ANF_CAVPO
ID ANF_CAVPO Reviewed; 128 AA.
AC P27596;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Natriuretic peptides A {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor prohormone {ECO:0000250|UniProtKB:P01160};
DE Short=preproANF {ECO:0000250|UniProtKB:P01161};
DE Short=proANF {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Atrial natriuretic peptide prohormone {ECO:0000250|UniProtKB:P01160};
DE Short=preproANP {ECO:0000250|UniProtKB:P01160};
DE Short=proANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Atriopeptigen {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Cardiodilatin {ECO:0000250|UniProtKB:P01160};
DE Short=CDD {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=preproCDD-ANF {ECO:0000250|UniProtKB:P01160};
DE Contains:
DE RecName: Full=Long-acting natriuretic peptide {ECO:0000250|UniProtKB:P01160};
DE Short=LANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Long-acting natriuretic hormone {ECO:0000305};
DE Short=LANH {ECO:0000305};
DE AltName: Full=Pro atrial natriuretic factor 1-30 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 1-30 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 1-30 {ECO:0000305};
DE Short=proANP 1-30 {ECO:0000305};
DE Contains:
DE RecName: Full=Vessel dilator {ECO:0000250|UniProtKB:P01160};
DE Short=VSDL {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic factor 31-67 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 31-67 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 31-67 {ECO:0000305};
DE Short=proANP 31-67 {ECO:0000305};
DE Contains:
DE RecName: Full=Kaliuretic peptide {ECO:0000250|UniProtKB:P01160};
DE Short=KP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic factor 79-98 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 79-98 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 79-98 {ECO:0000305};
DE Short=proANP 79-98 {ECO:0000305};
DE Contains:
DE RecName: Full=Urodilatin {ECO:0000250|UniProtKB:P01160};
DE Short=URO {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD 95-126 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD-ANP (95-126) {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 95-126 {ECO:0000250|UniProtKB:P01160};
DE Short=proANP 95-126 {ECO:0000250|UniProtKB:P01160};
DE Contains:
DE RecName: Full=Auriculin-C {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor 1-33 {ECO:0000250|UniProtKB:P01161};
DE Short=ANF 1-33 {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Auriculin-D {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor 3-33 {ECO:0000250|UniProtKB:P01161};
DE Short=ANF 3-33 {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atrial natriuretic peptide {ECO:0000250|UniProtKB:P01160};
DE Short=ANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Alpha-atrial natriuretic peptide {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Alpha-hANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Atrial natriuretic factor {ECO:0000250|UniProtKB:P01160};
DE Short=ANF {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD-ANF {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD-ANP (99-126) {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Cardionatrin {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Pro atrial natriuretic factor 99-126 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 99-126 {ECO:0000250|UniProtKB:P01160};
DE Contains:
DE RecName: Full=Auriculin-B {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor 8-33 {ECO:0000250|UniProtKB:P01161};
DE Short=ANF 8-33 {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Auriculin-A {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atriopeptin-1 {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Atriopeptin I {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atriopeptin-2 {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Atriopeptin II {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atriopeptin-3 {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Atriopeptin III {ECO:0000250|UniProtKB:P01161};
DE Flags: Precursor; Fragment;
GN Name=NPPA;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart atrium;
RA Maegert H.-J., Hanke M., Schmeding G., Teuteberg K., Schulz-Knappe P.,
RA Forssmann W.-G.;
RL Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role
CC in mediating cardio-renal homeostasis, and is involved in vascular
CC remodeling and regulating energy metabolism. Acts by specifically
CC binding and stimulating NPR1 to produce cGMP, which in turn activates
CC effector proteins, such as PRKG1, that drive various biological
CC responses. Regulates vasodilation, natriuresis, diuresis and
CC aldosterone synthesis and is therefore essential for regulating blood
CC pressure, controlling the extracellular fluid volume and maintaining
CC the fluid-electrolyte balance. Also involved in inhibiting cardiac
CC remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis
CC and attenuating the growth of cardiomyocytes and fibroblasts (By
CC similarity). Plays a role in female pregnancy by promoting trophoblast
CC invasion and spiral artery remodeling in uterus, and thus prevents
CC pregnancy-induced hypertension (By similarity). In adipose tissue, acts
CC in various cGMP- and PKG-dependent pathways to regulate lipid
CC metabolism and energy homeostasis. This includes up-regulating lipid
CC metabolism and mitochondrial oxygen utilization by activating the AMP-
CC activated protein kinase (AMPK), and increasing energy expenditure by
CC acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown
CC adipose tissue. Binds the clearance receptor NPR3 which removes the
CC hormone from circulation (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125}.
