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P16067

- ANPRB_RAT

UniProt

P16067 - ANPRB_RAT

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
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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. ossification Source: UniProtKB-KW
    6. receptor guanylyl cyclase signaling pathway Source: Ensembl

    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

    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.
    GeneTreeiENSGT00710000106571.
    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.
    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

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    MALPSLLLVV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA     50
    LAVEALGRAL PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG 100
    CVYPAASVAR FASHWHLPLL TAGAVASGFA AKNEHYRTLV RTGPSAPKLG 150
    EFVVTLHGHF NWTARAALLY LDARTDDRPH YFTIEGVFEA LQGSNLSVQH 200
    QVYTREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA QRENLTNGDY 250
    VFFYLDVFGE SLRAGPTRAT GRPWQDNRTQ EQAQALREAF QTVLVITYRE 300
    PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAQVLNE 350
    TIQEGGTRED GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL 400
    ESGDFQPAAH YSGAEKQIWW TGRPIPWVKG APPLDNPPCA FDLDDPSCDK 450
    TPLSTLAIVA LGTGITFIMF GVSSFLIFRK LMLEKELASM LWRIRWEELQ 500
    FGNSDRYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT GHFKGNVVAI 550
    KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP 600
    RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC 650
    VVDSRFVLKI TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT 700
    GMQKADVYSF AIILQEIALR SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP 750
    SIDRTQLNEE LVLLMERCWA QDPTERPDFG QIKGFIRRFN KEGGTSILDN 800
    LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH SVAEQLKRGE 850
    TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF 900
    DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP 950
    HDQLRLRIGV HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH 1000
    VSSTTKDALD ELGCFQLELR GDVEMKGKGK MRTYWLLGER KGPPGLL 1047
    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 ENSGT00710000106571.
    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.
    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 1, 2014
    This is version 139 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