ANF_MOUSE
ID ANF_MOUSE Reviewed; 152 AA.
AC P05125; Q5FW59;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Natriuretic peptides A {ECO:0000303|PubMed:8760210};
DE AltName: Full=Atrial natriuretic factor prohormone {ECO:0000250|UniProtKB:P01160};
DE Short=preproANF {ECO:0000250|UniProtKB:P01161};
DE Short=proANF {ECO:0000303|PubMed:6542248};
DE AltName: Full=Atrial natriuretic peptide prohormone {ECO:0000250|UniProtKB:P01160};
DE Short=preproANP {ECO:0000250|UniProtKB:P01160};
DE Short=proANP {ECO:0000303|PubMed:11884416};
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:0000303|PubMed:8760210};
DE Short=ANP {ECO:0000303|PubMed:8760210};
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:0000303|PubMed:6542248};
DE Short=ANF {ECO:0000303|PubMed:6542248};
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;
GN Name=Nppa; Synonyms=Pnd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6542248; DOI=10.1126/science.6542248;
RA Seidman C.E., Bloch K.D., Klein K.A., Smith J.A., Seidman J.G.;
RT "Nucleotide sequences of the human and mouse atrial natriuretic factor
RT genes.";
RL Science 226:1206-1209(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION (ATRIAL NATRIURETIC PEPTIDE), AND DISRUPTION PHENOTYPE (ATRIAL
RP NATRIURETIC PEPTIDE).
RX PubMed=8760210; DOI=10.1152/ajpregu.1996.271.1.r109;
RA John S.W., Veress A.T., Honrath U., Chong C.K., Peng L., Smithies O.,
RA Sonnenberg H.;
RT "Blood pressure and fluid-electrolyte balance in mice with reduced or
RT absent ANP.";
RL Am. J. Physiol. 271:R109-R114(1996).
RN [7]
RP PROTEOLYTIC PROCESSING, CLEAVAGE SITE, AND MUTAGENESIS OF ARG-122; ARG-125
RP AND ARG-126.
RX PubMed=11884416; DOI=10.1074/jbc.m201503200;
RA Wu F., Yan W., Pan J., Morser J., Wu Q.;
RT "Processing of pro-atrial natriuretic peptide by corin in cardiac
RT myocytes.";
RL J. Biol. Chem. 277:16900-16905(2002).
RN [8]
RP FUNCTION (ATRIAL NATRIURETIC PEPTIDE).
RX PubMed=12890708; DOI=10.1038/sj.bjp.0705365;
RA Madhani M., Scotland R.S., MacAllister R.J., Hobbs A.J.;
RT "Vascular natriuretic peptide receptor-linked particulate guanylate
RT cyclases are modulated by nitric oxide-cyclic GMP signalling.";
RL Br. J. Pharmacol. 139:1289-1296(2003).
RN [9]
RP PROTEOLYTIC PROCESSING.
RX PubMed=15637153; DOI=10.1073/pnas.0407234102;
RA Chan J.C., Knudson O., Wu F., Morser J., Dole W.P., Wu Q.;
RT "Hypertension in mice lacking the proatrial natriuretic peptide convertase
RT corin.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:785-790(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION (ATRIAL NATRIURETIC PEPTIDE), AND DISRUPTION PHENOTYPE (ATRIAL
RP NATRIURETIC PEPTIDE).
RX PubMed=22437503; DOI=10.1038/nature10897;
RA Cui Y., Wang W., Dong N., Lou J., Srinivasan D.K., Cheng W., Huang X.,
RA Liu M., Fang C., Peng J., Chen S., Wu S., Liu Z., Dong L., Zhou Y., Wu Q.;
RT "Role of corin in trophoblast invasion and uterine spiral artery
RT remodelling in pregnancy.";
RL Nature 484:246-250(2012).
