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Protein

Chromogranin-A

Gene

Chga

Organism
Rattus norvegicus (Rat)
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.
Catestatin inhibits catecholamine release from chromaffin cells and noradrenergic neurons by acting as a non-competitive nicotinic cholinergic antagonist. Can induce mast cell migration, degranulation and production of cytokines and chemokines.By similarity
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 (By similarity). Serpinin and pGlu-serpinin can enhance both myocardial contractility (inotropy) and relaxation (lusitropy) and this cardio-stimulation requires a beta 1-adrenergic receptor/adenylate cyclase/cAMP/PKA pathway (PubMed:22459152).By similarity1 Publication

GO - Biological processi

  • adrenergic receptor signaling pathway involved in cardiac muscle relaxation Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • mast cell activation Source: UniProtKB
  • mast cell chemotaxis Source: UniProtKB
  • mast cell cytokine production Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • negative regulation of catecholamine secretion Source: UniProtKB
  • negative regulation of neuron death Source: RGD
  • negative regulation of vasodilation Source: RGD
  • organelle organization Source: RGD
  • ovulation cycle Source: RGD
  • positive regulation of cAMP metabolic process Source: RGD
  • positive regulation of cardiac muscle contraction Source: UniProtKB
  • positive regulation of dense core granule biogenesis Source: UniProtKB
  • positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway Source: RGD
  • positive regulation of relaxation of cardiac muscle Source: UniProtKB
  • regulation of the force of heart contraction Source: RGD
Complete GO annotation...

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Chromogranin-A
Short name:
CgA
Cleaved into the following 8 chains:
Serpinin-RRG1 Publication
Serpinin1 Publication
Gene namesi
Name:Chga
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2338. Chga.

Subcellular locationi

Serpinin :
  • Secreted By similarity
  • Cytoplasmic vesiclesecretory vesicle By similarity

  • Note: Pyroglutaminated serpinin localizes to secretory vesicle.By similarity

GO - Cellular componenti

  • chromaffin granule Source: RGD
  • extracellular space Source: RGD
  • mast cell granule Source: GOC
  • secretory granule Source: RGD
  • 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 – 18181 PublicationAdd
BLAST
Chaini19 – 466448Chromogranin-APRO_0000005430Add
BLAST
Peptidei19 – 146128Beta-graninPRO_0000005431Add
BLAST
Peptidei281 – 33252PancreastatinSequence analysisPRO_0000005432Add
BLAST
Peptidei361 – 37414WE-14PRO_0000005433Add
BLAST
Peptidei385 – 40521CatestatinBy similarityPRO_0000432697Add
BLAST
Peptidei408 – 42619GE-25By similarityPRO_0000432698Add
BLAST
Peptidei438 – 46629Serpinin-RRG1 PublicationPRO_0000432699Add
BLAST
Peptidei438 – 46326Serpinin1 PublicationPRO_0000432700Add
BLAST
Peptidei441 – 46323p-Glu serpinin precursorBy similarityPRO_0000432701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 56By similarity
Modified residuei114 – 1141PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei288 – 2881PhosphoserineBy similarity
Modified residuei312 – 3121PhosphoserineCombined sources
Modified residuei332 – 3321Glycine amideCurated
Modified residuei353 – 3531PhosphoserineBy similarity
Modified residuei386 – 3861PhosphoserineCombined sources
Modified residuei387 – 3871Methionine sulfoxideBy similarity
Modified residuei413 – 4131PhosphoserineBy similarity
Modified residuei417 – 4171PhosphoserineCombined sources
Modified residuei433 – 4331PhosphoserineCombined sources
Modified residuei441 – 4411Pyrrolidone carboxylic acid1 Publication
Modified residuei447 – 4471PhosphoserineCombined sources

Post-translational modificationi

CgA is O-glycosylated.

Keywords - PTMi

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

Proteomic databases

PRIDEiP10354.

PTM databases

iPTMnetiP10354.
PhosphoSiteiP10354.

