. Source: UniProtKB defense response to Gram-positive bacterium Ref.19 Inferred from direct assay. Source: UniProtKB defense response to fungus Ref.19 Inferred from direct assay. Source: UniProtKB innate immune response Ref.19 Non-traceable author statement. Source: UniProtKB negative regulation of angiogenesis Ref.19 Traceable author statement. Source: UniProtKB negative regulation of insulin secretion Ref.14 Inferred from direct assay. Source: UniProtKB regulation of cell adhesion Ref.19 Traceable author statement. Source: UniProtKB xenobiotic metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Ref.19 Inferred from direct assay. Source: UniProtKB secretory granule Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.7 Ref.8 Ref.9 Ref.10

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

Amino acid modifications

Modified residue

99

1

Phosphoserine

Modified residue

142

1

Phosphoserine

Modified residue

191

1

Phosphotyrosine Ref.16

Modified residue

200

1

Phosphoserine By similarity

Modified residue

295

1

Phosphoserine By similarity

Modified residue

312

1

Glycine amide Probable

Modified residue

315

1

Phosphoserine

Modified residue

390

1

Phosphoserine

Modified residue

394

1

Phosphoserine

Glycosylation

185

1

O-linked (GalNAc...) Ref.20

CAR_000114

Glycosylation

204

1

O-linked (GalNAc...) Ref.16

CAR_000203

Glycosylation

249

1

O-linked (GalNAc...) Ref.20

CAR_000115

Disulfide bond

35 ↔ 56

Ref.20

Experimental info

Sequence conflict

112

1

N → T in AAA30765. Ref.4

Sequence conflict

136

1

F → S in CAA27636. Ref.2

Sequence conflict

136

1

F → S in AAI05516. Ref.6

Sequence conflict

154 – 155

2

SP → PQ in CAA27841. Ref.3

Sequence conflict

159

1

P → R in CAA27841. Ref.3

Sequence conflict

191

1

Y → H in AAB21297. Ref.1

Sequence conflict

254

1

P → A in AAB21297. Ref.1

Sequence conflict

293

1

A → S in AAC48700. Ref.5

Sequence conflict

311

1

R → H Ref.2

Sequence conflict

311

1

R → H in AAI05516. Ref.6

Sequence conflict

311

1

R → H Ref.13

Sequence conflict

319

1

E → K Ref.2

Sequence conflict

319

1

E → K in AAI05516. Ref.6

Sequence conflict

319

1

E → K Ref.13

Sequence conflict

379

1

G → R in AAA30765. Ref.4

Sequence conflict

391

1

R → Q in CAA27636. Ref.2

Sequence conflict

391

1

R → Q in AAI05516. Ref.6

Secondary structure

1

.

.

.

.

449

Helix Strand Turn

Details...

