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Protein

Chromogranin-A

Gene

CHGA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pancreastatin: Strongly inhibits glucose induced insulin release from the pancreas.1 Publication
Chromostatin: Completely inhibits catecholamine release from chromaffin cells.1 Publication
Chromacin: Has antibacterial activity against M.luteus. Not active against E.coli.1 Publication
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).By similarity3 Publications
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.1 Publication
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.1 Publication
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).1 Publication

GO - Biological processi

  • defense response to fungus Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • innate immune response Source: UniProtKB
  • killing of cells of other organism Source: UniProtKB-KW
  • mast cell activation Source: UniProtKB
  • mast cell chemotaxis Source: UniProtKB
  • mast cell cytokine production Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • negative regulation of angiogenesis Source: UniProtKB
  • negative regulation of catecholamine secretion Source: UniProtKB
  • negative regulation of hormone secretion Source: UniProtKB
  • negative regulation of insulin secretion Source: UniProtKB
  • positive regulation of dense core granule biogenesis Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Chromogranin-A2 Publications
Short name:
CgA
Alternative name(s):
Pituitary secretory protein I1 Publication
Short name:
SP-I
Cleaved into the following 11 chains:
Vasostatin-11 Publication
Chromofungin1 Publication
Chromostatin1 Publication
Chromacin1 Publication
Pancreastatin1 Publication
WE-14By similarity
Catestatin1 Publication
GE-251 Publication
Serpinin1 Publication
Gene namesi
Name:CHGA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Serpinin :

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • mast cell granule Source: GOC
  • secretory granule Source: UniProtKB
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18184 PublicationsAdd
BLAST
Chaini19 – 449431Chromogranin-APRO_0000005398Add
BLAST
Peptidei19 – 9476Vasostatin-11 PublicationPRO_0000005399Add
BLAST
Peptidei65 – 8824Chromofungin1 PublicationPRO_0000432587Add
BLAST
Peptidei142 – 16120Chromostatin1 PublicationPRO_0000005400Add
BLAST
Peptidei191 – 21222Chromacin1 PublicationPRO_0000005401Add
BLAST
Peptidei266 – 31247Pancreastatin1 PublicationPRO_0000005402Add
BLAST
Peptidei334 – 34714WE-14By similarityPRO_0000005403Add
BLAST
Peptidei362 – 38221Catestatin1 PublicationPRO_0000005404Add
BLAST
Peptidei385 – 40925GE-251 PublicationPRO_0000432673Add
BLAST
Peptidei421 – 44929Serpinin-RRGBy similarityPRO_0000432674Add
BLAST
Peptidei421 – 44626Serpinin1 PublicationPRO_0000432675Add
BLAST
Peptidei424 – 44623p-Glu serpinin precursorBy similarityPRO_0000432676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 561 Publication
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei142 – 1421Phosphoserine1 Publication
Glycosylationi185 – 1851O-linked (GalNAc...)1 PublicationCAR_000114
Modified residuei191 – 1911Phosphotyrosine1 Publication
Modified residuei200 – 2001PhosphoserineBy similarity
Glycosylationi204 – 2041O-linked (GalNAc...)1 PublicationCAR_000203
Modified residuei215 – 2151PhosphoserineBy similarity
Glycosylationi249 – 2491O-linked (GalNAc...)1 PublicationCAR_000115
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei312 – 3121Glycine amideCurated
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei325 – 3251PhosphoserineBy similarity
Modified residuei363 – 3631PhosphoserineBy similarity
Modified residuei364 – 3641Methionine sulfoxide1 Publication
Modified residuei390 – 3901Phosphoserine1 Publication
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei416 – 4161PhosphoserineBy similarity
Modified residuei424 – 4241Pyrrolidone carboxylic acidBy similarity
Modified residuei430 – 4301PhosphoserineBy similarity

Post-translational modificationi

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).1 Publication2 Publications

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP05059.
PeptideAtlasiP05059.
PRIDEiP05059.

PTM databases

iPTMnetiP05059.
UniCarbKBiP05059.

Expressioni

Tissue specificityi

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.2 Publications

Interactioni

Subunit structurei

Interacts with SCG3.By similarity

Protein-protein interaction databases

MINTiMINT-1214849.
STRINGi9913.ENSBTAP00000012973.

