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Protein

Chromogranin-A

Gene

Chga

Organism
Mus musculus (Mouse)
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 (PubMed:21436258). Pyroglutaminated (pGlu)-serpinin exerts an antiapoptotic effect on cells exposed to oxidative stress (PubMed:21537909).2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Chromogranin-A
Short name:
CgA
Cleaved into the following 8 chains:
Serpinin2 Publications
Alternative name(s):
AL261 Publication
p-Glu serpinin precursor1 Publication
Gene namesi
Name:Chga
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:88394. Chga.

Subcellular locationi

Serpinin :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 463445Chromogranin-APRO_0000005422Add
BLAST
Peptidei19 – 151133Beta-graninBy similarityPRO_0000005423Add
BLAST
Peptidei276 – 32954PancreastatinBy similarityPRO_0000005424Add
BLAST
Peptidei358 – 37114WE-14By similarityPRO_0000005425Add
BLAST
Peptidei382 – 40221CatestatinBy similarityPRO_0000432687Add
BLAST
Peptidei405 – 42319GE-25By similarityPRO_0000432688Add
BLAST
Peptidei435 – 46329Serpinin-RRGBy similarityPRO_0000432689Add
BLAST
Peptidei435 – 46026Serpinin2 PublicationsPRO_0000432690Add
BLAST
Peptidei438 – 46023p-Glu serpinin precursor1 PublicationPRO_0000432691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 56By similarity
Modified residuei119 – 1191PhosphoserineBy similarity
Modified residuei220 – 2201PhosphoserineBy similarity
Modified residuei308 – 3081PhosphoserineBy similarity
Modified residuei329 – 3291Glycine amideCurated
Modified residuei350 – 3501PhosphoserineBy similarity
Modified residuei384 – 3841Methionine sulfoxideBy similarity
Modified residuei410 – 4101PhosphoserineBy similarity
Modified residuei414 – 4141PhosphoserineBy similarity
Modified residuei438 – 4381Pyrrolidone carboxylic acid1 Publication

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

MaxQBiP26339.
PaxDbiP26339.
PRIDEiP26339.

PTM databases

PhosphoSiteiP26339.

Expressioni

Gene expression databases

BgeeiP26339.
CleanExiMM_CHGA.
ExpressionAtlasiP26339. baseline and differential.
GenevisibleiP26339. MM.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SOD1P004415EBI-990900,EBI-990792From a different organism.

Protein-protein interaction databases

IntActiP26339. 3 interactions.
STRINGi10090.ENSMUSP00000021610.

Structurei

3D structure databases

ProteinModelPortaliP26339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi103 – 11614Poly-GlnAdd
BLAST
Compositional biasi236 – 24510Poly-Glu
Compositional biasi340 – 3478Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG41926.
GeneTreeiENSGT00730000111266.
HOGENOMiHOG000111808.
HOVERGENiHBG001272.
InParanoidiP26339.
OMAiVNSPMNK.
OrthoDBiEOG7V766Z.
PhylomeDBiP26339.
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.

P26339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSTAVLALL LCAGQVFALP VNSPMTKGDT KVMKCVLEVI SDSLSKPSPM
60 70 80 90 100
PVSPECLETL QGDERILSIL RHQNLLKELQ DLALQGAKER AQQPLKQQQP
110 120 130 140 150
PKQQQQQQQQ QQQEQQHSSF EDELSEVFEN QSPDAKHRDA AAEVPSRDTM
160 170 180 190 200
EKRKDSDKGQ QDGFEATTEG PRPQAFPEPN QESPMMGDSE SPGEDTATNT
210 220 230 240 250
QSPTSLPSQE HVDPQATGDS ERGLSAQQQA RKAKQEEKEE EEEEEAVARE
260 270 280 290 300
KAGPEEVPTA ASSSHFHAGY KAIQKDDGQS DSQAVDGDGK TEASEALPSE
310 320 330 340 350
GKGELEHSQQ EEDGEEAMVG TPQGLFPQGG KGRELEHKQE EEEEEEERLS
360 370 380 390 400
REWEDKRWSR MDQLAKELTA EKRLEGEDDP DRSMKLSFRT RAYGFRDPGP
410 420 430 440 450
QLRRGWRPSS REDSVEARSD FEEKKEEEGS ANRRAEDQEL ESLSAIEAEL
460
EKVAHQLQAL RRG
Length:463
Mass (Da):51,789
Last modified:May 1, 1992 - v1
Checksum:i1AB3C5FF433C39E4
GO

