CMGA_BOVIN
ID CMGA_BOVIN Reviewed; 449 AA.
AC P05059; P79392; Q2KJ52;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 188.
DE RecName: Full=Chromogranin-A {ECO:0000303|PubMed:3018587, ECO:0000303|PubMed:3755681};
DE Short=CgA;
DE AltName: Full=Pituitary secretory protein I {ECO:0000303|PubMed:3474638};
DE Short=SP-I;
DE Contains:
DE RecName: Full=Vasostatin-1 {ECO:0000303|PubMed:10753865};
DE Contains:
DE RecName: Full=Chromofungin {ECO:0000303|PubMed:11451958};
DE Contains:
DE RecName: Full=Chromostatin {ECO:0000303|PubMed:1996343};
DE Contains:
DE RecName: Full=Chromacin {ECO:0000303|PubMed:8910482};
DE Contains:
DE RecName: Full=Pancreastatin {ECO:0000303|PubMed:2756155};
DE Contains:
DE RecName: Full=WE-14 {ECO:0000250|UniProtKB:P10645};
DE Contains:
DE RecName: Full=Catestatin {ECO:0000303|PubMed:14759560};
DE Contains:
DE RecName: Full=GE-25 {ECO:0000303|PubMed:7646465};
DE Contains:
DE RecName: Full=Serpinin-RRG;
DE Contains:
DE RecName: Full=Serpinin {ECO:0000303|PubMed:21436258};
DE Contains:
DE RecName: Full=p-Glu serpinin precursor;
DE Flags: Precursor;
GN Name=CHGA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1779968; DOI=10.1210/mend-5-11-1651;
RA Iacangelo A.L., Grimes M., Eiden L.E.;
RT "The bovine chromogranin A gene: structural basis for hormone regulation
RT and generation of biologically active peptides.";
RL Mol. Endocrinol. 5:1651-1660(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3755681; DOI=10.1002/j.1460-2075.1986.tb04388.x;
RA Benedum U.M., Baeuerle P.A., Konecki D.S., Frank R., Powell J., Mallet J.,
RA Huttner W.B.;
RT "The primary structure of bovine chromogranin A: a representative of a
RT class of acidic secretory proteins common to a variety of peptidergic
RT cells.";
RL EMBO J. 5:1495-1502(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3018587; DOI=10.1038/323082a0;
RA Iacangelo A.L., Affolter H.-U., Eiden L.E., Herbert E., Grimes M.;
RT "Bovine chromogranin A sequence and distribution of its messenger RNA in
RT endocrine tissues.";
RL Nature 323:82-86(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3474638; DOI=10.1073/pnas.84.14.5043;
RA Ahn T.G., Cohn D.V., Gorr S.U., Ornstein D.L., Kashdan M.A., Levine M.A.;
RT "Primary structure of bovine pituitary secretory protein I (chromogranin A)
RT deduced from the cDNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5043-5047(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9074643; DOI=10.1016/s0014-5793(97)00099-9;
RA Kang Y.K., Yoo S.H.;
RT "Identification of the secretory vesicle membrane binding region of
RT chromogranin A.";
RL FEBS Lett. 404:87-90(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 19-28; 97-106; 134-143; 266-275 AND 350-359, AND MASS
RP SPECTROMETRY.
RC TISSUE=Chromaffin cell;
RX PubMed=12795588; DOI=10.1021/bi0300433;
RA Lee J.C., Taylor C.V., Gaucher S.P., Toneff T., Taupenot L.,
RA Yasothornsrikul S., Mahata S.K., Sei C., Parmer R.J., Neveu J.M.,
RA Lane W.S., Gibson B.W., O'Connor D.T., Hook V.Y.H.;
RT "Primary sequence characterization of catestatin intermediates and peptides
RT defines proteolytic cleavage sites utilized for converting chromogranin A
RT into active catestatin secreted from neuroendocrine chromaffin cells.";
RL Biochemistry 42:6938-6946(2003).
RN [8]
RP PROTEIN SEQUENCE OF 19-38; 97-111 AND 134-139.
RX PubMed=1986917; DOI=10.1210/endo-128-1-174;
RA Barbosa J.A., Gill B.M., Takiyyuddin M.A., O'Connor D.T.;
RT "Chromogranin A: posttranslational modifications in secretory granules.";
RL Endocrinology 128:174-190(1991).
