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Natriuretic peptides A (Prepronatriodilatin) [Cleaved into: Atrial natriuretic factor (ANF) (Atrial natriuretic peptide) (ANP); Auriculin-B; Auriculin-A; Atriopeptin-1 (Atriopeptin I); Atriopeptin-2 (Atriopeptin II); Atriopeptin-3 (Atriopeptin III)]

 ANF_RAT                 Reviewed;         152 AA.
P01161;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
31-JAN-2018, entry version 151.
RecName: Full=Natriuretic peptides A;
AltName: Full=Prepronatriodilatin;
Contains:
RecName: Full=Atrial natriuretic factor;
Short=ANF;
AltName: Full=Atrial natriuretic peptide;
Short=ANP;
Contains:
RecName: Full=Auriculin-B;
Contains:
RecName: Full=Auriculin-A;
Contains:
RecName: Full=Atriopeptin-1;
AltName: Full=Atriopeptin I;
Contains:
RecName: Full=Atriopeptin-2;
AltName: Full=Atriopeptin II;
Contains:
RecName: Full=Atriopeptin-3;
AltName: Full=Atriopeptin III;
Flags: Precursor;
Name=Nppa;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6547210; DOI=10.1038/309719a0;
Yamanaka M., Greenberg B., Johnson L., Seilhamer J.J., Brewer M.,
Friedemann T., Miller J., Atlas S.A., Laragh J., Lewicki J.,
Fiddes J.C.;
"Cloning and sequence analysis of the cDNA for the rat atrial
natriuretic factor precursor.";
Nature 309:719-722(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6328328; DOI=10.1038/309722a0;
Maki M., Takayanagi R., Misono K.S., Pandey K.N., Tibbetts C.,
Inagami T.;
"Structure of rat atrial natriuretic factor precursor deduced from
cDNA sequence.";
Nature 309:722-724(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6234658; DOI=10.1126/science.6234658;
Seidman C.E., Duby A.D., Choi E., Graham R.M., Haber E., Homcy C.,
Smith J.A., Seidman J.G.;
"The structure of rat preproatrial natriuretic factor as defined by a
complementary DNA clone.";
Science 225:324-326(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6239103; DOI=10.1038/312152a0;
Kangawa K., Tawaragi Y., Oikawa S., Mizuno A., Sakuragawa Y.,
Nakazato H., Fukuda A., Minamino N., Matsuo H.;
"Identification of rat gamma atrial natriuretic polypeptide and
characterization of the cDNA encoding its precursor.";
Nature 312:152-155(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2985557;
Argentin S., Nemer M., Drouin J., Scott G.K., Kennedy B.P.,
Davies P.L.;
"The gene for rat atrial natriuretic factor.";
J. Biol. Chem. 260:4568-4571(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6238331; DOI=10.1073/pnas.81.20.6325;
Zivin R.A., Condra J.H., Dixon R.A.F., Seidah N.G., Chretien M.,
Nemer M., Chamberland M., Drouin J.;
"Molecular cloning and characterization of DNA sequences encoding rat
and human atrial natriuretic factors.";
Proc. Natl. Acad. Sci. U.S.A. 81:6325-6329(1984).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2962707;
Flynn T.G.;
"The elucidation of the structure of atrial natriuretic factor, a new
peptide hormone.";
Can. J. Physiol. Pharmacol. 65:2013-2020(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 38-152.
PubMed=2951736; DOI=10.1073/pnas.84.8.2175;
Gardner D.G., Vlasuk G.P., Baxter J.D., Fiddes J.C., Lewicki J.A.;
"Identification of atrial natriuretic factor gene transcripts in the
central nervous system of the rat.";
Proc. Natl. Acad. Sci. U.S.A. 84:2175-2179(1987).
[9]
PROTEIN SEQUENCE OF 126-150, AND SYNTHESIS OF 126-149.
PubMed=6233494; DOI=10.1038/309717a0;
Atlas S.A., Kleinert H.D., Camargo M.J., Januszewicz A., Sealey J.E.,
Laragh J.H., Schilling J.W., Lewicki J.A., Johnson L.K., Maack T.;
"Purification, sequencing and synthesis of natriuretic and vasoactive
rat atrial peptide.";
Nature 309:717-719(1984).
[10]
PROTEIN SEQUENCE OF 127-149, AND SYNTHESIS.