Mass spectrometryi

Molecular mass is 3020.6 Da from positions 434 - 460. Determined by MALDI. 1 Publication
Molecular mass is 2864.4 Da from positions 435 - 460. Determined by MALDI. 1 Publication
Molecular mass is 2864.5 Da from positions 435 - 460. Determined by MALDI. 1 Publication
Molecular mass is 2644.4 Da from positions 437 - 460. Determined by MALDI. 1 Publication
Molecular mass is 2532.4 Da from positions 438 - 460. Determined by MALDI. With pyrrolidone carboxylic acid at Gln-438.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64278 mRNA. Translation: AAA37457.1.
BC026554 mRNA. Translation: AAH26554.1.
CCDSiCCDS26120.1.
PIRiA39868.
RefSeqiNP_031719.1. NM_007693.1.
UniGeneiMm.4137.

Genome annotation databases

EnsembliENSMUST00000021610; ENSMUSP00000021610; ENSMUSG00000021194.
GeneIDi12652.
KEGGimmu:12652.
UCSCiuc007oui.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64278 mRNA. Translation: AAA37457.1.
BC026554 mRNA. Translation: AAH26554.1.
CCDSiCCDS26120.1.
PIRiA39868.
RefSeqiNP_031719.1. NM_007693.1.
UniGeneiMm.4137.

3D structure databases

ProteinModelPortaliP26339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP26339. 3 interactions.
STRINGi10090.ENSMUSP00000021610.

PTM databases

PhosphoSiteiP26339.

Proteomic databases

MaxQBiP26339.
PaxDbiP26339.
PRIDEiP26339.

Protocols and materials databases

DNASUi12652.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021610; ENSMUSP00000021610; ENSMUSG00000021194.
GeneIDi12652.
KEGGimmu:12652.
UCSCiuc007oui.1. mouse.

Organism-specific databases

CTDi1113.
MGIiMGI:88394. Chga.

Phylogenomic databases

eggNOGiNOG41926.
GeneTreeiENSGT00730000111266.
HOGENOMiHOG000111808.
HOVERGENiHBG001272.
InParanoidiP26339.
OMAiVNSPMNK.
OrthoDBiEOG7V766Z.
PhylomeDBiP26339.
TreeFamiTF336596.

Miscellaneous databases

NextBioi281864.
PROiP26339.
SOURCEiSearch...

Gene expression databases

BgeeiP26339.
CleanExiMM_CHGA.
ExpressionAtlasiP26339. baseline and differential.
GenevisibleiP26339. MM.

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. "Structure and function of the chromogranin A gene. Clues to evolution and tissue-specific expression."
    Wu H.J., Rozansky D.J., Parmer R.J., Gill B.M., O'Connor D.T.
    J. Biol. Chem. 266:13130-13134(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  3. "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.
  4. "Role of pGlu-serpinin, a novel chromogranin A-derived peptide in inhibition of cell death."
    Koshimizu H., Cawley N.X., Yergy A.L., Loh Y.P.
    J. Mol. Neurosci. 45:294-303(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (SERPININ), PYROGLUTAMATE FORMATION AT GLN-438, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  5. "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), MASS SPECTROMETRY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCMGA_MOUSE
AccessioniPrimary (citable) accession number: P26339
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 24, 2015
This is version 114 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.