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni369 – 3746Combined sources
Beta strandi375 – 3773Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFKmodel-A359-389[»]
1N2YNMR-A368-380[»]
DisProtiDP00118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05059.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II3Z. Eukaryota.
ENOG410YGBX. LUCA.
HOGENOMiHOG000111808.
HOVERGENiHBG001272.
InParanoidiP05059.
KOiK19990.
OrthoDBiEOG7V766Z.
TreeFamiTF336596.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 2 hits.
[Graphical view]
PRINTSiPR00659. CHROMOGRANIN.
PROSITEiPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05059-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSAAVLALL LCAGQVIALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM
60 70 80 90 100
PVSKECFETL RGDERILSIL RHQNLLKELQ DLALQGAKER THQQKKHSSY
110 120 130 140 150
EDELSEVLEK PNDQAEPKEV TEEVSSKDAA EKRDDFKEVE KSDEDSDGDR
160 170 180 190 200
PQASPGLGPG PKVEEDNQAP GEEEEAPSNA HPLASLPSPK YPGPQAKEDS
210 220 230 240 250
EGPSQGPASR EKGLSAEQGR QTEREEEEEK WEEAEAREKA VPEEESPPTA
260 270 280 290 300
AFKPPPSLGN KETQRAAPGW PEDGAGKMGA EEAKPPEGKG EWAHSRQEEE
310 320 330 340 350
EMARAPQVLF RGGKSGEPEQ EEQLSKEWED AKRWSKMDQL AKELTAEKRL
360 370 380 390 400
EGEEEEEEDP DRSMRLSFRA RGYGFRGPGL QLRRGWRPNS REDSVEAGLP
410 420 430 440
LQVRGYPEEK KEEEGSANRR PEDQELESLS AIEAELEKVA HQLEELRRG
Length:449
Mass (Da):50,015
Last modified:November 1, 1988 - v1
Checksum:iF304EDC587AA70A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121N → T in AAA30765 (PubMed:3474638).Curated
Sequence conflicti136 – 1361F → S in CAA27636 (PubMed:3755681).Curated
Sequence conflicti136 – 1361F → S in AAI05516 (Ref. 6) Curated
Sequence conflicti154 – 1552SP → PQ in CAA27841 (PubMed:3018587).Curated
Sequence conflicti159 – 1591P → R in CAA27841 (PubMed:3018587).Curated
Sequence conflicti191 – 1911Y → H in AAB21297 (PubMed:1779968).Curated
Sequence conflicti254 – 2541P → A in AAB21297 (PubMed:1779968).Curated
Sequence conflicti293 – 2931A → S in AAC48700 (PubMed:9074643).Curated
Sequence conflicti311 – 3111R → H in CAA27636 (PubMed:3755681).Curated
Sequence conflicti311 – 3111R → H in AAI05516 (Ref. 6) Curated
Sequence conflicti311 – 3111R → H AA sequence (PubMed:1710890).Curated
Sequence conflicti319 – 3191E → K in CAA27636 (PubMed:3755681).Curated
Sequence conflicti319 – 3191E → K in AAI05516 (Ref. 6) Curated
Sequence conflicti319 – 3191E → K AA sequence (PubMed:1710890).Curated
Sequence conflicti379 – 3791G → R in AAA30765 (PubMed:3474638).Curated
Sequence conflicti391 – 3911R → Q in CAA27636 (PubMed:3755681).Curated
Sequence conflicti391 – 3911R → Q in AAI05516 (Ref. 6) Curated

Mass spectrometryi

Molecular mass is 8584.9 Da from positions 19 - 94. Determined by MALDI. 1 Publication
Molecular mass is 3827 Da from positions 350 - 382. Determined by MALDI. From adrenal medullary chromaffin granules.1 Publication
Molecular mass is 3832 Da from positions 350 - 382. Determined by MALDI. From splenic nerve large dense core granules.1 Publication
Molecular mass is 3844 Da from positions 350 - 382. Determined by MALDI. From adrenal medullary chromaffin granules. With methionine sulfoxide at Met-364.1 Publication
Molecular mass is 3843 Da from positions 350 - 382. Determined by MALDI. From splenic nerve large dense core granules. With methionine sulfoxide at Met-364.1 Publication
Molecular mass is 3718 Da from positions 351 - 382. Determined by MALDI. 1 Publication
Molecular mass is 2300 Da from positions 361 - 380. Determined by MALDI. 1 Publication
Molecular mass is 2426 Da from positions 362 - 382. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA41520.
RefSeqiNP_851348.1. NM_181005.2.
UniGeneiBt.49630.

