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Chromogranin-A (CgA) (Pituitary secretory protein I) (SP-I) [Cleaved into: Vasostatin-1; Chromofungin; Chromostatin; Chromacin; Pancreastatin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin; p-Glu serpinin precursor]

 CMGA_BOVIN              Reviewed;         449 AA.
P05059; P79392; Q2KJ52;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
27-SEP-2017, entry version 164.
RecName: Full=Chromogranin-A {ECO:0000303|PubMed:3018587, ECO:0000303|PubMed:3755681};
Short=CgA;
AltName: Full=Pituitary secretory protein I {ECO:0000303|PubMed:3474638};
Short=SP-I;
Contains:
RecName: Full=Vasostatin-1 {ECO:0000303|PubMed:10753865};
Contains:
RecName: Full=Chromofungin {ECO:0000303|PubMed:11451958};
Contains:
RecName: Full=Chromostatin {ECO:0000303|PubMed:1996343};
Contains:
RecName: Full=Chromacin {ECO:0000303|PubMed:8910482};
Contains:
RecName: Full=Pancreastatin {ECO:0000303|PubMed:2756155};
Contains:
RecName: Full=WE-14 {ECO:0000250|UniProtKB:P10645};
Contains:
RecName: Full=Catestatin {ECO:0000303|PubMed:14759560};
Contains:
RecName: Full=GE-25 {ECO:0000303|PubMed:7646465};
Contains:
RecName: Full=Serpinin-RRG;
Contains:
RecName: Full=Serpinin {ECO:0000303|PubMed:21436258};
Contains:
RecName: Full=p-Glu serpinin precursor;
Flags: Precursor;
Name=CHGA;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1779968; DOI=10.1210/mend-5-11-1651;
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;
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].
PubMed=3018587; DOI=10.1038/323082a0;
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; DOI=10.1073/pnas.84.14.5043;
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].
PubMed=9074643; DOI=10.1016/S0014-5793(97)00099-9;
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;
PubMed=12795588; DOI=10.1021/bi0300433;
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; DOI=10.1210/endo-128-1-174;
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;
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.
PubMed=8243650; DOI=10.1016/0014-5793(93)80715-7;
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 FUNCTION (CHROMOSTATIN).
PubMed=1996343; DOI=10.1073/pnas.88.4.1426;
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; DOI=10.1042/bj2760471;
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, AMIDATION AT GLY-312, AND FUNCTION
(PANCREASTATIN).
PubMed=2756155; DOI=10.1016/0167-0115(89)90262-0;
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; DOI=10.1042/bj2950649;
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, PHOSPHORYLATION AT TYR-191, GLYCOSYLATION
AT SER-204, AND FUNCTION (CHROMACIN).
TISSUE=Chromaffin cell;
PubMed=8910482; DOI=10.1074/jbc.271.45.28533;
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]
PROTEIN SEQUENCE OF 351-363, MASS SPECTROMETRY, PROTEOLYTIC
PROCESSING, OXIDATION AT MET-364, AND SUBCELLULAR LOCATION.
PubMed=10781584; DOI=10.1074/jbc.M001232200;
Taylor C.V., Taupenot L., Mahata S.K., Mahata M., Wu H.,
Yasothornsrikul S., Toneff T., Caporale C., Jiang Q., Parmer R.J.,
Hook V.Y., O'Connor D.T.;
"Formation of the catecholamine release-inhibitory peptide catestatin
from chromogranin A. Determination of proteolytic cleavage sites in
hormone storage granules.";
J. Biol. Chem. 275:22905-22915(2000).
[18]
CHARACTERIZATION OF GE-25, AND TISSUE SPECIFICITY.
PubMed=7535395; DOI=10.1016/0306-4522(94)90582-7;
Kirchmair R., Benzer A., Troger J., Miller C., Marksteiner J.,
Saria A., Gasser R.W., 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 63:1179-1187(1994).
[19]
CHARACTERIZATION OF GE-25, AND TISSUE SPECIFICITY.
PubMed=7646465; DOI=10.1042/bj3100331;
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. 310:331-336(1995).
[20]
FUNCTION (CATESTATIN).
PubMed=9294131; DOI=10.1172/JCI119686;
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).
[21]
FUNCTION (CATESTATIN).
PubMed=9786174; DOI=10.1016/S0196-9781(98)00086-2;
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).
[22]
FUNCTION (VASOSTATIN-1).
PubMed=10753865; DOI=10.1074/jbc.275.15.10745;
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).
[23]
GLYCOSYLATION AT SER-185 AND THR-249, PHOSPHORYLATION, AND DISULFIDE
BOND.