CC -!- FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-
CC renal homeostasis through regulation of natriuresis, diuresis,
CC vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes
CC the production of cGMP and induces vasodilation. May promote
CC natriuresis, at least in part, by enhancing prostaglandin E2 synthesis
CC resulting in the inhibition of renal Na+-K+-ATPase (By similarity).
CC However reports on the involvement of this peptide in mammal blood
CC volume and blood pressure homeostasis are conflicting; according to a
CC report, in vivo it is not sufficient to activate cGMP and does not
CC inhibit collecting duct transport nor effect diuresis and natriuresis
CC (By similarity). Appears to bind to specific receptors that are
CC distinct from the receptors bound by atrial natriuretic peptide and
CC vessel dilator. Possibly enhances protein excretion in urine by
CC decreasing proximal tubular protein reabsorption (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis, diuresis, and vasodilation. In
CC vitro, promotes the production of cGMP and induces vasodilation. May
CC promote natriuresis, at least in part, by enhancing prostaglandin E2
CC synthesis resulting in the inhibition of renal Na+-K+-ATPase. However
CC reports on the involvement of this peptide in mammal blood volume and
CC blood pressure homeostasis are conflicting; according to a report it is
CC not sufficient to activate cGMP and does not inhibit collecting duct
CC transport nor effect diuresis and natriuresis. Appears to bind to
CC specific receptors that are distinct from the receptors bound by the
CC atrial natriuretic and long-acting natriuretic peptides. Possibly
CC functions in protein excretion in urine by maintaining the integrity of
CC the proximal tubules and enhancing protein excretion by decreasing
CC proximal tubular protein reabsorption. {ECO:0000250|UniProtKB:P01160}.
CC -!- FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal
CC homeostasis through regulation of diuresis and inhibiting aldosterone
CC synthesis. In vitro, promotes the production of cGMP and induces
CC vasodilation. May promote natriuresis, at least in part, by enhancing
CC prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-
CC ATPase. May have a role in potassium excretion but not sodium excretion
CC (natriuresis). Possibly enhances protein excretion in urine by
CC decreasing proximal tubular protein reabsorption.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to
CC be important for maintaining cardio-renal homeostasis. Mediates
CC vasodilation, natriuresis and diuresis primarily in the renal system,
CC in order to maintain the extracellular fluid volume and control the
CC fluid-electrolyte balance. Specifically binds and stimulates cGMP
CC production by renal transmembrane receptors, likely NPR1. Urodilatin
CC not ANP, may be the natriuretic peptide responsible for the regulation
CC of sodium and water homeostasis in the kidney.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis and in vitro, vasodilates renal artery strips.
CC {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis and in vitro, vasodilates renal artery strips.
CC {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis
CC through regulation of regulation of natriuresis and vasodilation. In
CC vivo promotes natriuresis. In vitro, vasodilates intestinal smooth
CC muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis. In vitro, selectively vasodilates intestinal and vascular
CC smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis. In vitro, selectively vasodilates intestinal smooth muscle
CC but not vascular smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
CC -!- SUBUNIT: [Atrial natriuretic peptide]: Homodimer; disulfide-linked
CC antiparallel dimer. {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Vessel dilator]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Urodilatin]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in
CC blood. Increased electrolytes, osmolality and intracellular cAMP levels
CC increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Perikaryon
CC {ECO:0000250|UniProtKB:P01160}. Cell projection
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in
CC urine in one study. However, in another study, was not detected in
CC urine. Detected in cytoplasmic bodies and neuronal processes of
CC pyramidal neurons (layers II-VI) (By similarity). Increased secretion
CC in response to the vasopressin AVP (By similarity). Likely to be
CC secreted in response to an increase in atrial pressure or atrial
CC stretch. In kidney cells, secretion increases in response to activated
CC guanylyl cyclases and increased intracellular cAMP levels. Plasma
CC levels increase 15 minutes after a high-salt meal, and decrease back to
CC normal plasma levels 1 hr later (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted
CC {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase
CC in secretion in response to the vasopressin AVP.
