ID   A5HUP2_TURTR            Unreviewed;       152 AA.
AC   A5HUP2;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   02-SEP-2026, entry version 75.
DE   RecName: Full=Natriuretic peptides A {ECO:0000256|ARBA:ARBA00020078};
DE   AltName: Full=Atrial natriuretic factor prohormone {ECO:0000256|ARBA:ARBA00031619};
DE   AltName: Full=Atrial natriuretic peptide prohormone {ECO:0000256|ARBA:ARBA00032736};
DE   AltName: Full=Atriopeptigen {ECO:0000256|ARBA:ARBA00031144};
DE   AltName: Full=Cardiodilatin {ECO:0000256|ARBA:ARBA00030903};
DE   AltName: Full=preproCDD-ANF {ECO:0000256|ARBA:ARBA00033220};
DE   Flags: Fragment;
GN   Name=ANP {ECO:0000313|EMBL:BAF62627.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|EMBL:BAF62627.1};
RN   [1] {ECO:0000313|EMBL:BAF62627.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Naka T., Katsumata E., Sasaki K., Minamino N., Yoshioka M., Takei Y.;
RT   "Natriuretic peptides in cetaceans: Identification, molecular
RT   characterization and changes in plasma concentration after landing.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hormone produced in the kidneys that appears to be important
CC       for maintaining cardio-renal homeostasis. Mediates vasodilation,
CC       natriuresis and diuresis primarily in the renal system, in order to
CC       maintain the extracellular fluid volume and control the fluid-
CC       electrolyte balance. Specifically binds and stimulates cGMP production
CC       by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may
CC       be the natriuretic peptide responsible for the regulation of sodium and
CC       water homeostasis in the kidney. {ECO:0000256|ARBA:ARBA00002857}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of diuresis and inhibiting aldosterone synthesis. In vitro,
CC       promotes 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. May have a role in
CC       potassium excretion but not sodium excretion (natriuresis). Possibly
CC       enhances protein excretion in urine by decreasing proximal tubular
CC       protein reabsorption. {ECO:0000256|ARBA:ARBA00003298}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis and vasodilation. In vivo promotes
CC       natriuresis and in vitro, vasodilates renal artery strips.
CC       {ECO:0000256|ARBA:ARBA00002352}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis and vasodilation. In vivo promotes
CC       natriuresis. In vitro, selectively vasodilates intestinal and vascular
CC       smooth muscle strips. {ECO:0000256|ARBA:ARBA00003360}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       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:0000256|ARBA:ARBA00002948}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis, diuresis, and vasodilation. In vitro,
CC       promotes 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. However reports on
CC       the involvement of this peptide in mammal blood volume and blood
CC       pressure homeostasis are conflicting; according to a report it is not
CC       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:0000256|ARBA:ARBA00002727}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis, diuresis, vasodilation, and inhibiting
CC       aldosterone synthesis. In vitro, promotes the production of cGMP and
CC       induces vasodilation. May promote natriuresis, at least in part, by
CC       enhancing prostaglandin E2 synthesis resulting in the inhibition of
CC       renal Na+-K+-ATPase. However reports on the involvement of this peptide
CC       in mammal blood volume and blood pressure homeostasis are conflicting;
CC       according to a report, in vivo it is not sufficient to activate cGMP
CC       and does not inhibit collecting duct transport nor effect diuresis and
CC       natriuresis. Appears to bind to specific receptors that are distinct
CC       from the receptors bound by atrial natriuretic peptide and vessel
CC       dilator. Possibly enhances protein excretion in urine by decreasing
CC       proximal tubular protein reabsorption. {ECO:0000256|ARBA:ARBA00045221}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of regulation of natriuresis and vasodilation. In vivo
CC       promotes natriuresis. In vitro, vasodilates intestinal smooth muscle
CC       but not smooth muscle strips. {ECO:0000256|ARBA:ARBA00003244}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked antiparallel dimer.
CC       {ECO:0000256|ARBA:ARBA00011384}.
CC   -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000256|ARBA:ARBA00004484}.
CC       Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU003686}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family.
CC       {ECO:0000256|ARBA:ARBA00009041, ECO:0000256|RuleBase:RU003686}.
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DR   EMBL; AB284172; BAF62627.1; -; mRNA.
DR   AlphaFoldDB; A5HUP2; -.
DR   STRING; 9739.ENSTTRP00000010897; -.
DR   GeneID; 101317132; -.
DR   CTD; 4878; -.
DR   OrthoDB; 8865096at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:InterPro.
DR   GO; GO:0051427; F:hormone receptor binding; IEA:TreeGrafter.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IEA:TreeGrafter.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IEA:TreeGrafter.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   InterPro; IPR050787; Natriuretic_peptide.
DR   InterPro; IPR002407; Natriuretic_peptide_atrial.
DR   PANTHER; PTHR14066; ATRIAL NATRIURETIC FACTOR PRECURSOR; 1.
DR   PANTHER; PTHR14066:SF2; NATRIURETIC PEPTIDES A; 1.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00711; ANATPEPTIDE.
DR   PRINTS; PR00710; NATPEPTIDES.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hormone {ECO:0000256|ARBA:ARBA00022702};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Vasoactive {ECO:0000256|ARBA:ARBA00022858, ECO:0000256|RuleBase:RU003686};
KW   Vasodilator {ECO:0000256|ARBA:ARBA00022429}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..152
FT                   /note="Natriuretic peptides A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5048112081"
FT   REGION          61..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAF62627.1"
SQ   SEQUENCE   152 AA;  16427 MW;  C71074B6089FA082 CRC64;
     MGSATIAASF LLFLAFQLPG QTGANPVYGS VSNADLMDFK NLLDHLEDKM PLEDEAMPQQ
     VLSDQNEEAG VPLSPLSEVP PWTGEVHPAQ RDGGALGRGP WEPSDRSALL NSKLRALLAA
     PRSLRRSSCF GGRMDRIGAQ SGLGCNSFRY RR
//