P10354
uniprot
P10354
canonical
amino_acid_sequence
MRSSAALALLLCAGQVFALPVNSPMTKGDTKVMKCVLEVISDSLSKPSPMPVSPECLETLQGDERVLSILRHQNLLKELQDLALQGAKERAQQQQQQQQQQQQQQQQQQQQHSSFEDELSEVFENQSPAAKHGDAASEAPSKDTVEKREDSDKGQQDAFEGTTEGPRPQAFPEPKQESSMMGNSQSPGEDTANNTQSPTSLPSQEHGIPQTTEGSERGPSAQQQARKAKQEEKEEEEEEKEEEEEEKEEKAIAREKAGPKEVPTAASSSHFYSGYKKIQKDDDGQSESQAVNGKTGASEAVPSEGKGELEHSQQEEDGEEAMAGPPQGLFPGGKGQELERKQQEEEEEEERLSREWEDKRWSRMDQLAKELTAEKRLEGEDDPDRSMKLSFRARAYGFRDPGPQLRRGWRPSSREDSVEARGDFEEKKEEEGSANRRAEDQELESLSAIEAELEKVAHQLQALRRG
uniprot
proteins
function
FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin release from the pancreas.; FUNCTION: 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. {ECO:0000250|UniProtKB:P10645}.; FUNCTION: 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). {ECO:0000250|UniProtKB:P26339, ECO:0000269|PubMed:22459152}.
uniprot
proteins
mass_dalton
52024
uniprot
proteins
post_translational_modification
PTM: O-glycosylated; contains chondroitin sulfate (CS). CS attachment is pH-dependent, being observed at mildly acidic conditions of pH 5 but not at neutral pH, and promotes self-assembly in vitro. {ECO:0000250|UniProtKB:P10645}.
uniprot
proteins
protein_family
Chromogranin/secretogranin protein family
uniprot
proteins
pubmed
12388744
uniprot
proteins
pubmed
14597614
uniprot
proteins
pubmed
22459152
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2828116
uniprot
proteins
pubmed
29166604
uniprot
proteins
pubmed
3044825
uniprot
proteins
pubmed
3896848
uniprot
proteins
sequence_length
466
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744, ECO:0000269|PubMed:3896848}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000269|PubMed:29166604}. Secreted. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions. In pituitary gonadotropes, located in large secretory granules.; SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.
uniprot
proteins