RN [9]
RP PROTEIN SEQUENCE OF 19-45, AND CALCIUM-BINDING.
RX PubMed=2387861; DOI=10.1016/s0021-9258(18)77318-3;
RA Yoo S.H., Albanesi J.P.;
RT "Ca2(+)-induced conformational change and aggregation of chromogranin A.";
RL J. Biol. Chem. 265:14414-14421(1990).
RN [10]
RP PROTEIN SEQUENCE OF 19-26 AND 266-272.
RX PubMed=8243650; DOI=10.1016/0014-5793(93)80715-7;
RA Yoo S.H., Ferretti J.A.;
RT "Nature of the pH-induced conformational changes and exposure of the C-
RT terminal region of chromogranin A.";
RL FEBS Lett. 334:373-377(1993).
RN [11]
RP PROTEIN SEQUENCE OF 142-161, AND FUNCTION (CHROMOSTATIN).
RX PubMed=1996343; DOI=10.1073/pnas.88.4.1426;
RA Galindo E., Rill A., Bader M.-F., Aunis D.;
RT "Chromostatin, a 20-amino acid peptide derived from chromogranin A,
RT inhibits chromaffin cell secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1426-1430(1991).
RN [12]
RP ERRATUM OF PUBMED:1996343.
RA Galindo E., Rill A., Bader M.-F., Aunis D.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:832-832(1994).
RN [13]
RP PROTEIN SEQUENCE OF 266-331.
RX PubMed=1710890; DOI=10.1042/bj2760471;
RA Watkinson A., Jonsson A.C., Davison M., Young J., Lee C.M., Moore S.,
RA Dockray G.J.;
RT "Heterogeneity of chromogranin A-derived peptides in bovine gut, pancreas
RT and adrenal medulla.";
RL Biochem. J. 276:471-479(1991).
RN [14]
RP PROTEIN SEQUENCE OF 266-312, AMIDATION AT GLY-312, AND FUNCTION
RP (PANCREASTATIN).
RX PubMed=2756155; DOI=10.1016/0167-0115(89)90262-0;
RA Nakano I., Funakoshi A., Miyasaka K., Ishida K., Makk G., Angwin P.,
RA Chang D., Tatemoto K.;
RT "Isolation and characterization of bovine pancreastatin.";
RL Regul. Pept. 25:207-213(1989).
RN [15]
RP PROTEIN SEQUENCE OF 303-331.
RX PubMed=8240272; DOI=10.1042/bj2950649;
RA Watkinson A., Rogers M., Dockray G.J.;
RT "Post-translational processing of chromogranin A: differential distribution
RT of phosphorylated variants of pancreastatin and fragments 248-313 and 297-
RT 313 in bovine pancreas and ileum.";
RL Biochem. J. 295:649-654(1993).
RN [16]
RP PROTEIN SEQUENCE OF 191-212, PHOSPHORYLATION AT TYR-191, GLYCOSYLATION AT
RP SER-204, AND FUNCTION (CHROMACIN).
RC TISSUE=Chromaffin cell;
RX PubMed=8910482; DOI=10.1074/jbc.271.45.28533;
RA Strub J.-M., Goumon Y., Lugardon K., Capon C., Lopez M., Moniatte M.,
RA van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
RT "Antibacterial activity of glycosylated and phosphorylated chromogranin A-
RT derived peptide 173-194 from bovine adrenal medullary chromaffin
RT granules.";
RL J. Biol. Chem. 271:28533-28540(1996).
RN [17]
RP PROTEIN SEQUENCE OF 351-363, MASS SPECTROMETRY, PROTEOLYTIC PROCESSING,
RP OXIDATION AT MET-364, AND SUBCELLULAR LOCATION.
RX PubMed=10781584; DOI=10.1074/jbc.m001232200;
RA Taylor C.V., Taupenot L., Mahata S.K., Mahata M., Wu H.,
RA Yasothornsrikul S., Toneff T., Caporale C., Jiang Q., Parmer R.J.,
RA Hook V.Y., O'Connor D.T.;
RT "Formation of the catecholamine release-inhibitory peptide catestatin from
RT chromogranin A. Determination of proteolytic cleavage sites in hormone
RT storage granules.";
RL J. Biol. Chem. 275:22905-22915(2000).
RN [18]
RP CHARACTERIZATION OF GE-25, AND TISSUE SPECIFICITY.
