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UniProtKB - P01160 (ANF_HUMAN)

Entry version 213 (07 Apr 2021)
Sequence version 2 (11 Dec 2019)
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Protein

Natriuretic peptides A

Gene

NPPA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (PubMed:8653797, PubMed:7595132, PubMed:2825692, PubMed:7720651, PubMed:8087923, PubMed:2532366, PubMed:22307324, PubMed:18835931, PubMed:21672517, PubMed:15741263, PubMed:16875975). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (PubMed:25401746, PubMed:9893117, PubMed:1672777, PubMed:1660465, PubMed:2162527, PubMed:2825692, PubMed:7720651, PubMed:22307324, PubMed:8384600, PubMed:21098034). 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 (PubMed:8653797, PubMed:7595132, PubMed:2825692, PubMed:7720651, PubMed:2532366, PubMed:8087923). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (PubMed:16875975). 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 (PubMed:22307324, PubMed:18835931, PubMed:21672517, PubMed:15741263). This includes upregulating 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 (PubMed:22307324, PubMed:18835931, PubMed:21672517, PubMed:15741263). Binds the clearance receptor NPR3 which removes the hormone from circulation (PubMed:1672777).By similarity18 Publications
May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis (PubMed:8653797, PubMed:7955907, PubMed:8087923, PubMed:2825692, PubMed:7595132, PubMed:2532366). In vitro, promotes the production of cGMP and induces vasodilation (PubMed:2825692). May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (PubMed:7720651). 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 (PubMed:2162527, PubMed:2825692). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (PubMed:11145122).By similarity9 Publications
May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation (PubMed:8653797, PubMed:7955907, PubMed:8087923, PubMed:2532366, PubMed:7595132). In vitro, promotes the production of cGMP and induces vasodilation (PubMed:2825692). May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (PubMed:7720651, PubMed:7595132). 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 (PubMed:7831500). Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides (PubMed:2162527, PubMed:2825692). 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 (PubMed:11145122).10 Publications
May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis (PubMed:8087923, PubMed:2825692, PubMed:7595132). In vitro, promotes the production of cGMP and induces vasodilation (PubMed:2825692). May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (PubMed:7720651, PubMed:7595132). May have a role in potassium excretion but not sodium excretion (natriuresis) (PubMed:8087923). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (PubMed:11145122).5 Publications
Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis (PubMed:8351194, PubMed:8853410, PubMed:8779891). Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance (PubMed:2528951, PubMed:8351194, PubMed:8853410, PubMed:8779891). Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1 (PubMed:8384600, PubMed:9893117). Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney (PubMed:8779891, PubMed:8384600).6 Publications
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.By similarity
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.By similarity
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.By similarity
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.By similarity
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.By similarity

Caution

Results concerning the involvement of this peptide in blood volume and blood pressure homeostasis are conflicting. Several studies utilising in vitro and heterologous expression systems show that it is able to activate cGMP and promote vasodilation and natriuresis (PubMed:2825692, PubMed:7720651). However, an in vivo study in rat found that it is not sufficient to induce any diuretic, natriuretic, nor hypotensive responses, and is unable to bind NPR1 nor increase guanylyl cyclase activity (By similarity).By similarity2 Publications
Results concerning the involvement of this peptide in blood volume and blood pressure homeostasis are conflicting. Several studies utilising in vitro and heterologous expression systems show that it is able to activate cGMP and promote vasodilation and natriuresis (PubMed:2825692, PubMed:7720651, PubMed:7595132). However, a heterologous expression study in rat found that it is not sufficient to induce any diuretic, natriuretic, nor hypotensive responses, and is unable to bind NPR1 nor increase guanylyl cyclase activity (PubMed:7831500).4 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHormone, Vasoactive, Vasodilator

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P01160

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2032785, YAP1- and WWTR1 (TAZ)-stimulated gene expression
R-HSA-5578768, Physiological factors
R-HSA-977225, Amyloid fiber formation

