Detail Information for IndEnz0002016769
IED ID IndEnz0002016769
Enzyme Type ID protease016769
Protein Name Natriuretic peptides A
Atrial natriuretic factor prohormone
preproANF
proANF
Atrial natriuretic peptide prohormone
preproANP
proANP
Atriopeptigen
Cardiodilatin
CDD
preproCDD-ANF

Cleaved into: Long-acting natriuretic peptide
LANP
Long-acting natriuretic hormone
LANH
Pro atrial natriuretic factor 1-30
proANF 1-30
Pro atrial natriuretic peptide 1-30
proANP 1-30
; Vessel dilator
VSDL
Pro atrial natriuretic factor 31-67
proANF 31-67
Pro atrial natriuretic peptide 31-67
proANP 31-67
; Kaliuretic peptide
KP
Pro atrial natriuretic factor 79-98
proANF 79-98
Pro atrial natriuretic peptide 79-98
proANP 79-98
; Urodilatin
URO
CDD 95-126
CDD-ANP
95-126
Pro atrial natriuretic peptide 95-126
proANP 95-126
; Auriculin-C
Atrial natriuretic factor 1-33
ANF 1-33
; Auriculin-D
Atrial natriuretic factor 3-33
ANF 3-33
; Atrial natriuretic peptide
ANP
Alpha-atrial natriuretic peptide
Alpha-hANP
Atrial natriuretic factor
ANF
CDD-ANF
CDD-ANP
99-126
Cardionatrin
Pro atrial natriuretic factor 99-126
proANF 99-126
; Auriculin-B
Atrial natriuretic factor 8-33
ANF 8-33
; Auriculin-A; Atriopeptin-1
Atriopeptin I
; Atriopeptin-2
Atriopeptin II
; Atriopeptin-3
Atriopeptin III
Gene Name NPPA
Organism Felis catus (Cat) (Felis silvestris catus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Carnivora Feliformia Felidae (cat family) Felinae Felis Felis catus (Cat) (Felis silvestris catus)
Enzyme Sequence MGSFSTITASFLLFLACQLLWQTGANPVYGSVSNADLMDFKNLLDHLEDKMPLEDEVVPPQVLSEQNEEAGAALSPLPEVPPWAGEVNPAQRDGGALGRGSWDSSDRSALLKSKLRALLAAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRYRR
Enzyme Length 153
Uniprot Accession Number Q9GLD0
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (By similarity). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (By similarity). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (By similarity). In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis (By similarity). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (By similarity). Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125}.; FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity). However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report, in vivo it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis (By similarity). Appears to bind to specific receptors that are distinct from the receptors bound by atrial natriuretic peptide and vessel dilator. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. However reports on the involvement of this peptide in mammal blood volume and blood pressure homeostasis are conflicting; according to a report it is not sufficient to activate cGMP and does not inhibit collecting duct transport nor effect diuresis and natriuresis. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. Possibly functions in protein excretion in urine by maintaining the integrity of the proximal tubules and enhancing protein excretion by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney. {ECO:0000250|UniProtKB:P01160}.; FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis and in vitro, vasodilates renal artery strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis through regulation of regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, vasodilates intestinal smooth muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal and vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.; FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis through regulation of natriuresis and vasodilation. In vivo promotes natriuresis. In vitro, selectively vasodilates intestinal smooth muscle but not vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (1); Modified residue (1); Peptide (12); Propeptide (2); Region (2); Signal peptide (1); Site (2)
Keywords Cell projection;Disulfide bond;Hormone;Phosphoprotein;Reference proteome;Secreted;Signal;Vasoactive;Vasodilator
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Urodilatin]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in blood. Increased electrolytes, osmolality and intracellular cAMP levels increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Perikaryon {ECO:0000250|UniProtKB:P01160}. Cell projection {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in urine in one study. However, in another study, was not detected in urine. Detected in cytoplasmic bodies and neuronal processes of pyramidal neurons (layers II-VI) (By similarity). Increased secretion in response to the vasopressin AVP (By similarity). Likely to be secreted in response to an increase in atrial pressure or atrial stretch. In kidney cells, secretion increases in response to activated guanylyl cyclases and increased intracellular cAMP levels. Plasma levels increase 15 minutes after a high-salt meal, and decrease back to normal plasma levels 1 hr later (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase in secretion in response to the vasopressin AVP. {ECO:0000250|UniProtKB:P01161}.
Modified Residue MOD_RES 129; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P01160
Post Translational Modification PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-123 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing gives rise to the auriculin and atriopeptin peptides (By similarity). In the kidneys, alternative processing by an unknown protease results in the peptide urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.; PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates degradation of the factor and thereby regulates its activity. Degradation by IDE results in reduced activation of NPR1 (in vitro). During IDE degradation, the resulting products can temporarily stimulate NPR2 to produce cGMP, before the fragments are completely degraded and inactivated by IDE (in vitro). {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.; PTM: [Urodilatin]: Phosphorylation on Ser-129 decreases vasorelaxant activity. {ECO:0000250|UniProtKB:P01160}.
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000250|UniProtKB:P24259
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 16,583
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda