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P16067

- ANPRB_RAT

UniProt

P16067 - ANPRB_RAT

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Protein

Atrial natriuretic peptide receptor 2

Gene

Npr2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. GTP binding Source: RGD
  3. guanylate cyclase activity Source: RGD
  4. natriuretic peptide receptor activity Source: RGD
  5. peptide hormone binding Source: RGD
  6. protein kinase activity Source: InterPro

GO - Biological processi

  1. bone development Source: Ensembl
  2. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: Ensembl
  3. cGMP biosynthetic process Source: RGD
  4. intracellular signal transduction Source: InterPro
  5. negative regulation of meiotic cell cycle Source: Ensembl
  6. negative regulation of oocyte maturation Source: Ensembl
  7. ossification Source: UniProtKB-KW
  8. receptor guanylyl cyclase signaling pathway Source: Ensembl
  9. single organism reproductive process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor

Keywords - Biological processi

cGMP biosynthesis, Osteogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Npr2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi620851. Npr2.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi513 – 5131S → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. 1 Publication
Mutagenesisi516 – 5161T → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. 1 Publication
Mutagenesisi518 – 5181S → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. 1 Publication
Mutagenesisi521 – 5211G → A: Reduced phosphorylation, 50% loss of CNP-dependent activity. 1 Publication
Mutagenesisi522 – 5221S → A: Reduced phosphorylation, 30% loss of CNP-dependent activity. 1 Publication
Mutagenesisi523 – 5231S → A: Markedly reduced phosphorylation, 70% loss of CNP-dependent activity. 1 Publication
Mutagenesisi526 – 5261S → A: Markedly reduced phosphorylation, 80% loss of CNP-dependent activity. 1 Publication
Mutagenesisi529 – 5291T → A: No effect on phosphorylation, 30% loss of CNP-dependent activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence AnalysisAdd
BLAST
Chaini17 – 10471031Atrial natriuretic peptide receptor 2PRO_0000012366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi75 ↔ 101By similarity
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi439 – 439InterchainCurated
Disulfide bondi448 – 448InterchainCurated
Modified residuei513 – 5131Phosphoserine2 Publications
Modified residuei516 – 5161Phosphothreonine2 Publications
Modified residuei518 – 5181Phosphoserine2 Publications
Modified residuei523 – 5231Phosphoserine2 Publications
Modified residuei526 – 5261Phosphoserine2 Publications
Modified residuei529 – 5291Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation of the protein kinase-like domain is required for full activation by CNP.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP16067.
PRIDEiP16067.

PTM databases

PhosphoSiteiP16067.

Expressioni

Gene expression databases

GenevestigatoriP16067.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021802.

Structurei

3D structure databases

ProteinModelPortaliP16067.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 458442ExtracellularSequence AnalysisAdd
BLAST
Topological domaini479 – 1047569CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei459 – 47820HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini513 – 786274Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini861 – 991131Guanylate cyclasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG051862.
InParanoidiP16067.
KOiK12324.
OMAiAAKSEHY.
OrthoDBiEOG7Z69BJ.
PhylomeDBiP16067.
TreeFamiTF106338.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR001170. Ntpep_rcpt.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00255. NATPEPTIDER.
SMARTiSM00044. CYCc. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16067-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALPSLLLVV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA
60 70 80 90 100
LAVEALGRAL PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG
110 120 130 140 150
CVYPAASVAR FASHWHLPLL TAGAVASGFA AKNEHYRTLV RTGPSAPKLG
160 170 180 190 200
EFVVTLHGHF NWTARAALLY LDARTDDRPH YFTIEGVFEA LQGSNLSVQH
210 220 230 240 250
QVYTREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA QRENLTNGDY
260 270 280 290 300
VFFYLDVFGE SLRAGPTRAT GRPWQDNRTQ EQAQALREAF QTVLVITYRE
310 320 330 340 350
PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAQVLNE
360 370 380 390 400
TIQEGGTRED GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL
410 420 430 440 450
ESGDFQPAAH YSGAEKQIWW TGRPIPWVKG APPLDNPPCA FDLDDPSCDK
460 470 480 490 500
TPLSTLAIVA LGTGITFIMF GVSSFLIFRK LMLEKELASM LWRIRWEELQ
510 520 530 540 550
FGNSDRYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT GHFKGNVVAI
560 570 580 590 600
KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP
610 620 630 640 650
RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC
660 670 680 690 700
VVDSRFVLKI TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT
710 720 730 740 750
GMQKADVYSF AIILQEIALR SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP
760 770 780 790 800
SIDRTQLNEE LVLLMERCWA QDPTERPDFG QIKGFIRRFN KEGGTSILDN
810 820 830 840 850
LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH SVAEQLKRGE
860 870 880 890 900
TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF
910 920 930 940 950
DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP
960 970 980 990 1000
HDQLRLRIGV HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH
1010 1020 1030 1040
VSSTTKDALD ELGCFQLELR GDVEMKGKGK MRTYWLLGER KGPPGLL
Length:1,047
Mass (Da):117,127
Last modified:April 1, 1990 - v1
Checksum:i5062C49228CC14A3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26896 mRNA. Translation: AAA41205.1.
PIRiA33300. OYRTBR.
RefSeqiNP_446290.1. NM_053838.1.
UniGeneiRn.32984.

Genome annotation databases

EnsembliENSRNOT00000021802; ENSRNOP00000021802; ENSRNOG00000015991.
GeneIDi116564.
KEGGirno:116564.
UCSCiRGD:620851. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26896 mRNA. Translation: AAA41205.1 .
PIRi A33300. OYRTBR.
RefSeqi NP_446290.1. NM_053838.1.
UniGenei Rn.32984.

3D structure databases

ProteinModelPortali P16067.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021802.

PTM databases

PhosphoSitei P16067.

Proteomic databases

PaxDbi P16067.
PRIDEi P16067.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021802 ; ENSRNOP00000021802 ; ENSRNOG00000015991 .
GeneIDi 116564.
KEGGi rno:116564.
UCSCi RGD:620851. rat.

Organism-specific databases

CTDi 4882.
RGDi 620851. Npr2.

Phylogenomic databases

eggNOGi COG2114.
GeneTreei ENSGT00760000118959.
HOGENOMi HOG000293307.
HOVERGENi HBG051862.
InParanoidi P16067.
KOi K12324.
OMAi AAKSEHY.
OrthoDBi EOG7Z69BJ.
PhylomeDBi P16067.
TreeFami TF106338.

Miscellaneous databases

NextBioi 619241.
PROi P16067.

Gene expression databases

Genevestigatori P16067.

Family and domain databases

Gene3Di 3.30.70.1230. 1 hit.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR011009. Kinase-like_dom.
IPR001170. Ntpep_rcpt.
IPR029787. Nucleotide_cyclase.
IPR028082. Peripla_BP_I.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00255. NATPEPTIDER.
SMARTi SM00044. CYCc. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
SSF55073. SSF55073. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00458. ANF_RECEPTORS. 1 hit.
PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiANPRB_RAT
AccessioniPrimary (citable) accession number: P16067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3