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P17342 (ANPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Atrial natriuretic peptide receptor 3
Alternative name(s):
Atrial natriuretic peptide clearance receptor
Atrial natriuretic peptide receptor type C
Short name=ANP-C
Short name=ANPR-C
Short name=NPR-C
Gene names
Name:NPR3
Synonyms:ANPRC, C5orf23, NPRC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity.

Subunit structure

Homodimer; disulfide-linked. Dimers can also be formed through the C-terminal cysteine of isoform 2. Ref.8 Ref.10 Ref.11

Subcellular location

Membrane; Single-pass type I membrane protein.

Miscellaneous

Has low affinity for peptide hormones in the absence of bound chloride.

Sequence similarities

Belongs to the ANF receptor family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   LigandChloride
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of adenylate cyclase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

osteoclast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

pancreatic juice secretion

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-mediated signaling

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of urine volume

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of osteoblast proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal system development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentintegral component of plasma membrane

Inferred by curator Ref.9. Source: BHF-UCL

   Molecular_functionG-protein coupled peptide receptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

hormone binding

Inferred from physical interaction Ref.9. Source: UniProtKB

natriuretic peptide receptor activity

Inferred from direct assay Ref.9. Source: UniProtKB

peptide hormone binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P17342-1)

Also known as: NPR-C5;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P17342-2)

Also known as: NPR-C6;

The sequence of this isoform differs from the canonical sequence as follows:
     476-477: SG → C
Isoform 3 (identifier: P17342-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MPSLLVLTFS...GGGGGAGIGG → MEPSALGPWS...FRRECGQNEK
     41-256: Missing.
     476-477: SG → C
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 541515Atrial natriuretic peptide receptor 3
PRO_0000012370

Regions

Topological domain27 – 481455Extracellular Potential
Transmembrane482 – 50423Helical; Potential
Topological domain505 – 54137Cytoplasmic Potential

Sites

Binding site1061Chloride
Binding site1351Chloride; via amide nitrogen
Binding site1361Chloride; via amide nitrogen

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) (complex) Ref.8 Ref.11
Glycosylation2931N-linked (GlcNAc...) (high mannose) Ref.8 Ref.10 Ref.11
Glycosylation3941N-linked (GlcNAc...) (complex) Ref.8 Ref.10 Ref.11
Disulfide bond108 ↔ 136 Ref.8 Ref.10 Ref.11
Disulfide bond213 ↔ 261 Ref.8 Ref.10 Ref.11
Disulfide bond473Interchain Ref.8 Ref.10 Ref.11

Natural variations

Alternative sequence1 – 4040MPSLL…AGIGG → MEPSALGPWSLFPDLAPRDQ EGQVLAPRRCFRRECGQNEK in isoform 3.
VSP_045901
Alternative sequence41 – 256216Missing in isoform 3.
VSP_045902
Alternative sequence476 – 4772SG → C in isoform 2 and isoform 3.
VSP_001812

Experimental info

Sequence conflict5221N → D in BAG61896. Ref.4

Secondary structure

........................................................................ 541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NPR-C5) [UniParc].

Last modified January 10, 2003. Version 2.
Checksum: 8A66415F7F7D62B7

FASTA54159,808
        10         20         30         40         50         60 
MPSLLVLTFS PCVLLGWALL AGGTGGGGVG GGGGGAGIGG GRQEREALPP QKIEVLVLLP 

        70         80         90        100        110        120 
QDDSYLFSLT RVRPAIEYAL RSVEGNGTGR RLLPPGTRFQ VAYEDSDCGN RALFSLVDRV 

       130        140        150        160        170        180 
AAARGAKPDL ILGPVCEYAA APVARLASHW DLPMLSAGAL AAGFQHKDSE YSHLTRVAPA 

       190        200        210        220        230        240 
YAKMGEMMLA LFRHHHWSRA ALVYSDDKLE RNCYFTLEGV HEVFQEEGLH TSIYSFDETK 

       250        260        270        280        290        300 
DLDLEDIVRN IQASERVVIM CASSDTIRSI MLVAHRHGMT SGDYAFFNIE LFNSSSYGDG 

       310        320        330        340        350        360 
SWKRGDKHDF EAKQAYSSLQ TVTLLRTVKP EFEKFSMEVK SSVEKQGLNM EDYVNMFVEG 

       370        380        390        400        410        420 
FHDAILLYVL ALHEVLRAGY SKKDGGKIIQ QTWNRTFEGI AGQVSIDANG DRYGDFSVIA 

       430        440        450        460        470        480 
MTDVEAGTQE VIGDYFGKEG RFEMRPNVKY PWGPLKLRID ENRIVEHTNS SPCKSSGGLE 

       490        500        510        520        530        540 
ESAVTGIVVG ALLGAGLLMA FYFFRKKYRI TIERRTQQEE SNLGKHRELR EDSIRSHFSV 


A 

« Hide

Isoform 2 (NPR-C6) [UniParc].