CC {ECO:0000250|UniProtKB:P01161}.
CC -!- DEVELOPMENTAL STAGE: Adult.
CC -!- PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-
CC 98 to produce atrial natriuretic peptide. Undergoes further proteolytic
CC cleavage by unknown proteases to give rise to long-acting natriuretic
CC peptide, vessel dilator and kaliuretic peptide (By similarity).
CC Additional processing gives rise to the auriculin and atriopeptin
CC peptides (By similarity). In the kidneys, alternative processing by an
CC unknown protease results in the peptide urodilatin (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates
CC degradation of the factor and thereby regulates its activity. Degraded
CC by IDE (in vitro). During IDE degradation, the resulting products can
CC temporarily stimulate NPR2 to produce cGMP, before the fragments are
CC completely degraded and inactivated by IDE (in vitro).
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.
CC -!- PTM: [Urodilatin]: Phosphorylation on Ser-104 decreases vasorelaxant
CC activity. {ECO:0000250|UniProtKB:P01160}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR EMBL; X58562; CAA41442.1; -; mRNA.
DR PIR; S14872; S14872.
DR AlphaFoldDB; P27596; -.
DR STRING; 10141.ENSCPOP00000015551; -.
DR ChEMBL; CHEMBL3097985; -.
DR eggNOG; ENOG502S9RQ; Eukaryota.
DR InParanoid; P27596; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR InterPro; IPR002407; Natriuretic_peptide_atrial.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00711; ANATPEPTIDE.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Disulfide bond; Hormone; Phosphoprotein;
KW Reference proteome; Secreted; Vasoactive.
FT CHAIN 1..128
FT /note="Natriuretic peptides A"
FT /id="PRO_0000451942"
FT PEPTIDE 1..30
FT /note="Long-acting natriuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000001486"
FT PEPTIDE 31..67
FT /note="Vessel dilator"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000451943"
FT PROPEP 68..78
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000451944"
FT PEPTIDE 79..98
FT /note="Kaliuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000451945"
FT PEPTIDE 94..126
FT /note="Auriculin-C"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451946"
FT PEPTIDE 95..126
FT /note="Urodilatin"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000451947"
FT PEPTIDE 96..120
FT /note="Auriculin-D"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451948"
FT PEPTIDE 99..126
FT /note="Atrial natriuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000001487"
FT PEPTIDE 102..126
FT /note="Auriculin-B"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451949"
FT PEPTIDE 102..125
FT /note="Auriculin-A"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451950"
FT PEPTIDE 103..126
FT /note="Atriopeptin-3"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451951"
FT PEPTIDE 103..125
FT /note="Atriopeptin-2"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451952"
FT PEPTIDE 103..123
FT /note="Atriopeptin-1"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000451953"
FT REGION 36..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..126
FT /note="Important for degradation of atrial natriuretic
FT peptide by IDE"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT SITE 98..99
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT SITE 105..106
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT DISULFID 105..121
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT NON_TER 1
SQ SEQUENCE 128 AA; 13966 MW; EFC5004B4DDEF318 CRC64;
NPMYNVVSNA DLVDFKNLLD HLEEKMPLED EVVLPQVASE QNEEAGAVLS ALPEVPSWPG
EAGPAQREGG ALGRGPWDSS DRSAPLKSKL RALLDAPRSL RRSSCFGGRM DRIGAQSSLG
CNSFRYRR