PubMed=10527498; DOI=10.1006/abio.1999.4244;
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).
[24]
FUNCTION (CATESTATIN).
PubMed=15723172; DOI=10.1007/s00018-004-4461-9;
Briolat J., Wu S.D., Mahata S.K., Gonthier B., Bagnard D.,
Chasserot-Golaz S., Helle K.B., Aunis D., Metz-Boutigue M.H.;
"New antimicrobial activity for the catecholamine release-inhibitory
peptide from chromogranin A.";
Cell. Mol. Life Sci. 62:377-385(2005).
[25]
FUNCTION (SERPININ).
PubMed=21436258; DOI=10.1210/me.2010-0124;
Koshimizu H., Cawley N.X., Kim T., Yergey A.L., Loh Y.P.;
"Serpinin: a novel chromogranin A-derived, secreted peptide up-
regulates protease nexin-1 expression and granule biogenesis in
endocrine cells.";
Mol. Endocrinol. 25:732-744(2011).
[26]
3D-STRUCTURE MODELING OF CATESTATIN.
PubMed=9809795; DOI=10.1016/S0167-0115(98)00040-8;
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).
[27]
STRUCTURE BY NMR OF 65-88, FUNCTION (CHROMOFUNGIN), AND SUBCELLULAR
LOCATION.
PubMed=11451958; DOI=10.1074/jbc.M104670200;
Lugardon K., Chasserot-Golaz S., Kieffer A.E., Maget-Dana R.,
Nullans G., Kieffer B., Aunis D., Metz-Boutigue M.H.;
"Structural and biological characterization of chromofungin, the
antifungal chromogranin A-(47-66)-derived peptide.";
J. Biol. Chem. 276:35875-35882(2001).
[28]
STRUCTURE BY NMR OF 368-380.
PubMed=14759560; DOI=10.1016/j.regpep.2003.10.035;
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).
-!- FUNCTION: Pancreastatin: Strongly inhibits glucose induced insulin
release from the pancreas. {ECO:0000269|PubMed:2756155}.
-!- FUNCTION: Chromostatin: Completely inhibits catecholamine release
from chromaffin cells. {ECO:0000269|PubMed:1996343}.
-!- FUNCTION: Chromacin: Has antibacterial activity against M.luteus.
Not active against E.coli. {ECO:0000269|PubMed:8910482}.
-!- FUNCTION: Catestatin: 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).
{ECO:0000250|UniProtKB:P10645, ECO:0000269|PubMed:15723172,
ECO:0000269|PubMed:9294131, ECO:0000269|PubMed:9786174}.
-!- 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
A.benhamiae. {ECO:0000269|PubMed:10753865}.
-!- FUNCTION: Chromofungin: 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. {ECO:0000269|PubMed:11451958}.
-!- FUNCTION: Serpinin: 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).
{ECO:0000269|PubMed:21436258}.
-!- SUBUNIT: Interacts with SCG3. {ECO:0000250|UniProtKB:P26339}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen
{ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory
vesicle membrane {ECO:0000250|UniProtKB:P26339}. Secreted
{ECO:0000269|PubMed:11451958}. Note=Associated with the secretory
granule membrane through direct interaction to SCG3 that in turn
binds to cholesterol-enriched lipid rafts in intragranular
conditions. {ECO:0000250|UniProtKB:P26339}.
-!- SUBCELLULAR LOCATION: Serpinin: Secreted
{ECO:0000269|PubMed:10781584}. Cytoplasmic vesicle, secretory
vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated
serpinin localizes to secretory vesicle.
{ECO:0000250|UniProtKB:P26339}.
-!- TISSUE SPECIFICITY: Highest concentration of GE-25 found in
adrenal medulla with lower levels present in the pituitary, the
intestinal mucosa and the pancreas. Also found in the brain.
{ECO:0000269|PubMed:7535395, ECO:0000269|PubMed:7646465}.
-!- PTM: In secretory granules, is attacked at both N- and C-terminal
sides by proteolytic enzymes generating numerous peptides of
various activities. Proteolytic processing can gives rise to
additional longer forms of catestatin peptides which display a
less potent catecholamine release-inhibitory activity
(PubMed:10781584). {ECO:0000269|PubMed:10781584,
ECO:0000269|PubMed:8240272, ECO:0000305|PubMed:11451958}.
