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Entry version 99 (02 Jun 2021)
Sequence version 1 (01 Mar 2001)
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Protein

Natriuretic peptides A

Gene

NPPA

Organism
Felis catus (Cat) (Felis silvestris catus)
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>
-Protein inferred from homologyi <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 (By similarity).

Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (By similarity).

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 (By similarity).

Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (By similarity).

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 (By similarity).

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 (By similarity).

Binds the clearance receptor NPR3 which removes the hormone from circulation (By similarity).

By similarity

May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase (By similarity).

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. Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption (By similarity).

By similarity

May have a role in cardio-renal homeostasis through regulation of natriuresis, diuresis, and vasodilation. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. 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. Appears to bind to specific receptors that are distinct from the receptors bound by the atrial natriuretic and long-acting natriuretic peptides. 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.

By similarity

May have a role in cardio-renal homeostasis through regulation of diuresis and inhibiting aldosterone synthesis. In vitro, promotes the production of cGMP and induces vasodilation. May promote natriuresis, at least in part, by enhancing prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-ATPase. May have a role in potassium excretion but not sodium excretion (natriuresis). Possibly enhances protein excretion in urine by decreasing proximal tubular protein reabsorption.

By similarity

Hormone produced in the kidneys that appears to be important for maintaining cardio-renal homeostasis. Mediates vasodilation, natriuresis and diuresis primarily in the renal system, in order to maintain the extracellular fluid volume and control the fluid-electrolyte balance. Specifically binds and stimulates cGMP production by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may be the natriuretic peptide responsible for the regulation of sodium and water homeostasis in the kidney.

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 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 (By similarity). 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 similarity
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 (By similarity). However, a heterologous and in vivo 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 (By similarity).By similarity

<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

GO - Biological processi

<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

<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 prohormoneBy similarity
Short name:
preproANFBy similarity
Short name:
proANFBy similarity
Atrial natriuretic peptide prohormoneBy similarity
Short name:
preproANPBy similarity
Short name:
proANPBy similarity
AtriopeptigenBy similarity
CardiodilatinBy similarity
Short name:
CDDBy similarity
preproCDD-ANFBy similarity
Cleaved into the following 12 chains:
Long-acting natriuretic peptideBy similarity
Short name:
LANPBy similarity
Alternative name(s):
Long-acting natriuretic hormoneCurated
Short name:
LANHCurated
Pro atrial natriuretic factor 1-30By similarity
Short name:
proANF 1-30By similarity
Pro atrial natriuretic peptide 1-30Curated
Short name:
proANP 1-30Curated
Vessel dilatorBy similarity
Short name:
VSDLBy similarity
Alternative name(s):
Pro atrial natriuretic factor 31-67By similarity
Short name:
proANF 31-67By similarity
Pro atrial natriuretic peptide 31-67Curated
Short name:
proANP 31-67Curated
Kaliuretic peptideBy similarity
Short name:
KPBy similarity
Alternative name(s):
Pro atrial natriuretic factor 79-98By similarity
Short name:
proANF 79-98By similarity
Pro atrial natriuretic peptide 79-98Curated
Short name:
proANP 79-98Curated
UrodilatinBy similarity
Short name:
UROBy similarity
Alternative name(s):
CDD 95-126By similarity
CDD-ANP (95-126)By similarity
Pro atrial natriuretic peptide 95-126By similarity
Short name:
proANP 95-126By similarity
Alternative name(s):
Atrial natriuretic factor 1-33By similarity
Short name:
ANF 1-33By similarity
Alternative name(s):
Atrial natriuretic factor 3-33By similarity
Short name:
ANF 3-33By similarity
Atrial natriuretic peptideBy similarity
Short name:
ANPBy similarity
Alternative name(s):
Alpha-atrial natriuretic peptideBy similarity
Alpha-hANPBy similarity
Atrial natriuretic factorBy similarity
Short name:
ANFBy similarity
CDD-ANFBy similarity
CDD-ANP (99-126)By similarity
CardionatrinBy similarity
Pro atrial natriuretic factor 99-126By similarity
Short name:
proANF 99-126By similarity
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
<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>OrganismiFelis catus (Cat) (Felis silvestris catus)
<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 identifieri9685 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
<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
  • UP000011712 <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 C1