SIGNOR Signaling Network Open Resource

More...SIGNORi		P01160

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Natriuretic peptides ACurated
Alternative name(s):
Atrial natriuretic factor prohormone1 Publication
Short name:
proANF1 Publication
Atrial natriuretic peptide prohormone1 Publication
Short name:
preproANP1 Publication
Short name:
proANPCurated
Atriopeptigen1 Publication
Cardiodilatin1 Publication
Short name:
CDD1 Publication
preproCDD-ANF1 Publication
Cleaved into the following 12 chains:
Long-acting natriuretic peptide1 Publication
Short name:
LANP1 Publication
Alternative name(s):
Long-acting natriuretic hormoneCurated
Short name:
LANHCurated
Pro atrial natriuretic factor 1-301 Publication
Short name:
proANF 1-301 Publication
Pro atrial natriuretic peptide 1-30Curated
Short name:
proANP 1-30Curated
Vessel dilator1 Publication
Short name:
VSDL1 Publication
Alternative name(s):
Pro atrial natriuretic factor 31-671 Publication
Short name:
proANF 31-671 Publication
Pro atrial natriuretic peptide 31-67Curated
Short name:
proANP 31-67Curated
Kaliuretic peptide1 Publication
Short name:
KP1 Publication
Alternative name(s):
Pro atrial natriuretic factor 79-981 Publication
Short name:
proANF 79-981 Publication
Pro atrial natriuretic peptide 79-98Curated
Short name:
proANP 79-98Curated
Urodilatin1 Publication
Short name:
URO1 Publication
Alternative name(s):
CDD 95-1261 Publication
CDD-ANP (95-126)1 Publication
Pro atrial natriuretic peptide 95-1261 Publication
Short name:
proANP 95-1261 Publication
Auriculin-CCurated
Alternative name(s):
Atrial natriuretic factor 1-33By similarity
Short name:
ANF 1-33By similarity
Auriculin-DCurated
Alternative name(s):
Atrial natriuretic factor 3-33By similarity
Short name:
ANF 3-33By similarity
Atrial natriuretic peptide1 Publication
Short name:
ANP1 Publication
Alternative name(s):
Alpha-atrial natriuretic peptide1 Publication
Alpha-hANP1 Publication
Atrial natriuretic factor1 Publication
Short name:
ANF1 Publication
CDD-ANF1 Publication
CDD-ANP (99-126)1 Publication
CardionatrinBy similarity
Pro atrial natriuretic factor 99-1261 Publication
Short name:
proANF 99-1261 Publication
Auriculin-BCurated
Alternative name(s):
Atrial natriuretic factor 8-33By similarity
Short name:
ANF 8-33By similarity
Auriculin-ABy similarity
Atriopeptin-1By similarity
Alternative name(s):
Atriopeptin IBy similarity
Atriopeptin-2By similarity
Alternative name(s):
Atriopeptin IIBy similarity
Atriopeptin-3By similarity
Alternative name(s):
Atriopeptin IIIBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NPPA
Synonyms:ANP, PND
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:7939, NPPA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		108780, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P01160

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000175206.10

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell projection, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Atrial standstill 2 (ATRST2)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA rare arrhythmia characterized by the absence of electrical and mechanical activity in the atria. Electrocardiographically, it is characterized by bradycardia, the absence of P waves, and a junctional narrow complex escape rhythm.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071307150R → Q in ATRST2. 1 PublicationCorresponds to variant dbSNP:rs202102042EnsemblClinVar.1
Atrial fibrillation, familial, 6 (ATFB6)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA familial form of atrial fibrillation, a common sustained cardiac rhythm disturbance. Atrial fibrillation is characterized by disorganized atrial electrical activity and ineffective atrial contraction promoting blood stasis in the atria and reduces ventricular filling. It can result in palpitations, syncope, thromboembolic stroke, and congestive heart failure.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi123R → G: Loss of cleavage by CORIN. 1 Publication1
Mutagenesisi124 – 129Missing : No effect on degradation of atrial natriuretic peptide by IDE. 1 Publication6
Mutagenesisi124 – 126Missing : Reduced degradation of atrial natriuretic peptide by IDE; when associated with N-147--151-Y DEL. 1 Publication3
Mutagenesisi147 – 151Missing : Reduced degradation of atrial natriuretic peptide by IDE; when associated with S-124--126-R DEL. 1 Publication5

Keywords - Diseasei

Atrial fibrillation, Cardiomyopathy, Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		4878

MalaCards human disease database

More...MalaCardsi		NPPA
MIMi612201, phenotype
615745, phenotype

Open Targets

More...OpenTargetsi		ENSG00000175206

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		1344, Atrial standstill
334, Familial atrial fibrillation

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA256

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P01160, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1293193

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		NPPA

Domain mapping of disease mutations (DMDM)