-!- MASS SPECTROMETRY: Mass=8584.9; Method=MALDI; Range=19-94;
Evidence={ECO:0000269|PubMed:12795588};
-!- MASS SPECTROMETRY: Mass=3827; Method=MALDI; Range=350-382;
Note=From adrenal medullary chromaffin granules.;
Evidence={ECO:0000269|PubMed:10781584};
-!- MASS SPECTROMETRY: Mass=3832; Method=MALDI; Range=350-382;
Note=From splenic nerve large dense core granules.;
Evidence={ECO:0000269|PubMed:10781584};
-!- MASS SPECTROMETRY: Mass=3844; Method=MALDI; Range=350-382;
Note=From adrenal medullary chromaffin granules. With methionine
sulfoxide at Met-364.; Evidence={ECO:0000269|PubMed:10781584};
-!- MASS SPECTROMETRY: Mass=3843; Method=MALDI; Range=350-382;
Note=From splenic nerve large dense core granules. With methionine
sulfoxide at Met-364.; Evidence={ECO:0000269|PubMed:10781584};
-!- MASS SPECTROMETRY: Mass=3718; Method=MALDI; Range=351-382;
Evidence={ECO:0000269|PubMed:10781584};
-!- MASS SPECTROMETRY: Mass=2300; Method=MALDI; Range=361-380;
Evidence={ECO:0000269|PubMed:10781584};
-!- MASS SPECTROMETRY: Mass=2426; Method=MALDI; Range=362-382;
Evidence={ECO:0000269|PubMed:12795588};
-!- MISCELLANEOUS: Binds calcium with a low-affinity.
-!- SIMILARITY: Belongs to the chromogranin/secretogranin protein
family. {ECO:0000305}.
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EMBL; S79270; AAB21297.1; -; Genomic_DNA.
EMBL; S79256; AAB21297.1; JOINED; Genomic_DNA.
EMBL; S79258; AAB21297.1; JOINED; Genomic_DNA.
EMBL; S79260; AAB21297.1; JOINED; Genomic_DNA.
EMBL; S79262; AAB21297.1; JOINED; Genomic_DNA.
EMBL; S79264; AAB21297.1; JOINED; Genomic_DNA.
EMBL; S79266; AAB21297.1; JOINED; Genomic_DNA.
EMBL; S79268; AAB21297.1; JOINED; Genomic_DNA.
EMBL; X04012; CAA27636.1; -; mRNA.
EMBL; X04298; CAA27841.1; -; mRNA.
EMBL; M16971; AAA30765.1; -; mRNA.
EMBL; U73523; AAC48700.1; -; mRNA.
EMBL; BC105515; AAI05516.1; -; mRNA.
PIR; A41520; A41520.
RefSeq; NP_851348.1; NM_181005.2.
UniGene; Bt.49630; -.
PDB; 1CFK; Model; -; A=359-389.
PDB; 1N2Y; NMR; -; A=368-380.
PDBsum; 1CFK; -.
PDBsum; 1N2Y; -.
DisProt; DP00118; -.
SMR; P05059; -.
IntAct; P05059; 2.
MINT; MINT-1214849; -.
STRING; 9913.ENSBTAP00000012973; -.
iPTMnet; P05059; -.
UniCarbKB; P05059; -.
PaxDb; P05059; -.
PeptideAtlas; P05059; -.
PRIDE; P05059; -.
GeneID; 281070; -.
KEGG; bta:281070; -.
CTD; 1113; -.
eggNOG; ENOG410II3Z; Eukaryota.
eggNOG; ENOG410YGBX; LUCA.
HOGENOM; HOG000111808; -.
HOVERGEN; HBG001272; -.
InParanoid; P05059; -.
KO; K19990; -.
TreeFam; TF336596; -.
EvolutionaryTrace; P05059; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0042583; C:chromaffin granule; IDA:CAFA.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
GO; GO:0019732; P:antifungal humoral response; IMP:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0052338; P:disruption by host of symbiont cell wall; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
GO; GO:0045576; P:mast cell activation; ISS:UniProtKB.
GO; GO:0002551; P:mast cell chemotaxis; ISS:UniProtKB.
GO; GO:0032762; P:mast cell cytokine production; ISS:UniProtKB.
GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; TAS:UniProtKB.
GO; GO:0033604; P:negative regulation of catecholamine secretion; IDA:UniProtKB.
GO; GO:0046888; P:negative regulation of hormone secretion; IDA:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; IDA:UniProtKB.
GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
InterPro; IPR001819; Chromogranin_AB.
InterPro; IPR018054; Chromogranin_CS.
InterPro; IPR001990; Granin.
PANTHER; PTHR10583; PTHR10583; 1.
Pfam; PF01271; Granin; 2.
PRINTS; PR00659; CHROMOGRANIN.
PROSITE; PS00422; GRANINS_1; 1.