Checksum: 53EE0020A296D6F5
Show »

FASTA54059,767
Isoform 3 [UniParc].

Checksum: C38DFF9C771B1A8B
Show »

FASTA32436,656

References

« Hide 'large scale' references
[1]"cDNA sequence of the human atrial natriuretic peptide clearance receptor."
Lowe D.G., Camerato T.R., Goeddel D.V.
Nucleic Acids Res. 18:3412-3412(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Kidney.
[2]"Isolation and functional expression of the human atrial natriuretic peptide clearance receptor cDNA."
Porter J.G., Arfsten A., Fuller F., Miller J.A., Gregory L.C., Lewicki J.A.
Biochem. Biophys. Res. Commun. 171:796-803(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Human lens epithelial mRNA for atrial natriuretic peptide clearance receptor."
Rae J.L., Shepard A.R.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Lens epithelium.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Pericardium.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer."
Stults J.T., O'Connell K.L., Garcia C., Wong S., Engel A.M., Garbers D.L., Lowe D.G.
Biochemistry 33:11372-11381(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE (ISOFORMS 1 AND 2), DISULFIDE BONDS, GLYCOSYLATION AT ASN-86; ASN-293 AND ASN-394, STRUCTURE OF CARBOHYDRATES.
[9]"Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera."
Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G.
J. Biol. Chem. 266:23060-23067(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: LIGAND-BINDING.
[10]"Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone."
He X.-L., Chow D.-C., Martick M.M., Garcia K.C.
Science 293:1657-1662(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-485 IN COMPLEX WITH NATRIURETIC PEPTIDE, GLYCOSYLATION AT ASN-293 AND ASN-394, DISULFIDE BONDS, SUBUNIT.
[11]"Structural determinants of natriuretic peptide receptor specificity and degeneracy."
He X.-L., Dukkipati A., Garcia K.C.
J. Mol. Biol. 361:698-714(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-480 IN COMPLEX WITH NATRIURETIC PEPTIDE AND CHLORIDE IONS, GLYCOSYLATION AT ASN-86; ASN-293 AND ASN-394, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52282 mRNA. Translation: CAA36523.1.
M59305 mRNA. Translation: AAA51734.1.
AF025998 mRNA. Translation: AAB88801.1.
AK300094 mRNA. Translation: BAG61896.1.
AC008766 Genomic DNA. No translation available.
AC026703 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10799.1.
BC131540 mRNA. Translation: AAI31541.1.
PIROYHUCR. S10150.
RefSeqNP_000899.1. NM_000908.3.
NP_001191304.1. NM_001204375.1.
NP_001191305.1. NM_001204376.1.
UniGeneHs.13528.
Hs.619466.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JDNX-ray2.90A44-475[»]
1JDPX-ray2.00A/B44-475[»]
1YK0X-ray2.40A/B1-480[»]
1YK1X-ray2.90A/B2-480[»]
ProteinModelPortalP17342.
SMRP17342. Positions 46-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110943. 4 interactions.
STRING9606.ENSP00000398028.

Chemistry

BindingDBP17342.
ChEMBLCHEMBL2247.
DrugBankDB04899. Nesiritide.
GuidetoPHARMACOLOGY1749.

PTM databases

PhosphoSiteP17342.

Polymorphism databases

DMDM27735161.

Proteomic databases

PaxDbP17342.
PRIDEP17342.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265074; ENSP00000265074; ENSG00000113389. [P17342-1]
ENST00000415167; ENSP00000398028; ENSG00000113389. [P17342-2]
ENST00000415685; ENSP00000402490; ENSG00000113389. [P17342-3]
GeneID4883.
KEGGhsa:4883.
UCSCuc003jhv.3. human. [P17342-1]

Organism-specific databases

CTD4883.
GeneCardsGC05P032747.
HGNCHGNC:7945. NPR3.
HPAHPA031065.
MIM108962. gene.
neXtProtNX_P17342.
PharmGKBPA31737.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255055.
HOGENOMHOG000236252.
HOVERGENHBG060145.
InParanoidP17342.
KOK12325.
OMAFQVAYED.
OrthoDBEOG7BZVS0.
PhylomeDBP17342.
TreeFamTF106339.

Gene expression databases

ArrayExpressP17342.
BgeeP17342.
CleanExHS_NPR3.
GenevestigatorP17342.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR001170. Ntpep_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
[Graphical view]
PRINTSPR00255. NATPEPTIDER.
SUPFAMSSF53822. SSF53822. 1 hit.
PROSITEPS00458. ANF_RECEPTORS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17342.
GeneWikiNPR3.
GenomeRNAi4883.
NextBio18796.
PROP17342.
SOURCESearch...

Entry information

Entry nameANPRC_HUMAN
AccessionPrimary (citable) accession number: P17342
Secondary accession number(s): A2RRD1, B4DT84, E7EPG9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 10, 2003
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM