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P18910

- ANPRA_RAT

UniProt

P18910 - ANPRA_RAT

Protein

Atrial natriuretic peptide receptor 1

Gene

Npr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei81 – 811Chloride2 Publications
    Binding sitei113 – 1131Chloride; via amide nitrogen2 Publications
    Binding sitei114 – 1141Chloride; via amide nitrogen2 Publications

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    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 binding Source: RGD
    7. protein kinase activity Source: InterPro
    8. protein kinase binding Source: RGD

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: RGD
    2. cGMP biosynthetic process Source: RGD
    3. dopamine metabolic process Source: RGD
    4. intracellular signal transduction Source: RGD
    5. negative regulation of smooth muscle cell proliferation Source: RGD
    6. positive regulation of cGMP biosynthetic process Source: RGD
    7. receptor guanylyl cyclase signaling pathway Source: Ensembl
    8. regulation of blood vessel size Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase, Receptor, Vasoactive

    Keywords - Biological processi

    cGMP biosynthesis

    Keywords - Ligandi

    Chloride, GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Atrial natriuretic peptide receptor 1 (EC:4.6.1.2)
    Alternative name(s):
    Atrial natriuretic peptide receptor type A
    Short name:
    ANP-A
    Short name:
    ANPR-A
    Short name:
    NPR-A
    Guanylate cyclase A
    Short name:
    GC-A
    Gene namesi
    Name:Npr1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi3195. Npr1.

    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
    Mutagenesisi197 – 1971E → K: Abolishes hormone binding. 1 Publication
    Mutagenesisi213 – 2131H → D: Abolishes hormone binding. 1 Publication
    Mutagenesisi522 – 5221S → A: No effect on phosphorylation, 15% loss of ANP-dependent activity. 1 Publication
    Mutagenesisi525 – 5251S → A: Reduced phosphorylation, 80% loss of ANP-dependent activity. 1 Publication
    Mutagenesisi525 – 5251S → E: No effect on ANP-dependent activity. 1 Publication
    Mutagenesisi528 – 5281T → A: Reduced phosphorylation, 50% loss of ANP-dependent activity. 1 Publication
    Mutagenesisi530 – 5301S → A: Reduced phosphorylation, 50% loss of ANP-dependent activity. 1 Publication
    Mutagenesisi534 – 5341S → A: Reduced phosphorylation, 50% loss of ANP-dependent activity. 1 Publication
    Mutagenesisi538 – 5381S → A: Reduced phosphorylation, 60% loss of CNP-dependent activity. 1 Publication
    Mutagenesisi541 – 5411T → A: Markedly reduced phosphorylation, 50% loss of CNP-dependent activity. 1 Publication
    Mutagenesisi542 – 5421T → A: No effect on phosphorylation, 30% loss of ANP-dependent activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Add
    BLAST
    Chaini29 – 10571029Atrial natriuretic peptide receptor 1PRO_0000012362Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi41 – 411N-linked (GlcNAc...)
    Disulfide bondi88 ↔ 1141 Publication
    Disulfide bondi192 ↔ 2411 Publication
    Glycosylationi208 – 2081N-linked (GlcNAc...)2 Publications
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi423 – 4231N-linked (GlcNAc...)
    Disulfide bondi451 ↔ 4601 Publication
    Modified residuei515 – 5151Phosphoserine1 Publication
    Modified residuei525 – 5251Phosphoserine2 Publications
    Modified residuei528 – 5281Phosphothreonine2 Publications
    Modified residuei530 – 5301Phosphoserine2 Publications
    Modified residuei534 – 5341Phosphoserine2 Publications
    Modified residuei538 – 5381Phosphoserine2 Publications
    Modified residuei541 – 5411Phosphothreonine2 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP18910.
    PRIDEiP18910.

    PTM databases

    PhosphoSiteiP18910.

    Expressioni

    Gene expression databases

    GenevestigatoriP18910.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    IntActiP18910. 1 interaction.

