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P16067 (ANPRB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Atrial natriuretic peptide receptor 2

EC=4.6.1.2
Alternative name(s):
Atrial natriuretic peptide receptor type B
Short name=ANP-B
Short name=ANPR-B
Short name=NPR-B
Guanylate cyclase B
Short name=GC-B
Gene names
Name:Npr2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1047 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 C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth By similarity.

Catalytic activity

GTP = 3',5'-cyclic GMP + diphosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Phosphorylation of the protein kinase-like domain is required for full activation by CNP.

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 1 guanylate cyclase domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processcGMP biosynthesis
Osteogenesis
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionLyase
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from electronic annotation. Source: Ensembl

cGMP biosynthetic process

Inferred from direct assay PubMed 12003819PubMed 14691198PubMed 7552344. Source: RGD

cellular response to granulocyte macrophage colony-stimulating factor stimulus

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

receptor guanylyl cyclase signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 7552344. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 14691198. Source: RGD

GTP binding

Inferred from direct assay PubMed 7552344. Source: RGD

guanylate cyclase activity

Inferred from direct assay PubMed 14691198PubMed 7552344. Source: RGD

natriuretic peptide receptor activity

Inferred from direct assay PubMed 14691198PubMed 7552344. Source: RGD

peptide hormone binding

Inferred from direct assay PubMed 14691198PubMed 7552344. Source: RGD

protein kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 10471031Atrial natriuretic peptide receptor 2
PRO_0000012366

Regions

Topological domain17 – 458442Extracellular Potential
Transmembrane459 – 47820Helical; Potential
Topological domain479 – 1047569Cytoplasmic Potential
Domain513 – 786274Protein kinase
Domain861 – 991131Guanylate cyclase

Amino acid modifications

Modified residue5131Phosphoserine Ref.2 Ref.3
Modified residue5161Phosphothreonine Ref.2 Ref.3
Modified residue5181Phosphoserine Ref.2 Ref.3
Modified residue5231Phosphoserine Ref.2 Ref.3
Modified residue5261Phosphoserine Ref.2 Ref.3
Modified residue5291Phosphothreonine Ref.3
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Disulfide bond75 ↔ 101 By similarity
Disulfide bond439Interchain Probable
Disulfide bond448Interchain Probable

Experimental info

Mutagenesis5131S → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. Ref.2
Mutagenesis5161T → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. Ref.2
Mutagenesis5181S → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. Ref.2
Mutagenesis5211G → A: Reduced phosphorylation, 50% loss of CNP-dependent activity. Ref.2
Mutagenesis5221S → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. Ref.2
Mutagenesis5231S → A: Markedly reduced phosphorylation, 70% loss of CNP-dependent activity. Ref.2
Mutagenesis5261S → A: Markedly reduced phosphorylation, 80% loss of CNP-dependent activity. Ref.2
Mutagenesis5291T → A: No effect on phosphorylation, 30% loss of CNP-dependent activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16067 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5062C49228CC14A3

FASTA1,047117,127
        10         20         30         40         50         60 
MALPSLLLVV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL 

        70         80         90        100        110        120 
PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWHLPLL 

       130        140        150        160        170        180 
TAGAVASGFA AKNEHYRTLV RTGPSAPKLG EFVVTLHGHF NWTARAALLY LDARTDDRPH 

       190        200        210        220        230        240 
YFTIEGVFEA LQGSNLSVQH QVYTREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA 

       250        260        270        280        290        300 
QRENLTNGDY VFFYLDVFGE SLRAGPTRAT GRPWQDNRTQ EQAQALREAF QTVLVITYRE 

       310        320        330        340        350        360 
PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAQVLNE TIQEGGTRED 

       370        380        390        400        410        420 
GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL ESGDFQPAAH YSGAEKQIWW 

       430        440        450        460        470        480 
TGRPIPWVKG APPLDNPPCA FDLDDPSCDK TPLSTLAIVA LGTGITFIMF GVSSFLIFRK 

       490        500        510        520        530        540 
LMLEKELASM LWRIRWEELQ FGNSDRYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT 

       550        560        570        580        590        600 
GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP 

       610        620        630        640        650        660 
RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC VVDSRFVLKI 

       670        680        690        700        710        720 
TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF AIILQEIALR 

       730        740        750        760        770        780 
SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPTERPDFG 

       790        800        810        820        830        840 
QIKGFIRRFN KEGGTSILDN LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH 

       850        860        870        880        890        900 
SVAEQLKRGE TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF 

       910        920        930        940        950        960 
DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP HDQLRLRIGV 

       970        980        990       1000       1010       1020 
HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH VSSTTKDALD ELGCFQLELR 

      1030       1040 
GDVEMKGKGK MRTYWLLGER KGPPGLL 

« Hide

References

[1]"The primary structure of a plasma membrane guanylate cyclase demonstrates diversity within this new receptor family."
Schulz S., Singh S., Bellet R.A., Singh G., Tubb D.J., Chin H., Garbers D.L.
Cell 58:1155-1162(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification and characterization of the major phosphorylation sites of the B-type natriuretic peptide receptor."
Potter L.R., Hunter T.
J. Biol. Chem. 273:15533-15539(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523 AND SER-526, MUTAGENESIS OF SER-513; THR-516; SER-518; GLY-521; SER-522; SER-523; SER-526 AND THR-529.
[3]"Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B."
Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.
Biochemistry 49:10137-10145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523; SER-526 AND THR-529.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26896 mRNA. Translation: AAA41205.1.
PIROYRTBR. A33300.
RefSeqNP_446290.1. NM_053838.1.
UniGeneRn.32984.

3D structure databases

ProteinModelPortalP16067.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000021802.

PTM databases

PhosphoSiteP16067.

Proteomic databases

PaxDbP16067.
PRIDEP16067.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021802; ENSRNOP00000021802; ENSRNOG00000015991.
GeneID116564.
KEGGrno:116564.
UCSCRGD:620851. rat.

Organism-specific databases

CTD4882.
RGD620851. Npr2.

Phylogenomic databases

eggNOGCOG2114.
GeneTreeENSGT00710000106571.
HOGENOMHOG000293307.
HOVERGENHBG051862.
InParanoidP16067.
KOK12324.
OMAAAKSEHY.
OrthoDBEOG7Z69BJ.
PhylomeDBP16067.
TreeFamTF106338.

Gene expression databases

GenevestigatorP16067.

Family and domain databases

Gene3D3.30.70.1230. 1 hit.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR001170. Ntpep_rcpt.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00255. NATPEPTIDER.
SMARTSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619241.
PROP16067.

Entry information

Entry nameANPRB_RAT
AccessionPrimary (citable) accession number: P16067
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families