PubMed=6419347; DOI=10.1126/science.6419347;
Currie M.G., Geller D.M., Cole B.R., Siegel N.R., Fok K.F.,
Adams S.P., Eubanks S.R., Galluppi G.R., Needleman P.;
"Purification and sequence analysis of bioactive atrial peptides
(atriopeptins).";
Science 223:67-69(1984).
[11]
PROTEIN SEQUENCE OF 118-150.
PubMed=6232612; DOI=10.1073/pnas.81.9.2640;
Seidah N.G., Lazure C., Chretien M., Thibault G., Garcia R.,
Cantin M., Genest J., Nutt R.F., Brady S.F., Lyle T.A., Paleveda W.J.,
Colton C.D., Ciccarone T.M., Veber D.F.;
"Amino acid sequence of homologous rat atrial peptides: natriuretic
activity of native and synthetic forms.";
Proc. Natl. Acad. Sci. U.S.A. 81:2640-2644(1984).
[12]
PROTEIN SEQUENCE OF 25-38.
PubMed=2966345; DOI=10.1016/0196-9781(88)90008-3;
Thibault G., Murthy K.K., Gutkowska J., Seidah N.G., Lazure C.,
Chretien M., Cantin M.;
"NH2-terminal fragment of rat pro-atrial natriuretic factor in the
circulation: identification, radioimmunoassay and half-life.";
Peptides 9:47-53(1988).
[13]
PROTEOLYTIC PROCESSING BY MME, AND CLEAVAGE SITE.
PubMed=2966343; DOI=10.1016/0196-9781(88)90024-1;
Sonnenberg J.L., Sakane Y., Jeng A.Y., Koehn J.A., Ansell J.A.,
Wennogle L.P., Ghai R.D.;
"Identification of protease 3.4.24.11 as the major atrial natriuretic
factor degrading enzyme in the rat kidney.";
Peptides 9:173-180(1988).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[15]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 129-149 IN COMPLEX WITH
NPR1, AND DISULFIDE BOND.
PubMed=15117952; DOI=10.1074/jbc.M313222200;
Ogawa H., Qiu Y., Ogata C.M., Misono K.S.;
"Crystal structure of hormone-bound atrial natriuretic peptide
receptor extracellular domain: rotation mechanism for transmembrane
signal transduction.";
J. Biol. Chem. 279:28625-28631(2004).
-!- FUNCTION: Hormone playing a key role in cardiovascular homeostasis
through regulation of natriuresis, diuresis, and vasodilation.
Also plays a role in female pregnancy by promoting trophoblast
invasion and spiral artery remodeling in uterus. Specifically
binds and stimulates the cGMP production of the NPR1 receptor.
Binds the clearance receptor NPR3 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with NPR1. {ECO:0000269|PubMed:15117952}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Cleaved by CORIN upon secretion to produce the functional
hormone (By similarity). {ECO:0000250|UniProtKB:P01160,
ECO:0000250|UniProtKB:P05125}.
-!- PTM: Atrial natriuretic factor: Cleaved by MME. The cleavage
initiates degradation of the factor and thereby regulate its
activity. {ECO:0000269|PubMed:2966343}.
-!- SIMILARITY: Belongs to the natriuretic peptide family.
{ECO:0000305}.
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EMBL; M15868; AAA40736.1; -; mRNA.
EMBL; X00665; CAA25285.1; -; mRNA.
EMBL; K02062; AAA40735.1; -; Genomic_DNA.
EMBL; X01118; CAA25586.1; -; mRNA.
EMBL; M27498; AAA40737.1; -; mRNA.
PIR; A22570; AWRT.
RefSeq; NP_036744.1; NM_012612.2.
UniGene; Rn.2004; -.
PDB; 1T34; X-ray; 2.95 A; H=129-149.
PDBsum; 1T34; -.
SMR; P01161; -.
IntAct; P01161; 1.
STRING; 10116.ENSRNOP00000011005; -.
BindingDB; P01161; -.
ChEMBL; CHEMBL4287; -.
iPTMnet; P01161; -.
PhosphoSitePlus; P01161; -.
PaxDb; P01161; -.
PRIDE; P01161; -.
Ensembl; ENSRNOT00000011005; ENSRNOP00000011005; ENSRNOG00000008176.
GeneID; 24602; -.
KEGG; rno:24602; -.
UCSC; RGD:3193; rat.
CTD; 4878; -.
RGD; 3193; Nppa.
eggNOG; ENOG410IW5F; Eukaryota.
eggNOG; ENOG410ZUY6; LUCA.
GeneTree; ENSGT00510000048659; -.