Turn

369 – 374

6

Beta strand

375 – 377

3

Sequences

	Sequence		Length	Mass (Da)
	P05059-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: F304EDC587AA70A3	FASTA	449	50,015
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The bovine chromogranin A gene: structural basis for hormone regulation and generation of biologically active peptides." Iacangelo A.L., Grimes M., Eiden L.E. Mol. Endocrinol. 5:1651-1660(1991) [PubMed: 1779968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells." Benedum U.M., Baeuerle P.A., Konecki D.S., Frank R., Powell J., Mallet J., Huttner W.B. EMBO J. 5:1495-1502(1986) [PubMed: 3755681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues." Iacangelo A.L., Affolter H.-U., Eiden L.E., Herbert E., Grimes M. Nature 323:82-86(1986) [PubMed: 3018587] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Primary structure of bovine pituitary secretory protein I (chromogranin A) deduced from the cDNA sequence." Ahn T.G., Cohn D.V., Gorr S.U., Ornstein D.L., Kashdan M.A., Levine M.A. Proc. Natl. Acad. Sci. U.S.A. 84:5043-5047(1987) [PubMed: 3474638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Identification of the secretory vesicle membrane binding region of chromogranin A." Kang Y.K., Yoo S.H. FEBS Lett. 404:87-90(1997) [PubMed: 9074643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon.
[7]	"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." 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. Biochemistry 42:6938-6946(2003) [PubMed: 12795588] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-28; 97-106; 134-143; 266-275 AND 350-359, MASS SPECTROMETRY. Tissue: Chromaffin cell.
[8]	"Chromogranin A: posttranslational modifications in secretory granules." Barbosa J.A., Gill B.M., Takiyyuddin M.A., O'Connor D.T. Endocrinology 128:174-190(1991) [PubMed: 1986917] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-38; 97-111 AND 134-139.
[9]	"Ca2(+)-induced conformational change and aggregation of chromogranin A." Yoo S.H., Albanesi J.P. J. Biol. Chem. 265:14414-14421(1990) [PubMed: 2387861] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-45, CALCIUM-BINDING.
[10]	"Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A." Yoo S.H., Ferretti J.A. FEBS Lett. 334:373-377(1993) [PubMed: 8243650] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-26 AND 266-272.
[11]	"Chromostatin, a 20-amino acid peptide derived from chromogranin A, inhibits chromaffin cell secretion." Galindo E., Rill A., Bader M.-F., Aunis D. Proc. Natl. Acad. Sci. U.S.A. 88:1426-1430(1991) [PubMed: 1996343] [Abstract] Cited for: PROTEIN SEQUENCE OF 142-161, SYNTHESIS OF CHROMOSTATIN.
[12]	Erratum Galindo E., Rill A., Bader M.-F., Aunis D. Proc. Natl. Acad. Sci. U.S.A. 91:832-832(1994)
[13]	"Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas and adrenal medulla." Watkinson A., Jonsson A.C., Davison M., Young J., Lee C.M., Moore S., Dockray G.J. Biochem. J. 276:471-479(1991) [PubMed: 1710890] [Abstract] Cited for: PROTEIN SEQUENCE OF 266-331.
[14]	"Isolation and characterization of bovine pancreastatin." Nakano I., Funakoshi A., Miyasaka K., Ishida K., Makk G., Angwin P., Chang D., Tatemoto K. Regul. Pept. 25:207-213(1989) [PubMed: 2756155] [Abstract] Cited for: PROTEIN SEQUENCE OF 266-312.
[15]	"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." Watkinson A., Rogers M., Dockray G.J. Biochem. J. 295:649-654(1993) [PubMed: 8240272] [Abstract] Cited for: PROTEIN SEQUENCE OF 303-331.
[16]	"Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules." Strub J.-M., Goumon Y., Lugardon K., Capon C., Lopez M., Moniatte M., van Dorsselaer A., Aunis D., Metz-Boutigue M.-H. J. Biol. Chem. 271:28533-28540(1996) [PubMed: 8910482] [Abstract] Cited for: PROTEIN SEQUENCE OF 191-212 (CHROMACIN), PHOSPHORYLATION AT TYR-191, GLYCOSYLATION AT SER-204. Tissue: Chromaffin cell.
[17]	"Novel autocrine feedback control of catecholamine release. A discrete chromogranin a fragment is a noncompetitive nicotinic cholinergic antagonist." Mahata S.K., O'Connor D.T., Mahata M., Yoo S.H., Taupenot L., Wu H., Gill B.M., Parmer R.J. J. Clin. Invest. 100:1623-1633(1997) [PubMed: 9294131] [Abstract] Cited for: CHARACTERIZATION OF CATESTATIN.
[18]	"Mechanism of cardiovascular actions of the chromogranin A fragment catestatin in vivo." Kennedy B.P., Mahata S.K., O'Connor D.T., Ziegler M.G. Peptides 19:1241-1248(1998) [PubMed: 9786174] [Abstract] Cited for: CHARACTERIZATION OF CATESTATIN.
[19]	"Antibacterial and antifungal activities of vasostatin-1, the N-terminal fragment of chromogranin A." Lugardon K., Raffner R., Goumon Y., Corti A., Delmas A., Bulet P., Aunis D., Metz-Boutigue M.-H. J. Biol. Chem. 275:10745-10753(2000) [PubMed: 10753865] [Abstract] Cited for: CHARACTERIZATION OF VASOSTATIN-1.
[20]	"Chromogranin A from bovine adrenal medulla: molecular characterization of glycosylations, phosphorylations, and sequence heterogeneities by mass spectrometry." Bauer S.H., Zhang X.Y., Van Dongen W., Claeys M., Przybylski M. Anal. Biochem. 274:69-80(1999) [PubMed: 10527498] [Abstract] Cited for: GLYCOSYLATION AT SER-185 AND THR-249, PHOSPHORYLATION, DISULFIDE BOND.
[21]	"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." Tsigelny I., Mahata S.K., Taupenot L., Preece N.E., Mahata M., Khan I., Parmer R.J., O'Connor D.T. Regul. Pept. 77:43-53(1998) [PubMed: 9809795] [Abstract] Cited for: 3D-STRUCTURE MODELING OF CATESTATIN.
[22]	"Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A." Preece N.E., Nguyen M., Mahata M., Mahata S.K., Mahapatra N.R., Tsigelny I., O'Connor D.T. Regul. Pept. 118:75-87(2004) [PubMed: 14759560] [Abstract] Cited for: STRUCTURE BY NMR OF 368-380.

Cross-references

Sequence databases

EMBLGenBankDDBJ

S79270 , S79256, S79258, S79260, S79262, S79264, S79266, S79268 Genomic DNA. Translation: AAB21297.1.
X04012 mRNA. Translation: CAA27636.1.
X04298 mRNA. Translation: CAA27841.1.
M16971 mRNA. Translation: AAA30765.1.
U73523 mRNA. Translation: AAC48700.1.
BC105515 mRNA. Translation: AAI05516.1.

IPI

IPI00712381.

PIR

A41520.

RefSeq

NP_851348.1.

UniGene

Bt.49630

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CFK	model	-	A	359-389	[»]
1N2Y	NMR	-	A	368-380	[»]

DisProt

DP00118.

ModBase

Search...

PTM databases

GlycoSuiteDB

P05059.

Genome annotation databases

Ensembl

ENSBTAG00000009836. Bos taurus. [Contig view]

GeneID

281070.

KEGG

bta:281070.

Phylogenomic databases

HOVERGEN

P05059.

Family and domain databases

InterPro

IPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]

PANTHER

PTHR10583. Chromogranin_AB. 1 hit.

Pfam

PF01271. Granin. 1 hit.
[Graphical view]

PRINTS

PR00659. CHROMOGRANIN.

PROSITE

PS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CMGA_BOVIN

Accession

Primary (citable) accession number: P05059
Secondary accession number(s): P79392, Q2KJ52

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	November 1, 1988
Last modified:	May 5, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)