    Structurei

    Secondary structure

    1
    1057
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 378
    Helixi48 – 6316
    Beta strandi73 – 808
    Beta strandi86 – 883
    Helixi92 – 10413
    Beta strandi107 – 1104
    Helixi115 – 12814
    Beta strandi132 – 1354
    Helixi140 – 1434
    Turni145 – 1473
    Beta strandi151 – 1533
    Helixi158 – 17215
    Beta strandi176 – 1838
    Beta strandi186 – 1883
    Helixi191 – 20717
    Beta strandi210 – 2167
    Helixi221 – 2233
    Helixi224 – 23411
    Beta strandi236 – 2427
    Helixi244 – 25613
    Turni261 – 2633
    Beta strandi265 – 2695
    Beta strandi291 – 2933
    Helixi295 – 3017
    Helixi302 – 3043
    Beta strandi305 – 3106
    Helixi316 – 33318
    Helixi341 – 3433
    Helixi344 – 36522
    Helixi373 – 3786
    Turni379 – 3824
    Beta strandi383 – 3875
    Beta strandi390 – 3945
    Beta strandi398 – 4003
    Beta strandi404 – 4096
    Turni411 – 4133
    Beta strandi416 – 4227
    Turni424 – 4263
    Beta strandi429 – 4324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DP4X-ray2.00A/C29-463[»]
    1T34X-ray2.95A/B29-463[»]
    1T53model-A509-799[»]
    3A3KX-ray2.50A/B29-463[»]
    ProteinModelPortaliP18910.
    SMRiP18910. Positions 29-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18910.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini29 – 469441ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini491 – 1057567CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei470 – 49021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini524 – 801278Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini872 – 1002131Guanylate 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

    eggNOGiCOG0515.
    GeneTreeiENSGT00710000106571.
    HOGENOMiHOG000293307.
    HOVERGENiHBG051862.
    InParanoidiP18910.
    KOiK12323.
    OMAiCFFLVEG.
    OrthoDBiEOG7Z69BJ.
    PhylomeDBiP18910.
    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.

    P18910-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGSRRVRPR LRALLLLPPL LLLRGGHASD LTVAVVLPLT NTSYPWSWAR     50
    VGPAVELALA RVKARPDLLP GWTVRMVLGS SENAAGVCSD TAAPLAAVDL 100
    KWEHSPAVFL GPGCVYSAAP VGRFTAHWRV PLLTAGAPAL GIGVKDEYAL 150
    TTRTGPSHVK LGDFVTALHR RLGWEHQALV LYADRLGDDR PCFFIVEGLY 200
    MRVRERLNIT VNHQEFVEGD PDHYPKLLRA VRRKGRVIYI CSSPDAFRNL 250
    MLLALNAGLT GEDYVFFHLD VFGQSLKSAQ GLVPQKPWER GDGQDRSARQ 300
    AFQAAKIITY KEPDNPEYLE FLKQLKLLAD KKFNFTVEDG LKNIIPASFH 350
    DGLLLYVQAV TETLAQGGTV TDGENITQRM WNRSFQGVTG YLKIDRNGDR 400
    DTDFSLWDMD PETGAFRVVL NYNGTSQELM AVSEHKLYWP LGYPPPDVPK 450
    CGFDNEDPAC NQDHFSTLEV LALVGSLSLI SFLIVSFFIY RKMQLEKELV 500
    SELWRVRWED LQPSSLERHL RSAGSRLTLS GRGSNYGSLL TTEGQFQVFA 550
    KTAYYKGNLV AVKRVNRKRI ELTRKVLFEL KHMRDVQNEH LTRFVGACTD 600
    PPNICILTEY CPRGSLQDIL ENESITLDWM FRYSLTNDIV KGMLFLHNGA 650
    ICSHGNLKSS NCVVDGRFVL KITDYGLESF RDPEPEQGHT LFAKKLWTAP 700
    ELLRMASPPA RGSQAGDVYS FGIILQEIAL RSGVFYVEGL DLSPKEIIER 750
    VTRGEQPPFR PSMDLQSHLE ELGQLMQRCW AEDPQERPPF QQIRLALRKF 800
    NKENSSNILD NLLSRMEQYA NNLEELVEER TQAYLEEKRK AEALLYQILP 850
    HSVAEQLKRG ETVQAEAFDS VTIYFSDIVG FTALSAESTP MQVVTLLNDL 900
    YTCFDAVIDN FDVYKVETIG DAYMVVSGLP VRNGQLHARE VARMALALLD 950
    AVRSFRIRHR PQEQLRLRIG IHTGPVCAGV VGLKMPRYCL FGDTVNTASR 1000
    MESNGEALKI HLSSETKAVL EEFDGFELEL RGDVEMKGKG KVRTYWLLGE 1050
    RGCSTRG 1057
    Length:1,057
    Mass (Da):118,951
    Last modified:November 1, 1990 - v1
    Checksum:i9EA9AE685AC05816
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti366 – 3661Q → H in AAA41202. (PubMed:1679239)Curated
    Sequence conflicti392 – 3921L → P in AAA41202. (PubMed:1679239)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14773 mRNA. Translation: CAA32881.1.
    J05677 Genomic DNA. Translation: AAA41200.1.
    M74535 mRNA. Translation: AAA41202.1.
    BC128742 mRNA. Translation: AAI28743.1.
    PIRiS03348. OYRTR.
    RefSeqiNP_036745.1. NM_012613.1.
    XP_006232653.1. XM_006232591.1.
    UniGeneiRn.10463.