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 (PubMed:8760210,
CC PubMed:22437503, PubMed:12890708). Acts by specifically binding and
CC stimulating NPR1 to produce cGMP, which in turn activates effector
CC proteins, such as PRKG1, that drive various biological responses
CC (PubMed:12890708). 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 (PubMed:8760210, PubMed:22437503). Also
CC involved in inhibiting cardiac remodeling and cardiac hypertrophy by
CC inducing cardiomyocyte apoptosis and attenuating the growth of
CC cardiomyocytes and fibroblasts (By similarity). Plays a role in female
CC pregnancy by promoting trophoblast invasion and spiral artery
CC remodeling in uterus, and thus prevents pregnancy-induced hypertension
CC (PubMed:22437503). In adipose tissue, acts in various cGMP- and PKG-
CC dependent pathways to regulate lipid metabolism and energy homeostasis
CC (By similarity). This includes up-regulating lipid metabolism and
CC mitochondrial oxygen utilization by activating the AMP-activated
CC protein kinase (AMPK), and increasing energy expenditure by acting via
CC MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose
CC tissue (By similarity). Binds the clearance receptor NPR3 which removes
CC the hormone from circulation (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000269|PubMed:12890708,
CC ECO:0000269|PubMed:22437503, ECO:0000269|PubMed:8760210}.
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 -!- PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-
CC 122 to produce atrial natriuretic peptide (PubMed:11884416,
CC PubMed:15637153). Undergoes further proteolytic cleavage by unknown
CC proteases to give rise to long-acting natriuretic peptide, vessel
CC dilator and kaliuretic peptide (By similarity). Additional processing
CC gives rise to the auriculin and atriopeptin peptides (By similarity).
CC In the kidneys, alternative processing by an unknown protease results
CC in the peptide urodilatin (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161,
CC ECO:0000269|PubMed:11884416, ECO:0000269|PubMed:15637153}.
CC -!- PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates
CC degradation of the factor and thereby regulates its activity.
CC Degradation by IDE results in reduced activation of NPR1 (in vitro).
CC During IDE degradation, the resulting products can temporarily
CC stimulate NPR2 to produce cGMP, before the fragments are completely
CC 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-128 decreases vasorelaxant
CC activity. {ECO:0000250|UniProtKB:P01160}.
CC -!- DISRUPTION PHENOTYPE: Mice display increased arterial blood pressure
CC which is dietary salt intake independent (PubMed:8760210). During
CC pregnancy, increased blood pressure is observed, leading to late
CC gestational proteinuria and smaller litters (PubMed:22437503). Impaired
CC trophoblast invasion and smaller spiral arteries are also observed in
CC 12.5 dpc embryos (PubMed:22437503). In 18.5 dpc embryos, mice display
CC fewer trophoblasts and smaller arteries in the decidua and myometrium
CC than those in wild-type mice (PubMed:22437503).
CC {ECO:0000269|PubMed:22437503, ECO:0000269|PubMed:8760210}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
CC -!- CAUTION: [Long-acting natriuretic peptide]: Results concerning the
CC involvement of this peptide in blood volume and blood pressure
CC homeostasis are conflicting. Several studies utilising in vitro and
CC heterologous expression systems show that it is able to activate cGMP
CC and promote vasodilation and natriuresis (By similarity). However, an
CC in vivo study in rat found that it is not sufficient to induce any
CC diuretic, natriuretic, nor hypotensive responses, and is unable to bind
CC NPR1 nor increase guanylyl cyclase activity (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- CAUTION: [Vessel dilator]: Results concerning the involvement of this
CC peptide in blood volume and blood pressure homeostasis are conflicting.
CC Several studies utilising in vitro and heterologous expression systems
CC show that it is able to activate cGMP and promote vasodilation and
CC natriuresis (By similarity). However, a heterologous and in vivo
CC expression study in rat found that it is not sufficient to induce any
CC diuretic, natriuretic, nor hypotensive responses, and is unable to bind
CC NPR1 nor increase guanylyl cyclase activity (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K02781; AAA37235.1; -; Genomic_DNA.
DR EMBL; AK147180; BAE27742.1; -; mRNA.
DR EMBL; AL714013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466594; EDL14792.1; -; Genomic_DNA.
DR EMBL; BC089615; AAH89615.1; -; mRNA.
DR CCDS; CCDS18927.1; -.
DR PIR; A29370; AWMS.
DR RefSeq; NP_032751.1; NM_008725.3.
DR AlphaFoldDB; P05125; -.
DR BMRB; P05125; -.
DR BioGRID; 231051; 1.
DR IntAct; P05125; 3.
DR STRING; 10090.ENSMUSP00000099520; -.
DR iPTMnet; P05125; -.
DR PhosphoSitePlus; P05125; -.
DR PaxDb; P05125; -.
DR PeptideAtlas; P05125; -.
DR PRIDE; P05125; -.
DR ProteomicsDB; 296035; -.
DR Antibodypedia; 13911; 763 antibodies from 40 providers.