More...DMDMi		113864

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25By similarityAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000044972126 – 151Natriuretic peptides A1 PublicationAdd BLAST126
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000044972226 – 55Long-acting natriuretic peptide3 PublicationsAdd BLAST30
PeptideiPRO_000044972356 – 92Vessel dilator3 PublicationsAdd BLAST37
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044972493 – 103CuratedAdd BLAST11
PeptideiPRO_0000449725104 – 123Kaliuretic peptide3 PublicationsAdd BLAST20
PeptideiPRO_0000449726119 – 151Auriculin-CBy similarityAdd BLAST33
PeptideiPRO_0000449727120 – 151Urodilatin1 PublicationAdd BLAST32
PeptideiPRO_0000449728121 – 145Auriculin-DBy similarityAdd BLAST25
PeptideiPRO_0000449729124 – 151Atrial natriuretic peptide4 PublicationsAdd BLAST28
PeptideiPRO_0000449730127 – 151Auriculin-BBy similarityAdd BLAST25
PeptideiPRO_0000449731127 – 150Auriculin-ABy similarityAdd BLAST24
PeptideiPRO_0000449732128 – 151Atriopeptin-3By similarityAdd BLAST24
PeptideiPRO_0000449733128 – 150Atriopeptin-2By similarityAdd BLAST23
PeptideiPRO_0000449734128 – 148Atriopeptin-1By similarityAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei129Phosphoserine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi130 ↔ 1462 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The precursor molecule is proteolytically cleaved by CORIN at Arg-123 to produce atrial natriuretic peptide (PubMed:10880574, PubMed:14559895, PubMed:7984506). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (PubMed:2532366, PubMed:7955907, PubMed:7984506). 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 (PubMed:2972874, PubMed:8351194, PubMed:9794555).By similarity8 Publications
Cleavage by MME initiates degradation of the factor and thereby regulates its activity (PubMed:2972276, PubMed:16254193). Degraded by IDE (in vitro) (PubMed:21098034). 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) (PubMed:21098034).3 Publications
Degraded by IDE.1 Publication
Phosphorylation on Ser-129 decreases vasorelaxant activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei123 – 124Cleavage; by CORIN1 Publication2
Sitei130 – 131Cleavage; by MME1 Publication2

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P01160

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P01160

PeptideAtlas

More...PeptideAtlasi		P01160

PRoteomics IDEntifications database

More...PRIDEi		P01160

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51340

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P01160

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P01160, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P01160

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P01160

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in the kidney distal tubular cells (at protein level) (PubMed:9794555, PubMed:8384600). Present in urine (at protein level) (PubMed:2972874, PubMed:9794555, PubMed:8351194, PubMed:8779891).5 Publications
Detected in atrial and ventricular plasma samples, and in adipocytes (at protein level) (PubMed:22291141, PubMed:21672517). Detected in urine in one study (PubMed:8351194). However, was not detected in urine in another study (PubMed:7984506). In the brain, predominantly expressed in the gray matter with very weak expression in the white matter (at protein level) (PubMed:30534047). Localizes to astrocyte-like structures throughout the white matter, and in the cerebral vessels detected in the leptomeningeal and parenchymal vessels, and endothelium and smooth muscle layers (at protein level) (PubMed:30534047). Relatively low levels of expression in the kidneys compared to urodilatin (at protein level) (PubMed:9794555, PubMed:8384600).7 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000175206, Expressed in cardiac muscle of right atrium and 203 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P01160, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P01160, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000175206, Tissue enriched (heart)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked antiparallel dimer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110938, 52 interactors

Protein interaction database and analysis system

More...IntActi		P01160, 39 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000365663

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P01160, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P01160

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P01160

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni147 – 151Important for degradation of atrial natriuretic peptide by IDE1 Publication5

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the natriuretic peptide family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502S9RQ, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154513

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P01160

Identification of Orthologs from Complete Genome Data

More...OMAi		LSEVPPW

Database of Orthologous Groups

More...OrthoDBi		1596502at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P01160

TreeFam database of animal gene trees

More...TreeFami		TF106304

Family and domain databases

Database of protein disorder

More...DisProti		DP00747

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000663, Natr_peptide
IPR030480, Natr_peptide_CS
IPR002407, Natriuretic_peptide_atrial

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00212, ANP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00711, ANATPEPTIDE
PR00710, NATPEPTIDES

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00183, NAT_PEP, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00263, NATRIURETIC_PEPTIDE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P01160-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSFSTTTVS FLLLLAFQLL GQTRANPMYN AVSNADLMDF KNLLDHLEEK 
        60         70         80         90        100
MPLEDEVVPP QVLSEPNEEA GAALSPLPEV PPWTGEVSPA QRDGGALGRG 
       110        120        130        140        150
PWDSSDRSAL LKSKLRALLT APRSLRRSSC FGGRMDRIGA QSGLGCNSFR 

Y
Length:151
Mass (Da):16,396
Last modified:December 11, 2019 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF3AA066A73EC97EF
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X094A0A087X094_HUMAN
Alpha-atrial natriuretic peptide
NPPA
152Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0ZBE8B0ZBE8_HUMAN
Alpha-atrial natriuretic peptide
NPPA
101Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti65E → D in AAA35529 (PubMed:3158606).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01457932V → M. Corresponds to variant dbSNP:rs5063Ensembl.1
Natural variantiVAR_071307150R → Q in ATRST2. 1 PublicationCorresponds to variant dbSNP:rs202102042EnsemblClinVar.1
Natural variantiVAR_082651151Y → YRR2 Publications1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
K02043 Genomic DNA Translation: AAB59379.1
M30262 mRNA Translation: AAA35669.1
X01470, X02558 Genomic DNA Translation: CAA25699.1
X01471 Genomic DNA Translation: CAA25700.2
M54951, M54947 Genomic DNA Translation: AAA35529.1
AL021155 Genomic DNA No translation available.
EU326308 Genomic DNA Translation: ACA05916.1
BC005893 mRNA Translation: AAH05893.1
K02399 Genomic DNA Translation: AAA35528.1
K02044 mRNA Translation: AAA51730.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS139.1