Genome annotation databases

GeneIDi281070.
KEGGibta:281070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA41520.
RefSeqiNP_851348.1. NM_181005.2.
UniGeneiBt.49630.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFKmodel-A359-389[»]
1N2YNMR-A368-380[»]
DisProtiDP00118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1214849.
STRINGi9913.ENSBTAP00000012973.

PTM databases

iPTMnetiP05059.
UniCarbKBiP05059.

Proteomic databases

PaxDbiP05059.
PeptideAtlasiP05059.
PRIDEiP05059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281070.
KEGGibta:281070.

Organism-specific databases

CTDi1113.

Phylogenomic databases

eggNOGiENOG410II3Z. Eukaryota.
ENOG410YGBX. LUCA.
HOGENOMiHOG000111808.
HOVERGENiHBG001272.
InParanoidiP05059.
KOiK19990.
OrthoDBiEOG7V766Z.
TreeFamiTF336596.

Miscellaneous databases

EvolutionaryTraceiP05059.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 2 hits.
[Graphical view]
PRINTSiPR00659. CHROMOGRANIN.
PROSITEiPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 142-161, FUNCTION (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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 266-331.
  14. Cited for: PROTEIN SEQUENCE OF 266-312, FUNCTION (PANCREASTATIN).
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 191-212, PHOSPHORYLATION AT TYR-191, GLYCOSYLATION AT SER-204, FUNCTION (CHROMACIN).
    Tissue: Chromaffin cell.
  17. "Formation of the catecholamine release-inhibitory peptide catestatin from chromogranin A. Determination of proteolytic cleavage sites in hormone storage granules."
    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.
    J. Biol. Chem. 275:22905-22915(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 351-363, MASS SPECTROMETRY, PROTEOLYTIC PROCESSING, OXIDATION AT MET-364, SUBCELLULAR LOCATION.
  18. "Molecular characterization of immunoreactivities of peptides derived from chromogranin A (GE-25) and from secretogranin II (secretoneurin) in human and bovine cerebrospinal fluid."
    Kirchmair R., Benzer A., Troger J., Miller C., Marksteiner J., Saria A., Gasser R.W., Hogue-Angeletti R., Fischer-Colbrie R., Winkler H.
    Neuroscience 63:1179-1187(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF GE-25, TISSUE SPECIFICITY.
  19. "Large variations in the proteolytic formation of a chromogranin A-derived peptide (GE-25) in neuroendocrine tissues."
    Kirchmair R., Leitner B., Fischer-Colbrie R., Marksteiner J., Hogue-Angeletti R., Winkler H.
    Biochem. J. 310:331-336(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF GE-25, TISSUE SPECIFICITY.
  20. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CATESTATIN).
  21. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CATESTATIN).
  22. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION (VASOSTATIN-1).
  23. "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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-185 AND THR-249, PHOSPHORYLATION, DISULFIDE BOND.
  24. "New antimicrobial activity for the catecholamine release-inhibitory peptide from chromogranin A."
    Briolat J., Wu S.D., Mahata S.K., Gonthier B., Bagnard D., Chasserot-Golaz S., Helle K.B., Aunis D., Metz-Boutigue M.H.
    Cell. Mol. Life Sci. 62:377-385(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (CATESTATIN).
  25. "Serpinin: a novel chromogranin A-derived, secreted peptide up-regulates protease nexin-1 expression and granule biogenesis in endocrine cells."
    Koshimizu H., Cawley N.X., Kim T., Yergey A.L., Loh Y.P.
    Mol. Endocrinol. 25:732-744(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (SERPININ).
  26. "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] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF CATESTATIN.
  27. "Structural and biological characterization of chromofungin, the antifungal chromogranin A-(47-66)-derived peptide."
    Lugardon K., Chasserot-Golaz S., Kieffer A.E., Maget-Dana R., Nullans G., Kieffer B., Aunis D., Metz-Boutigue M.H.
    J. Biol. Chem. 276:35875-35882(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 65-88, FUNCTION (CHROMOFUNGIN), SUBCELLULAR LOCATION.
  28. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 368-380.

Entry informationi

Entry nameiCMGA_BOVIN
AccessioniPrimary (citable) accession number: P05059
Secondary accession number(s): P79392, Q2KJ52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1988
Last modified: July 6, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds calcium with a low-affinity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.