Expressioni

Tissue specificityi

Expressed in the brain and adrenal and pituitary glands.1 Publication

Interactioni

Subunit structurei

Interacts with SCG3; this interaction is optimal in conditions mimicking the lumenal milieu of the trans-Golgi network, i.e. pH 5.5 and 10 mM Ca(+2).1 Publication

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 11019Poly-GlnAdd
BLAST
Compositional biasi231 – 24919Poly-GluAdd
BLAST
Compositional biasi344 – 3507Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000111808.
HOVERGENiHBG001272.
InParanoidiP10354.
PhylomeDBiP10354.

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.

P10354-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSAALALL LCAGQVFALP VNSPMTKGDT KVMKCVLEVI SDSLSKPSPM
60 70 80 90 100
PVSPECLETL QGDERVLSIL RHQNLLKELQ DLALQGAKER AQQQQQQQQQ
110 120 130 140 150
QQQQQQQQQQ QHSSFEDELS EVFENQSPAA KHGDAASEAP SKDTVEKRED
160 170 180 190 200
SDKGQQDAFE GTTEGPRPQA FPEPKQESSM MGNSQSPGED TANNTQSPTS
210 220 230 240 250
LPSQEHGIPQ TTEGSERGPS AQQQARKAKQ EEKEEEEEEK EEEEEEKEEK
260 270 280 290 300
AIAREKAGPK EVPTAASSSH FYSGYKKIQK DDDGQSESQA VNGKTGASEA
310 320 330 340 350
VPSEGKGELE HSQQEEDGEE AMAGPPQGLF PGGKGQELER KQQEEEEEEE
360 370 380 390 400
RLSREWEDKR WSRMDQLAKE LTAEKRLEGE DDPDRSMKLS FRARAYGFRD
410 420 430 440 450
PGPQLRRGWR PSSREDSVEA RGDFEEKKEE EGSANRRAED QELESLSAIE
460
AELEKVAHQL QALRRG
Length:466
Mass (Da):52,024
Last modified:July 1, 1989 - v1
Checksum:i05D135FFA657C48C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06832 mRNA. Translation: CAA29988.1.
PIRiA23996.
UniGeneiRn.41024.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06832 mRNA. Translation: CAA29988.1.
PIRiA23996.
UniGeneiRn.41024.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiP10354.
PhosphoSiteiP10354.

Proteomic databases

PRIDEiP10354.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi2338. Chga.

Phylogenomic databases

HOGENOMiHOG000111808.
HOVERGENiHBG001272.
InParanoidiP10354.
PhylomeDBiP10354.

Miscellaneous databases

PROiP10354.

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. "Primary structure of rat chromogranin A and distribution of its mRNA."
    Iacangelo A., Okayama H., Eiden L.E.
    FEBS Lett. 227:115-121(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The molecular cloning of the chromogranin A-like precursor of beta-granin and pancreastatin from the endocrine pancreas."
    Hutton J.C., Nielsen E., Kastern W.
    FEBS Lett. 236:269-274(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-466.
    Tissue: Pancreas.
  3. "Beta-granins: 21 kDa co-secreted peptides of the insulin granule closely related to adrenal medullary chromogranin A."
    Hutton J.C., Hansen F., Peshavaria M.
    FEBS Lett. 188:336-340(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-32.
  4. "Identification of a chromogranin A domain that mediates binding to secretogranin III and targeting to secretory granules in pituitary cells and pancreatic beta-cells."
    Hosaka M., Watanabe T., Sakai Y., Uchiyama Y., Takeuchi T.
    Mol. Biol. Cell 13:3388-3399(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCG3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Secretogranin III binds to cholesterol in the secretory granule membrane as an adapter for chromogranin A."
    Hosaka M., Suda M., Sakai Y., Izumi T., Watanabe T., Takeuchi T.
    J. Biol. Chem. 279:3627-3634(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "The novel chromogranin A-derived serpinin and pyroglutaminated serpinin peptides are positive cardiac beta-adrenergic-like inotropes."
    Tota B., Gentile S., Pasqua T., Bassino E., Koshimizu H., Cawley N.X., Cerra M.C., Loh Y.P., Angelone T.
    FASEB J. 26:2888-2898(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF SERPININ PEPTIDE; SERPININ-RRG PEPTIDE AND PYROGLUTAMINATED SERPININ, FUNCTION (SERPININ).
  7. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-386; SER-417; SER-433 AND SER-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCMGA_RAT
AccessioniPrimary (citable) accession number: P10354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 20, 2016
This is version 106 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.