Protein sequence database of the Protein Information Resource

More...PIRi		A22693, AWHU

NCBI Reference Sequences

More...RefSeqi		NP_006163.1, NM_006172.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000376480; ENSP00000365663; ENSG00000175206

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4878

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4878

UCSC genome browser

More...UCSCi		uc001ati.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Atrial natriuretic peptide entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02043 Genomic DNA Translation: AAB59379.1
M30262 mRNA Translation: AAA35669.1
X01470, X02558 Genomic DNA Translation: CAA25699.1
X01471 Genomic DNA Translation: CAA25700.2
M54951, M54947 Genomic DNA Translation: AAA35529.1
AL021155 Genomic DNA No translation available.
EU326308 Genomic DNA Translation: ACA05916.1
BC005893 mRNA Translation: AAH05893.1
K02399 Genomic DNA Translation: AAA35528.1
K02044 mRNA Translation: AAA51730.1
CCDSiCCDS139.1
PIRiA22693, AWHU
RefSeqiNP_006163.1, NM_006172.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ANPNMR-A124-151[»]
1YK0X-ray2.40E129-149[»]
3N57X-ray3.03C/D124-151[»]
SMRiP01160
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110938, 52 interactors
IntActiP01160, 39 interactors
STRINGi9606.ENSP00000365663

Chemistry databases

ChEMBLiCHEMBL1293193

PTM databases

CarbonylDBiP01160
GlyGeniP01160, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP01160
PhosphoSitePlusiP01160

Genetic variation databases

BioMutaiNPPA
DMDMi113864

Proteomic databases

MassIVEiP01160
PaxDbiP01160
PeptideAtlasiP01160
PRIDEiP01160
ProteomicsDBi51340

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		13911, 740 antibodies

The DNASU plasmid repository

More...DNASUi		4878

Genome annotation databases

EnsembliENST00000376480; ENSP00000365663; ENSG00000175206
GeneIDi4878
KEGGihsa:4878
UCSCiuc001ati.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4878
DisGeNETi4878

GeneCards: human genes, protein and diseases

More...GeneCardsi		NPPA
HGNCiHGNC:7939, NPPA
HPAiENSG00000175206, Tissue enriched (heart)
MalaCardsiNPPA
MIMi108780, gene
612201, phenotype
615745, phenotype
neXtProtiNX_P01160
OpenTargetsiENSG00000175206
Orphaneti1344, Atrial standstill
334, Familial atrial fibrillation
PharmGKBiPA256
VEuPathDBiHostDB:ENSG00000175206.10

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502S9RQ, Eukaryota
GeneTreeiENSGT00940000154513
InParanoidiP01160
OMAiLSEVPPW
OrthoDBi1596502at2759
PhylomeDBiP01160
TreeFamiTF106304

Enzyme and pathway databases

PathwayCommonsiP01160
ReactomeiR-HSA-2032785, YAP1- and WWTR1 (TAZ)-stimulated gene expression
R-HSA-5578768, Physiological factors
R-HSA-977225, Amyloid fiber formation
SIGNORiP01160

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		4878, 9 hits in 981 CRISPR screens
EvolutionaryTraceiP01160

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Atrial_natriuretic_peptide

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4878
PharosiP01160, Tchem

Protein Ontology

More...PROi		PR:P01160
RNActiP01160, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000175206, Expressed in cardiac muscle of right atrium and 203 other tissues
ExpressionAtlasiP01160, baseline and differential
GenevisibleiP01160, HS

Family and domain databases

DisProtiDP00747
InterProiView protein in InterPro
IPR000663, Natr_peptide
IPR030480, Natr_peptide_CS
IPR002407, Natriuretic_peptide_atrial
PfamiView protein in Pfam
PF00212, ANP, 1 hit
PRINTSiPR00711, ANATPEPTIDE
PR00710, NATPEPTIDES
SMARTiView protein in SMART
SM00183, NAT_PEP, 1 hit
PROSITEiView protein in PROSITE
PS00263, NATRIURETIC_PEPTIDE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiANF_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P01160
Secondary accession number(s): Q13766, Q5JZE1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 11, 2019
Last modified: April 7, 2021
This is version 213 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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