RX PubMed=7535395; DOI=10.1016/0306-4522(94)90582-7;
RA Kirchmair R., Benzer A., Troger J., Miller C., Marksteiner J., Saria A.,
RA Gasser R.W., Hogue-Angeletti R., Fischer-Colbrie R., Winkler H.;
RT "Molecular characterization of immunoreactivities of peptides derived from
RT chromogranin A (GE-25) and from secretogranin II (secretoneurin) in human
RT and bovine cerebrospinal fluid.";
RL Neuroscience 63:1179-1187(1994).
RN [19]
RP CHARACTERIZATION OF GE-25, AND TISSUE SPECIFICITY.
RX PubMed=7646465; DOI=10.1042/bj3100331;
RA Kirchmair R., Leitner B., Fischer-Colbrie R., Marksteiner J.,
RA Hogue-Angeletti R., Winkler H.;
RT "Large variations in the proteolytic formation of a chromogranin A-derived
RT peptide (GE-25) in neuroendocrine tissues.";
RL Biochem. J. 310:331-336(1995).
RN [20]
RP FUNCTION (CATESTATIN).
RX PubMed=9294131; DOI=10.1172/jci119686;
RA Mahata S.K., O'Connor D.T., Mahata M., Yoo S.H., Taupenot L., Wu H.,
RA Gill B.M., Parmer R.J.;
RT "Novel autocrine feedback control of catecholamine release. A discrete
RT chromogranin a fragment is a noncompetitive nicotinic cholinergic
RT antagonist.";
RL J. Clin. Invest. 100:1623-1633(1997).
RN [21]
RP FUNCTION (CATESTATIN).
RX PubMed=9786174; DOI=10.1016/s0196-9781(98)00086-2;
RA Kennedy B.P., Mahata S.K., O'Connor D.T., Ziegler M.G.;
RT "Mechanism of cardiovascular actions of the chromogranin A fragment
RT catestatin in vivo.";
RL Peptides 19:1241-1248(1998).
RN [22]
RP FUNCTION (VASOSTATIN-1).
RX PubMed=10753865; DOI=10.1074/jbc.275.15.10745;
RA Lugardon K., Raffner R., Goumon Y., Corti A., Delmas A., Bulet P.,
RA Aunis D., Metz-Boutigue M.-H.;
RT "Antibacterial and antifungal activities of vasostatin-1, the N-terminal
RT fragment of chromogranin A.";
RL J. Biol. Chem. 275:10745-10753(2000).
RN [23]
RP GLYCOSYLATION AT SER-185 AND THR-249, PHOSPHORYLATION AT SER-99; SER-142;
RP SER-315; SER-390 AND SER-394, AND DISULFIDE BOND.
RX PubMed=10527498; DOI=10.1006/abio.1999.4244;
RA Bauer S.H., Zhang X.Y., Van Dongen W., Claeys M., Przybylski M.;
RT "Chromogranin A from bovine adrenal medulla: molecular characterization of
RT glycosylations, phosphorylations, and sequence heterogeneities by mass
RT spectrometry.";
RL Anal. Biochem. 274:69-80(1999).
RN [24]
RP FUNCTION (CATESTATIN).
RX PubMed=15723172; DOI=10.1007/s00018-004-4461-9;
RA Briolat J., Wu S.D., Mahata S.K., Gonthier B., Bagnard D.,
RA Chasserot-Golaz S., Helle K.B., Aunis D., Metz-Boutigue M.H.;
RT "New antimicrobial activity for the catecholamine release-inhibitory
RT peptide from chromogranin A.";
RL Cell. Mol. Life Sci. 62:377-385(2005).
RN [25]
RP FUNCTION (SERPININ).
RX PubMed=21436258; DOI=10.1210/me.2010-0124;
RA Koshimizu H., Cawley N.X., Kim T., Yergey A.L., Loh Y.P.;
RT "Serpinin: a novel chromogranin A-derived, secreted peptide up-regulates
RT protease nexin-1 expression and granule biogenesis in endocrine cells.";
RL Mol. Endocrinol. 25:732-744(2011).
RN [26]
RP 3D-STRUCTURE MODELING OF CATESTATIN.
RX PubMed=9809795; DOI=10.1016/s0167-0115(98)00040-8;
RA Tsigelny I., Mahata S.K., Taupenot L., Preece N.E., Mahata M., Khan I.,
RA Parmer R.J., O'Connor D.T.;
RT "Mechanism of action of chromogranin A on catecholamine release: molecular
RT modeling of the catestatin region reveals a beta-strand/loop/beta-strand
RT structure secured by hydrophobic interactions and predictive of activity.";
RL Regul. Pept. 77:43-53(1998).