HOGENOM; HOG000033937; -.
HOVERGEN; HBG004227; -.
InParanoid; P01161; -.
KO; K12334; -.
OMA; CNSFRYR; -.
OrthoDB; EOG091G0SV3; -.
PhylomeDB; P01161; -.
TreeFam; TF106304; -.
Reactome; R-RNO-5578768; Physiological factors.
EvolutionaryTrace; P01161; -.
PMAP-CutDB; P01161; -.
PRO; PR:P01161; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000008176; -.
ExpressionAtlas; P01161; baseline and differential.
Genevisible; P01161; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0042629; C:mast cell granule; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0005179; F:hormone activity; IDA:RGD.
GO; GO:0051427; F:hormone receptor binding; ISO:RGD.
GO; GO:0005184; F:neuropeptide hormone activity; ISO:RGD.
GO; GO:0071855; F:neuropeptide receptor binding; ISO:RGD.
GO; GO:0051428; F:peptide hormone receptor binding; IDA:RGD.
GO; GO:0005102; F:receptor binding; IDA:RGD.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; ISO:RGD.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0006182; P:cGMP biosynthetic process; IDA:RGD.
GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
GO; GO:0007507; P:heart development; TAS:UniProtKB.
GO; GO:0050891; P:multicellular organismal water homeostasis; TAS:RGD.
GO; GO:0030308; P:negative regulation of cell growth; IMP:RGD.
GO; GO:1903815; P:negative regulation of collecting lymphatic vessel constriction; IDA:RGD.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IDA:RGD.
GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD.
GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:RGD.
GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
GO; GO:0010460; P:positive regulation of heart rate; ISO:RGD.
GO; GO:1903595; P:positive regulation of histamine secretion by mast cell; IDA:UniProtKB.
GO; GO:1903766; P:positive regulation of potassium ion export across plasma membrane; IDA:BHF-UCL.
GO; GO:0006457; P:protein folding; ISO:RGD.
GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IDA:MGI.
GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:RGD.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; IEA:UniProtKB-KW.
GO; GO:0050878; P:regulation of body fluid levels; TAS:RGD.
GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:BHF-UCL.
GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
InterPro; IPR000663; Natr_peptide.
InterPro; IPR030480; Natr_peptide_CS.
InterPro; IPR002407; Natriuretic_peptide_atrial.
Pfam; PF00212; ANP; 1.
PRINTS; PR00711; ANATPEPTIDE.
PRINTS; PR00710; NATPEPTIDES.
SMART; SM00183; NAT_PEP; 1.
PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Hormone;
Reference proteome; Secreted; Signal; Vasoactive.
SIGNAL 1 24 {ECO:0000269|PubMed:2966345}.
PROPEP 25 122 {ECO:0000305}.
/FTId=PRO_0000001505.
PEPTIDE 123 150 Atrial natriuretic factor.
{ECO:0000250|UniProtKB:P01160}.
/FTId=PRO_0000391785.
PEPTIDE 126 150 Auriculin-B.
{ECO:0000269|PubMed:6233494}.
/FTId=PRO_0000001506.
PEPTIDE 126 149 Auriculin-A.
{ECO:0000269|PubMed:6233494}.
/FTId=PRO_0000001507.
PEPTIDE 127 150 Atriopeptin-3.
{ECO:0000269|PubMed:6419347}.
/FTId=PRO_0000001508.
PEPTIDE 127 149 Atriopeptin-2.
{ECO:0000269|PubMed:6419347}.
/FTId=PRO_0000001509.
PEPTIDE 127 147 Atriopeptin-1.
{ECO:0000269|PubMed:6419347}.
/FTId=PRO_0000001510.
SITE 122 123 Cleavage; by CORIN.
{ECO:0000250|UniProtKB:P01160}.
SITE 129 130 Cleavage; by MME.
{ECO:0000269|PubMed:2966343}.
DISULFID 129 145 {ECO:0000269|PubMed:15117952}.
TURN 136 139 {ECO:0000244|PDB:1T34}.
SEQUENCE 152 AA; 16556 MW; D8AAB2191E29519F CRC64;
MGSFSITKGF FLFLAFWLPG HIGANPVYSA VSNTDLMDFK NLLDHLEEKM PVEDEVMPPQ
ALSEQTDEAG AALSSLSEVP PWTGEVNPSQ RDGGALGRGP WDPSDRSALL KSKLRALLAG
PRSLRRSSCF GGRIDRIGAQ SGLGCNSFRY RR


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