DR Ensembl; ENSMUST00000103230; ENSMUSP00000099520; ENSMUSG00000041616.
DR GeneID; 230899; -.
DR KEGG; mmu:230899; -.
DR UCSC; uc008vtq.1; mouse.
DR CTD; 4878; -.
DR MGI; MGI:97367; Nppa.
DR VEuPathDB; HostDB:ENSMUSG00000041616; -.
DR eggNOG; ENOG502S9RQ; Eukaryota.
DR GeneTree; ENSGT00940000154513; -.
DR HOGENOM; CLU_144536_0_0_1; -.
DR InParanoid; P05125; -.
DR OMA; LSEVPPW; -.
DR OrthoDB; 1596502at2759; -.
DR TreeFam; TF106304; -.
DR Reactome; R-MMU-5578768; Physiological factors.
DR BioGRID-ORCS; 230899; 6 hits in 72 CRISPR screens.
DR PRO; PR:P05125; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P05125; protein.
DR Bgee; ENSMUSG00000041616; Expressed in cardiac atrium and 79 other tissues.
DR Genevisible; P05125; MM.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0042629; C:mast cell granule; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0051427; F:hormone receptor binding; ISO:MGI.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISO:MGI.
DR GO; GO:0071855; F:neuropeptide receptor binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IDA:MGI.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0007565; P:female pregnancy; IMP:UniProtKB.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:1903815; P:negative regulation of collecting lymphatic vessel constriction; ISO:MGI.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:MGI.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; ISO:MGI.
DR GO; GO:1903766; P:positive regulation of potassium ion export across plasma membrane; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:MGI.
DR GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
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 PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cleavage on pair of basic residues; Disulfide bond;
KW Hormone; Phosphoprotein; Reference proteome; Secreted; Signal; Vasoactive;
KW Vasodilator.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P24259"
FT CHAIN 25..150
FT /note="Natriuretic peptides A"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449735"
FT PROPEP 25..122
FT /evidence="ECO:0000305"
FT /id="PRO_0000001495"
FT PEPTIDE 25..54
FT /note="Long-acting natriuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449736"
FT PEPTIDE 55..91
FT /note="Vessel dilator"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449737"
FT PROPEP 92..102
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449738"
FT PEPTIDE 103..122
FT /note="Kaliuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449739"
FT PEPTIDE 118..150
FT /note="Auriculin-C"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449740"
FT PEPTIDE 119..150
FT /note="Urodilatin"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449741"
FT PEPTIDE 120..144
FT /note="Auriculin-D"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449742"
FT PEPTIDE 123..150
FT /note="Atrial natriuretic peptide"
FT /evidence="ECO:0000269|PubMed:11884416"
FT /id="PRO_0000391784"
FT PEPTIDE 126..150
FT /note="Auriculin-B"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000001496"
FT PEPTIDE 126..149
FT /note="Auriculin-A"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000001497"
FT PEPTIDE 127..150
FT /note="Atriopeptin-3"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449743"
FT PEPTIDE 127..149
FT /note="Atriopeptin-1"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000001498"
FT PEPTIDE 127..147
FT /note="Atriopeptin-2"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000001499"
FT REGION 76..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..150
FT /note="Important for degradation of atrial natriuretic
FT peptide by IDE"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT SITE 122..123
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000269|PubMed:11884416"
FT SITE 129..130
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT DISULFID 129..145
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT MUTAGEN 122
FT /note="R->A: Abolishes maturation and cleavage by CORIN."
FT /evidence="ECO:0000269|PubMed:11884416"
FT MUTAGEN 125
FT /note="R->A: Does not affect maturation and cleavage by
FT CORIN."
FT /evidence="ECO:0000269|PubMed:11884416"
FT MUTAGEN 126
FT /note="R->A: Does not affect maturation and cleavage by
FT CORIN."
FT /evidence="ECO:0000269|PubMed:11884416"
FT CONFLICT 96..97
FT /note="LG -> SR (in Ref. 1; AAA37235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 16572 MW; 1693D134B5FCA23D CRC64;
MGSFSITLGF FLVLAFWLPG HIGANPVYSA VSNTDLMDFK NLLDHLEEKM PVEDEVMPPQ
ALSEQTEEAG AALSSLPEVP PWTGEVNPPL RDGSALGRSP WDPSDRSALL KSKLRALLAG
PRSLRRSSCF GGRIDRIGAQ SGLGCNSFRY RR