RN [27]
RP STRUCTURE BY NMR OF 65-88, FUNCTION (CHROMOFUNGIN), AND SUBCELLULAR
RP LOCATION.
RX PubMed=11451958; DOI=10.1074/jbc.m104670200;
RA Lugardon K., Chasserot-Golaz S., Kieffer A.E., Maget-Dana R., Nullans G.,
RA Kieffer B., Aunis D., Metz-Boutigue M.H.;
RT "Structural and biological characterization of chromofungin, the antifungal
RT chromogranin A-(47-66)-derived peptide.";
RL J. Biol. Chem. 276:35875-35882(2001).
RN [28]
RP STRUCTURE BY NMR OF 368-380.
RX PubMed=14759560; DOI=10.1016/j.regpep.2003.10.035;
RA Preece N.E., Nguyen M., Mahata M., Mahata S.K., Mahapatra N.R.,
RA Tsigelny I., O'Connor D.T.;
RT "Conformational preferences and activities of peptides from the
RT catecholamine release-inhibitory (catestatin) region of chromogranin A.";
RL Regul. Pept. 118:75-87(2004).
CC -!- FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin
CC release from the pancreas. {ECO:0000269|PubMed:2756155}.
CC -!- FUNCTION: [Chromostatin]: Completely inhibits catecholamine release
CC from chromaffin cells. {ECO:0000269|PubMed:1996343}.
CC -!- FUNCTION: [Chromacin]: Has antibacterial activity against M.luteus. Not
CC active against E.coli. {ECO:0000269|PubMed:8910482}.
CC -!- FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin
CC cells and noradrenergic neurons by acting as a non-competitive
CC nicotinic cholinergic antagonist (PubMed:9294131 and PubMed:9786174).
CC Displays antibacterial activity against Gram-positive bacteria M.luteus
CC and B.megaterium, and Gram-negative bacteria E.coli, and antifungal
CC activity against a variety of filamentous fungi including A.fumigatus,
CC N.hematococca, F.culmorum, F.oxyporum, T. mentagrophytes and several
CC forms of Candida: C.albicans, C.tropicalis, C.glabrata and C.neoform
CC (PubMed:15723172). Can induce mast cell migration, degranulation and
CC production of cytokines and chemokines (By similarity).
CC {ECO:0000250|UniProtKB:P10645, ECO:0000269|PubMed:15723172,
CC ECO:0000269|PubMed:9294131, ECO:0000269|PubMed:9786174}.
CC -!- FUNCTION: [Vasostatin-1]: Has antibacterial activity against Gram-
CC positive bacteria M.luteus, B.megaterium. Not active against Gram-
CC positive bacteria B.cereus, B.subtilis, S.pyogenes, M.fortuitum,
CC S.aureus and L.monocytogenes and against Gram-negative bacteria E.coli,
CC E.cloacae, S.typhimurium, K.pneumoniae and P.aeruginosa. Possesses
CC antifungal activity against N.crassa, A.fumigatus, A.brassicicola,
CC N.hematococca, F.culmorum and F.oxyporum and against the yeast
CC S.cerevisiae and C.albicans. Inactive against A.benhamiae.
CC {ECO:0000269|PubMed:10753865}.
CC -!- FUNCTION: [Chromofungin]: Has antifungal activity against N.crassa,
CC A.fumigatus, A.brassicicola, N.hematococca, F.culmorum, F.oxyporum,
CC A.benhamiae, C.neoformans, as well as against yeasts C.albicans, and
CC C.tropicalis. Seems to be inactive against C.glabrata. Interacts with
CC the fungal cell wall, crosses the plasma membrane and accumulates in
CC fungal cells where it inhibits calcineurin activity.
CC {ECO:0000269|PubMed:11451958}.
CC -!- FUNCTION: [Serpinin]: Regulates granule biogenesis in endocrine cells
CC by up-regulating the transcription of protease nexin 1 (SERPINE2) via a
CC cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein
CC degradation in the Golgi complex which in turn promotes granule
CC formation (PubMed:21436258). {ECO:0000269|PubMed:21436258}.
CC -!- SUBUNIT: Interacts with SCG3. {ECO:0000250|UniProtKB:P26339}.
