CMGA_HORSE
ID CMGA_HORSE Reviewed; 448 AA.
AC Q9XS63;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Chromogranin-A;
DE Short=CgA;
DE Contains:
DE RecName: Full=Pancreastatin;
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;
GN Name=CHGA;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Adrenal medulla;
RX PubMed=11039590; DOI=10.1292/jvms.62.953;
RA Sato F., Hasegawa T., Katayama Y., Iwanaga T., Yanaihara N., Kanno T.,
RA Ishida N.;
RT "Molecular cloning of equine chromogranin A and its expression in endocrine
RT and exocrine tissues.";
RL J. Vet. Med. Sci. 62:953-959(2000).
CC -!- FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin
CC release from the pancreas.
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 -!- TISSUE SPECIFICITY: Highly expressed in adrenal medulla and pituitary
CC gland. Weaker expression detected in cerebrum, cerebellum, spinal cord,
CC liver, thyroid gland, striated muscle, lung, spleen, kidney, parotid
CC gland, and sublingual gland. {ECO:0000269|PubMed:11039590}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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; AB025570; BAA76748.1; -; mRNA.
DR RefSeq; NP_001075283.2; NM_001081814.2.
DR AlphaFoldDB; Q9XS63; -.
DR SMR; Q9XS63; -.
DR STRING; 9796.ENSECAP00000030274; -.
DR PaxDb; Q9XS63; -.
DR GeneID; 100033828; -.
DR KEGG; ecb:100033828; -.
DR CTD; 1113; -.
DR InParanoid; Q9XS63; -.
DR OrthoDB; 1127088at2759; -.
DR Proteomes; UP000002281; 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:0050886; P:endocrine process; NAS: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 2: Evidence at transcript level;
KW Amidation; Calcium; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Oxidation;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..448
FT /note="Chromogranin-A"
FT /id="PRO_0000005405"
FT PEPTIDE 260..308
FT /note="Pancreastatin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005406"
FT PEPTIDE 333..346
FT /note="WE-14"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005407"
FT PEPTIDE 361..381
FT /note="Catestatin"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT /id="PRO_0000432677"
FT PEPTIDE 384..408
FT /note="GE-25"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT /id="PRO_0000432678"
FT PEPTIDE 420..448
FT /note="Serpinin-RRG"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT /id="PRO_0000432679"
FT PEPTIDE 420..445
FT /note="Serpinin"
FT /evidence="ECO:0000250|UniProtKB:P26339"
FT /id="PRO_0000432680"
FT PEPTIDE 423..445
FT /note="p-Glu serpinin precursor"
FT /evidence="ECO:0000250|UniProtKB:P26339"
FT /id="PRO_0000432681"
FT REGION 116..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 308
FT /note="Glycine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT MOD_RES 363
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P10645"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05059"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10354"
FT DISULFID 35..56
FT /evidence="ECO:0000250"
SQ SEQUENCE 448 AA; 49861 MW; EC2D6418F5BA5274 CRC64;
MRSAVVLALL LCAGQVIALP VNSPMDTGDT EVMKCIVEVI SDTLSKPSPV PVSQECFETL
RGDERILSIL RHQNLLKELQ DLALQGAKER APQQKHSRLE DELAEVLEKQ NHQAELKEVT
EEALSEDAAE ARGDSKEVEE NGEDADGARP QAALEPEQES RVEDAQAPGE EKEAINTHSP
TRLPSQKHPD PQAEGDSDSP SQGLVDREKG LGAERGQQAK REEEEDEAGE KADAEEEGPT
AAFNPHPSLS YKIRKGESWS EALVVDGARK TGAEEAQPPE GQGEREHSRQ EEEEEEETAG
ASRGLFRGGK SRELEQEKEQ ERLSKEWEDA KRWSKMDQLA KELTAEKRLE GEDEEEDDPD
RSMKLSFRAR AYGFRGPGLQ LRRGWRPSSR EDSIEAGLPP PVRGYPEEKK EEEGSANRRP
EDQELESLSA IEAELEKVAH QLQALRRG