    Genome annotation databases

    EnsembliENSRNOT00000020307; ENSRNOP00000020307; ENSRNOG00000014684.
    GeneIDi24603.
    KEGGirno:24603.
    UCSCiRGD:3195. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14773 mRNA. Translation: CAA32881.1 .
    J05677 Genomic DNA. Translation: AAA41200.1 .
    M74535 mRNA. Translation: AAA41202.1 .
    BC128742 mRNA. Translation: AAI28743.1 .
    PIRi S03348. OYRTR.
    RefSeqi NP_036745.1. NM_012613.1.
    XP_006232653.1. XM_006232591.1.
    UniGenei Rn.10463.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DP4 X-ray 2.00 A/C 29-463 [» ]
    1T34 X-ray 2.95 A/B 29-463 [» ]
    1T53 model - A 509-799 [» ]
    3A3K X-ray 2.50 A/B 29-463 [» ]
    ProteinModelPortali P18910.
    SMRi P18910. Positions 29-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P18910. 1 interaction.

    PTM databases

    PhosphoSitei P18910.

    Proteomic databases

    PaxDbi P18910.
    PRIDEi P18910.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000020307 ; ENSRNOP00000020307 ; ENSRNOG00000014684 .
    GeneIDi 24603.
    KEGGi rno:24603.
    UCSCi RGD:3195. rat.

    Organism-specific databases

    CTDi 4881.
    RGDi 3195. Npr1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00710000106571.
    HOGENOMi HOG000293307.
    HOVERGENi HBG051862.
    InParanoidi P18910.
    KOi K12323.
    OMAi CFFLVEG.
    OrthoDBi EOG7Z69BJ.
    PhylomeDBi P18910.
    TreeFami TF106338.

    Miscellaneous databases

    EvolutionaryTracei P18910.
    NextBioi 603816.
    PROi P18910.

    Gene expression databases

    Genevestigatori P18910.

    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. "A membrane form of guanylate cyclase is an atrial natriuretic peptide receptor."
      Chinkers M., Garbers D.L., Chang M.S., Lowe D.G., Chin H., Goeddel D.V., Schulz S.
      Nature 338:78-83(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The primary structure of the rat guanylyl cyclase A/atrial natriuretic peptide receptor gene."
      Yamaguchi M., Rutledge L.J., Garbers D.L.
      J. Biol. Chem. 265:20414-20420(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Site-directed mutational analysis of a membrane guanylate cyclase cDNA reveals the atrial natriuretic factor signaling site."
      Duda T., Goraczniak R.M., Sharma R.K.
      Proc. Natl. Acad. Sci. U.S.A. 88:7882-7886(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Placenta.
    5. "Phosphorylation of the kinase homology domain is essential for activation of the A-type natriuretic peptide receptor."
      Potter L.R., Hunter T.
      Mol. Cell. Biol. 18:2164-2172(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-525; THR-528; SER-530; SER-534; SER-538 AND THR-541, MUTAGENESIS OF SER-522; SER-525; THR-528; SER-530; SER-534; SER-538; THR-541 AND THR-542.
    6. "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-515; SER-525; THR-528; SER-530; SER-534; SER-538 AND THR-541.
    7. "Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor."
      van den Akker F., Zhang X., Miyagi M., Huo X., Misono K.S., Yee V.C.
      Nature 406:101-104(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-463 IN COMPLEX WITH CHLORIDE, MUTAGENESIS OF GLU-197 AND HIS-213, SUBUNIT, GLYCOSYLATION AT ASN-208.
    8. "Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction."
      Ogawa H., Qiu Y., Ogata C.M., Misono K.S.
      J. Biol. Chem. 279:28625-28631(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 29-463 IN COMPLEX WITH NPPA AND CHLORIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-208.

    Entry informationi

    Entry nameiANPRA_RAT
    AccessioniPrimary (citable) accession number: P18910
    Secondary accession number(s): A1A5N8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 141 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3