CC -!- SUBCELLULAR LOCATION: [Serpinin]: Secreted
CC {ECO:0000269|PubMed:10781584}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin
CC localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:P10354}. Cytoplasmic vesicle, secretory vesicle,
CC neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted
CC {ECO:0000269|PubMed:11451958}. Note=Associated with the secretory
CC granule membrane through direct interaction to SCG3 that in turn binds
CC to cholesterol-enriched lipid rafts in intragranular conditions. In
CC pituitary gonadotropes, located in large secretory granules.
CC {ECO:0000250|UniProtKB:P10354}.
CC -!- TISSUE SPECIFICITY: Highest concentration of GE-25 found in adrenal
CC medulla with lower levels present in the pituitary, the intestinal
CC mucosa and the pancreas. Also found in the brain.
CC {ECO:0000269|PubMed:7535395, ECO:0000269|PubMed:7646465}.
CC -!- PTM: In secretory granules, is attacked at both N- and C-terminal sides
CC by proteolytic enzymes generating numerous peptides of various
CC activities. Proteolytic processing can give rise to additional longer
CC forms of catestatin peptides which display a less potent catecholamine
CC release-inhibitory activity (PubMed:10781584).
CC {ECO:0000269|PubMed:10781584, ECO:0000269|PubMed:8240272,
CC ECO:0000305|PubMed:11451958}.
CC -!- MASS SPECTROMETRY: [Vasostatin-1]: Mass=8584.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12795588};
CC -!- MASS SPECTROMETRY: [Catestatin]: Mass=2426; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12795588};
CC -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; S79270; AAB21297.1; -; Genomic_DNA.
DR EMBL; S79256; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; S79258; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; S79260; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; S79262; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; S79264; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; S79266; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; S79268; AAB21297.1; JOINED; Genomic_DNA.
DR EMBL; X04012; CAA27636.1; -; mRNA.
DR EMBL; X04298; CAA27841.1; -; mRNA.
DR EMBL; M16971; AAA30765.1; -; mRNA.
DR EMBL; U73523; AAC48700.1; -; mRNA.
DR EMBL; BC105515; AAI05516.1; -; mRNA.
DR PIR; A41520; A41520.
DR RefSeq; NP_851348.1; NM_181005.2.
DR PDB; 1N2Y; NMR; -; A=368-380.
DR PDBsum; 1N2Y; -.
DR AlphaFoldDB; P05059; -.
DR SMR; P05059; -.
DR MINT; P05059; -.
DR STRING; 9913.ENSBTAP00000012973; -.
DR GlyConnect; 92; 8 O-Linked glycans (3 sites).
DR iPTMnet; P05059; -.
DR PaxDb; P05059; -.
DR PeptideAtlas; P05059; -.
DR PRIDE; P05059; -.
DR GeneID; 281070; -.
DR KEGG; bta:281070; -.
DR CTD; 1113; -.
DR eggNOG; ENOG502RZBD; Eukaryota.
DR HOGENOM; CLU_050861_0_0_1; -.
DR InParanoid; P05059; -.
DR OrthoDB; 1127088at2759; -.
DR TreeFam; TF336596; -.
DR EvolutionaryTrace; P05059; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0042583; C:chromaffin granule; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0086030; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation; IBA:GO_Central.
DR GO; GO:0019732; P:antifungal humoral response; IMP:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0052338; P:disruption by host of symbiont cell wall; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0045576; P:mast cell activation; ISS:UniProtKB.
DR GO; GO:0002551; P:mast cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; TAS:UniProtKB.
DR GO; GO:0033604; P:negative regulation of catecholamine secretion; IDA:UniProtKB.
DR GO; GO:0046888; P:negative regulation of hormone secretion; IDA:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:UniProtKB.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
DR DisProt; DP00118; -.
DR InterPro; IPR001819; Chromogranin_AB.
DR InterPro; IPR018054; Chromogranin_CS.
DR InterPro; IPR001990; Granin.
DR PANTHER; PTHR10583; PTHR10583; 1.
DR Pfam; PF01271; Granin; 2.
DR PRINTS; PR00659; CHROMOGRANIN.
DR PROSITE; PS00422; GRANINS_1; 1.