<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 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_000044969526 – 151Natriuretic peptides ABy similarityAdd BLAST126
<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_000000148826 – 123CuratedAdd BLAST98
<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_000044969626 – 55Long-acting natriuretic peptideBy similarityAdd BLAST30
PeptideiPRO_000044969756 – 92Vessel dilatorBy similarityAdd BLAST37
PropeptideiPRO_000044969893 – 103By similarityAdd BLAST11
PeptideiPRO_0000449699104 – 123Kaliuretic peptideBy similarityAdd BLAST20
PeptideiPRO_0000449700119 – 151Auriculin-CBy similarityAdd BLAST33
PeptideiPRO_0000449701120 – 151UrodilatinBy similarityAdd BLAST32
PeptideiPRO_0000449702121 – 145Auriculin-DBy similarityAdd BLAST25
PeptideiPRO_0000001489124 – 151Atrial natriuretic peptideBy similarityAdd BLAST28
PeptideiPRO_0000449703127 – 151Auriculin-BBy similarityAdd BLAST25
PeptideiPRO_0000449704127 – 150Auriculin-ABy similarityAdd BLAST24
PeptideiPRO_0000449705128 – 151Atriopeptin-3By similarityAdd BLAST24
PeptideiPRO_0000449706128 – 150Atriopeptin-2By similarityAdd BLAST23
PeptideiPRO_0000449707128 – 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 residuei129PhosphoserineBy similarity1
<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 ↔ 146By similarity

<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 the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). 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 (By similarity).By similarity
Cleavage by MME initiates degradation of the factor and thereby regulates its activity. Degradation by IDE results in reduced activation of NPR1 (in vitro). 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).By similarity
Degraded by IDE.By similarity
Phosphorylation on Ser-129 decreases vasorelaxant activity.By similarity

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 CORINBy similarity2
Sitei130 – 131Cleavage; by MMEBy similarity2

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9GLD0

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSFCAG00000000070, Expressed in embryonic head and 2 other tissues

<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.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9685.ENSFCAP00000000063

<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

3D structure databases

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

More...
SMRi
Q9GLD0

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Regioni62 – 104DisorderedSequence analysisAdd BLAST43
Regioni147 – 151Important for degradation of atrial natriuretic peptide by IDEBy similarity5

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_144536_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9GLD0

Identification of Orthologs from Complete Genome Data

More...
OMAi
LSEVPPW

Database of Orthologous Groups

More...
OrthoDBi
1596502at2759

TreeFam database of animal gene trees

More...
TreeFami
TF106304

Family and domain databases

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

Q9GLD0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSFSTITAS FLLFLACQLL WQTGANPVYG SVSNADLMDF KNLLDHLEDK
60 70 80 90 100
MPLEDEVVPP QVLSEQNEEA GAALSPLPEV PPWAGEVNPA QRDGGALGRG
110 120 130 140 150
SWDSSDRSAL LKSKLRALLA APRSLRRSSC FGGRMDRIGA QSGLGCNSFR

YRR
Length:153
Mass (Da):16,583
Last modified:March 1, 2001 - v1
<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:i32DEBD205B285686
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
A0A5F5XPK4A0A5F5XPK4_FELCA
Alpha-atrial natriuretic peptide
NPPA
204Annotation 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>
A0A0A0MPX2A0A0A0MPX2_FELCA
Brain natriuretic factor prohormone
NPPA
146Annotation score:

Annotation score:2 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF298813 Genomic DNA Translation: AAG23837.1

NCBI Reference Sequences

More...
RefSeqi
XP_003989547.1, XM_003989498.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSFCAT00000062724; ENSFCAP00000048114; ENSFCAG00000000072

Database of genes from NCBI RefSeq genomes

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GeneIDi
101100575

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
fca:101100575

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF298813 Genomic DNA Translation: AAG23837.1
RefSeqiXP_003989547.1, XM_003989498.3

3D structure databases

SMRiQ9GLD0
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000000063

Proteomic databases

PRIDEiQ9GLD0

Genome annotation databases

EnsembliENSFCAT00000062724; ENSFCAP00000048114; ENSFCAG00000000072
GeneIDi101100575
KEGGifca:101100575

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4878

Phylogenomic databases

eggNOGiENOG502S9RQ, Eukaryota
GeneTreeiENSGT00940000154513
HOGENOMiCLU_144536_0_0_1
InParanoidiQ9GLD0
OMAiLSEVPPW
OrthoDBi1596502at2759
TreeFamiTF106304

Gene expression databases

BgeeiENSFCAG00000000070, Expressed in embryonic head and 2 other tissues

Family and domain databases

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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_FELCA
<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: Q9GLD0
<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: May 10, 2004
Last sequence update: March 1, 2001
Last modified: June 2, 2021
This is version 99 of the entry and version 1 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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