PROSITE; PS00423; GRANINS_2; 1.
1: Evidence at protein level;
3D-structure; Amidation; Antibiotic; Antimicrobial; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
Fungicide; Glycoprotein; Membrane; Oxidation; Phosphoprotein;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:12795588,
ECO:0000269|PubMed:1986917,
ECO:0000269|PubMed:2387861,
ECO:0000269|PubMed:8243650}.
CHAIN 19 449 Chromogranin-A.
/FTId=PRO_0000005398.
PEPTIDE 19 94 Vasostatin-1.
{ECO:0000269|PubMed:12795588}.
/FTId=PRO_0000005399.
PEPTIDE 65 88 Chromofungin.
{ECO:0000269|PubMed:11451958}.
/FTId=PRO_0000432587.
PEPTIDE 142 161 Chromostatin.
{ECO:0000269|PubMed:1996343}.
/FTId=PRO_0000005400.
PEPTIDE 191 212 Chromacin. {ECO:0000269|PubMed:8910482}.
/FTId=PRO_0000005401.
PEPTIDE 266 312 Pancreastatin.
{ECO:0000269|PubMed:2756155}.
/FTId=PRO_0000005402.
PEPTIDE 334 347 WE-14. {ECO:0000250|UniProtKB:P10645}.
/FTId=PRO_0000005403.
PEPTIDE 362 382 Catestatin.
{ECO:0000269|PubMed:12795588}.
/FTId=PRO_0000005404.
PEPTIDE 385 409 GE-25. {ECO:0000303|PubMed:7646465}.
/FTId=PRO_0000432673.
PEPTIDE 421 449 Serpinin-RRG.
{ECO:0000250|UniProtKB:P10354}.
/FTId=PRO_0000432674.
PEPTIDE 421 446 Serpinin. {ECO:0000303|PubMed:21436258}.
/FTId=PRO_0000432675.
PEPTIDE 424 446 p-Glu serpinin precursor.
{ECO:0000250|UniProtKB:P26339}.
/FTId=PRO_0000432676.
MOD_RES 99 99 Phosphoserine.
{ECO:0000269|PubMed:10527498}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000269|PubMed:10527498}.
MOD_RES 191 191 Phosphotyrosine.
{ECO:0000269|PubMed:8910482}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000250|UniProtKB:P10645}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000250|UniProtKB:P10645}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:P10645}.
MOD_RES 312 312 Glycine amide.
{ECO:0000269|PubMed:2756155}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000269|PubMed:10527498}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:P10645}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:P10354}.
MOD_RES 364 364 Methionine sulfoxide.
{ECO:0000269|PubMed:10781584}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000269|PubMed:10527498}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000269|PubMed:10527498}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:P10354}.
MOD_RES 424 424 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P26339}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000250|UniProtKB:P10354}.
CARBOHYD 185 185 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:10527498}.
/FTId=CAR_000114.
CARBOHYD 204 204 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:8910482}.
/FTId=CAR_000203.
CARBOHYD 249 249 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:10527498}.
/FTId=CAR_000115.
DISULFID 35 56 {ECO:0000269|PubMed:10527498}.
CONFLICT 112 112 N -> T (in Ref. 4; AAA30765).
{ECO:0000305}.
CONFLICT 136 136 F -> S (in Ref. 2; CAA27636 and 6;
AAI05516). {ECO:0000305}.
CONFLICT 154 155 SP -> PQ (in Ref. 3; CAA27841).
{ECO:0000305}.
CONFLICT 159 159 P -> R (in Ref. 3; CAA27841).
{ECO:0000305}.
CONFLICT 191 191 Y -> H (in Ref. 1; AAB21297).
{ECO:0000305}.
CONFLICT 254 254 P -> A (in Ref. 1; AAB21297).
{ECO:0000305}.
CONFLICT 293 293 A -> S (in Ref. 5; AAC48700).
{ECO:0000305}.
CONFLICT 311 311 R -> H (in Ref. 2; CAA27636, 6; AAI05516
and 13; AA sequence). {ECO:0000305}.
CONFLICT 319 319 E -> K (in Ref. 2; CAA27636, 6; AAI05516
and 13; AA sequence). {ECO:0000305}.
CONFLICT 379 379 G -> R (in Ref. 4; AAA30765).
{ECO:0000305}.
CONFLICT 391 391 R -> Q (in Ref. 2; CAA27636 and 6;
AAI05516). {ECO:0000305}.
TURN 369 374 {ECO:0000244|PDB:1N2Y}.
STRAND 375 377 {ECO:0000244|PDB:1N2Y}.
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


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