CMGA_PIG
ID CMGA_PIG Reviewed; 446 AA.
AC P04404;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Chromogranin-A;
DE Short=CgA;
DE Contains:
DE RecName: Full=Pancreastatin;
DE Contains:
DE RecName: Full=Parastatin;
DE Contains:
DE RecName: Full=WE-14;
DE Contains:
DE RecName: Full=Catestatin;
DE Contains:
DE RecName: Full=GE-25;
DE Contains:
DE RecName: Full=Serpinin-RRG;
DE Contains:
DE RecName: Full=Serpinin;
DE Contains:
DE RecName: Full=p-Glu serpinin precursor;
DE Flags: Precursor; Fragment;
GN Name=CHGA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2834189; DOI=10.1210/endo-122-5-2339;
RA Iacangelo A.L., Fischer-Colbrie R., Koller K.J., Brownstein M.J.,
RA Eiden L.E.;
RT "The sequence of porcine chromogranin A messenger RNA demonstrates
RT chromogranin A can serve as the precursor for the biologically active
RT hormone, pancreastatin.";
RL Endocrinology 122:2339-2341(1988).
RN [2]
RP PROTEIN SEQUENCE OF 256-304, AND AMIDATION AT GLY-304.
RX PubMed=3537810; DOI=10.1038/324476a0;
RA Tatemoto K., Efendie S., Mutt V., Makk G., Feistner G.J., Barchas J.D.;
RT "Pancreastatin, a novel pancreatic peptide that inhibits insulin
RT secretion.";
RL Nature 324:476-478(1986).
RN [3]
RP PROTEIN SEQUENCE OF 363-377.
RX PubMed=8344192; DOI=10.1210/endo.133.2.8344192;
RA Fasciotto B.H., Trauss C.A., Greeley G.H., Cohn D.V.;
RT "Parastatin (porcine chromogranin A347-419), a novel chromogranin A-derived
RT peptide, inhibits parathyroid cell secretion.";
RL Endocrinology 133:461-466(1993).
RN [4]
RP SULFATION.
RX PubMed=2105940; DOI=10.1016/s0021-9258(19)39725-x;
RA Gorr S.U., Cohn D.V.;
RT "Secretion of sulfated and nonsulfated forms of parathyroid chromogranin A
RT (secretory protein-I).";
RL J. Biol. Chem. 265:3012-3016(1990).
CC -!- FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin
CC release from the pancreas.
CC -!- FUNCTION: [Parastatin]: Inhibits low calcium-stimulated parathyroid
CC cell secretion.
CC -!- FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin
CC cells and noradrenergic neurons by acting as a non-competitive
CC nicotinic cholinergic antagonist. Can induce mast cell migration,
CC degranulation and production of cytokines and chemokines.
CC {ECO:0000250|UniProtKB:P10645}.
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. {ECO:0000250|UniProtKB:P26339}.
CC -!- SUBUNIT: Interacts with SCG3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Serpinin]: Secreted
CC {ECO:0000250|UniProtKB:P26339}. 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:0000250|UniProtKB:P10354}. 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 -!- PTM: O-glycosylated.
CC -!- PTM: Parathyroid CHGA is sulfated on tyrosine residues, whereas adrenal
CC CHGA seems to be mainly sulfated on oligosaccharide residues.
CC {ECO:0000269|PubMed:2105940}.
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; M20926; AAA31016.1; -; mRNA.
DR PIR; A32284; A32284.
DR RefSeq; NP_001157477.2; NM_001164005.2.
DR STRING; 9823.ENSSSCP00000002657; -.
DR GlyConnect; 94; 1 O-Linked glycan.
DR PaxDb; P04404; -.
DR PeptideAtlas; P04404; -.
DR GeneID; 397540; -.
DR KEGG; ssc:397540; -.
DR CTD; 1113; -.
DR eggNOG; ENOG502RZBD; Eukaryota.
DR InParanoid; P04404; -.
DR OrthoDB; 1127088at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042583; C:chromaffin granule; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0086030; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
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:0033604; P:negative regulation of catecholamine secretion; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IBA:GO_Central.
DR GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
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 Amidation; Calcium; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Oxidation; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Sulfation.
FT SIGNAL <1..16
FT CHAIN 17..446
FT /note="Chromogranin-A"
FT /id="PRO_0000005426"
FT PEPTIDE 256..304
FT /note="Pancreastatin"
FT /id="PRO_0000005427"
FT PEPTIDE 328..341
FT /note="WE-14"
FT /id="PRO_0000005428"
FT PEPTIDE 359..379
FT /note="Catestatin"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT /id="PRO_0000432692"
FT PEPTIDE 363..435
FT /note="Parastatin"
FT /id="PRO_0000005429"
FT PEPTIDE 382..406
FT /note="GE-25"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT /id="PRO_0000432693"
FT PEPTIDE 418..446
FT /note="Serpinin-RRG"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT /id="PRO_0000432694"
FT PEPTIDE 418..443
FT /note="Serpinin"
FT /evidence="ECO:0000250|UniProtKB:P26339"
FT /id="PRO_0000432695"
FT PEPTIDE 421..443
FT /note="p-Glu serpinin precursor"
FT /evidence="ECO:0000250|UniProtKB:P26339"
FT /id="PRO_0000432696"
FT REGION 85..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 304
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:3537810"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT MOD_RES 361
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT DISULFID 33..54
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 446 AA; 49328 MW; D9801F9596D39CD6 CRC64;
SAAALALLLC AGQVIALPVN SPMNKGDTEV MKCIVEVISD TLSKPSPMPV SQECFETLRG
DERILSILRH QNLLKELQDL ALQGAKERSH QQKKQSSYED ELSEVLEKQN DQAELKEGTE
EASSKEAAEK RGDSKEVEKN DEDADGAKPQ ASLEPPXXXE AEDQTPGEEE AASTHPLASL
PSKKRPGAQA EEDHEGPSQG PVDREKGPSA EQGPQAEREE EEEAEAGEKA VPEEEGPRSE
AFDSHPSLGY KEMQRGWPQA PAMDGAGKTG AEEAQPPEGK GAREHSRQEE EEETAGAPQG
LFRGGKRGEP AQEEEERLSE EWENAKRWSK MDRLAKELTA EKRLQGEEEE EEEEEDPDRS
MKLSFRAPAY GFRGPGLQLR RGWRPSSRED SVEAGLPLQV RXYLEEKKEE EGSANRRPED
QELESLSAIE AELEKVAPQL QSLRRG