DR PROSITE; PS00423; GRANINS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial; Calcium;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Fungicide; Glycoprotein;
KW Oxidation; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:12795588,
FT ECO:0000269|PubMed:1986917, ECO:0000269|PubMed:2387861,
FT ECO:0000269|PubMed:8243650"
FT CHAIN 19..449
FT /note="Chromogranin-A"
FT /id="PRO_0000005398"
FT PEPTIDE 19..94
FT /note="Vasostatin-1"
FT /evidence="ECO:0000269|PubMed:12795588"
FT /id="PRO_0000005399"
FT PEPTIDE 65..88
FT /note="Chromofungin"
FT /evidence="ECO:0000269|PubMed:11451958"
FT /id="PRO_0000432587"
FT PEPTIDE 142..161
FT /note="Chromostatin"
FT /evidence="ECO:0000269|PubMed:1996343"
FT /id="PRO_0000005400"
FT PEPTIDE 191..212
FT /note="Chromacin"
FT /evidence="ECO:0000269|PubMed:8910482"
FT /id="PRO_0000005401"
FT PEPTIDE 266..312
FT /note="Pancreastatin"
FT /evidence="ECO:0000269|PubMed:2756155"
FT /id="PRO_0000005402"
FT PEPTIDE 334..347
FT /note="WE-14"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT /id="PRO_0000005403"
FT PEPTIDE 362..382
FT /note="Catestatin"
FT /evidence="ECO:0000269|PubMed:12795588"
FT /id="PRO_0000005404"
FT PEPTIDE 385..409
FT /note="GE-25"
FT /evidence="ECO:0000303|PubMed:7646465"
FT /id="PRO_0000432673"
FT PEPTIDE 421..449
FT /note="Serpinin-RRG"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT /id="PRO_0000432674"
FT PEPTIDE 421..446
FT /note="Serpinin"
FT /evidence="ECO:0000303|PubMed:21436258"
FT /id="PRO_0000432675"
FT PEPTIDE 424..446
FT /note="p-Glu serpinin precursor"
FT /evidence="ECO:0000250|UniProtKB:P26339"
FT /id="PRO_0000432676"
FT REGION 87..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT MOD_RES 191
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8910482"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 312
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:2756155"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT MOD_RES 364
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:10781584"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT CARBOHYD 185
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT /id="CAR_000114"
FT CARBOHYD 204
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:8910482"
FT /id="CAR_000203"
FT CARBOHYD 249
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:10527498"
FT /id="CAR_000115"
FT DISULFID 35..56
FT /evidence="ECO:0000269|PubMed:10527498"
FT CONFLICT 112
FT /note="N -> T (in Ref. 4; AAA30765)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="F -> S (in Ref. 2; CAA27636 and 6; AAI05516)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="SP -> PQ (in Ref. 3; CAA27841)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="P -> R (in Ref. 3; CAA27841)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="Y -> H (in Ref. 1; AAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="P -> A (in Ref. 1; AAB21297)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="A -> S (in Ref. 5; AAC48700)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> H (in Ref. 2; CAA27636, 6; AAI05516 and 13; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="E -> K (in Ref. 2; CAA27636, 6; AAI05516 and 13; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="G -> R (in Ref. 4; AAA30765)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="R -> Q (in Ref. 2; CAA27636 and 6; AAI05516)"
FT /evidence="ECO:0000305"
FT TURN 369..374
FT /evidence="ECO:0007829|PDB:1N2Y"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:1N2Y"
SQ SEQUENCE 449 AA; 50015 MW; F304EDC587AA70A3 CRC64;
MRSAAVLALL LCAGQVIALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM PVSKECFETL
RGDERILSIL RHQNLLKELQ DLALQGAKER THQQKKHSSY EDELSEVLEK PNDQAEPKEV
TEEVSSKDAA EKRDDFKEVE KSDEDSDGDR PQASPGLGPG PKVEEDNQAP GEEEEAPSNA
HPLASLPSPK YPGPQAKEDS EGPSQGPASR EKGLSAEQGR QTEREEEEEK WEEAEAREKA
VPEEESPPTA AFKPPPSLGN KETQRAAPGW PEDGAGKMGA EEAKPPEGKG EWAHSRQEEE
EMARAPQVLF RGGKSGEPEQ EEQLSKEWED AKRWSKMDQL AKELTAEKRL EGEEEEEEDP
DRSMRLSFRA RGYGFRGPGL QLRRGWRPNS REDSVEAGLP LQVRGYPEEK KEEEGSANRR
PEDQELESLS AIEAELEKVA HQLEELRRG
