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P17342

- ANPRC_HUMAN

UniProt

P17342 - ANPRC_HUMAN

Protein

Atrial natriuretic peptide receptor 3

Gene

NPR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (10 Jan 2003)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei106 – 1061Chloride
    Binding sitei135 – 1351Chloride; via amide nitrogen
    Binding sitei136 – 1361Chloride; via amide nitrogen

    GO - Molecular functioni

    1. G-protein coupled peptide receptor activity Source: BHF-UCL
    2. hormone binding Source: UniProtKB
    3. natriuretic peptide receptor activity Source: UniProtKB
    4. peptide hormone binding Source: BHF-UCL

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: Ensembl
    2. negative regulation of adenylate cyclase activity Source: Ensembl
    3. negative regulation of smooth muscle cell proliferation Source: Ensembl
    4. osteoclast proliferation Source: UniProtKB
    5. pancreatic juice secretion Source: Ensembl
    6. phosphatidylinositol-mediated signaling Source: Ensembl
    7. phospholipase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
    8. positive regulation of nitric-oxide synthase activity Source: BHF-UCL
    9. positive regulation of urine volume Source: UniProtKB
    10. regulation of blood pressure Source: UniProtKB
    11. regulation of osteoblast proliferation Source: UniProtKB
    12. skeletal system development Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Chloride

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:NPR3
    Synonyms:ANPRC, C5orf23, NPRC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:7945. NPR3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31737.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 541515Atrial natriuretic peptide receptor 3PRO_0000012370Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi86 – 861N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi108 ↔ 136
    Disulfide bondi213 ↔ 261
    Glycosylationi293 – 2931N-linked (GlcNAc...) (high mannose)3 Publications
    Glycosylationi394 – 3941N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi473 – 473Interchain

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP17342.
    PaxDbiP17342.
    PRIDEiP17342.

    PTM databases

    PhosphoSiteiP17342.

    Expressioni

    Gene expression databases

    ArrayExpressiP17342.
    BgeeiP17342.
    CleanExiHS_NPR3.
    GenevestigatoriP17342.

    Organism-specific databases

    HPAiHPA031065.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Dimers can also be formed through the C-terminal cysteine of isoform 2.3 Publications

    Protein-protein interaction databases

    BioGridi110943. 4 interactions.
    STRINGi9606.ENSP00000398028.

    Structurei

    Secondary structure

    1
    541
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi52 – 598
    Helixi69 – 8315
    Beta strandi98 – 1058
    Helixi111 – 12212
    Turni123 – 1253
    Beta strandi129 – 1324
    Helixi137 – 15014
    Beta strandi154 – 1574
    Helixi162 – 1654
    Turni167 – 1737
    Beta strandi174 – 1763
    Helixi181 – 19515
    Beta strandi199 – 2057
    Beta strandi208 – 2103
    Helixi212 – 22716
    Beta strandi230 – 2367
    Beta strandi238 – 2403
    Helixi244 – 25411
    Beta strandi256 – 2627
    Helixi264 – 27613
    Turni280 – 2834
    Beta strandi285 – 2895
    Helixi291 – 2933
    Turni297 – 2993
    Helixi309 – 3157
    Helixi316 – 3183
    Beta strandi319 – 3246
    Helixi330 – 34415
    Turni345 – 3473
    Helixi356 – 37722
    Helixi385 – 3928
    Beta strandi393 – 3997
    Beta strandi402 – 4065
    Beta strandi410 – 4123
    Beta strandi415 – 4239
    Turni424 – 4274
    Beta strandi428 – 4369
    Turni437 – 4404
    Beta strandi441 – 4444
    Beta strandi451 – 4533
    Helixi454 – 4563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JDNX-ray2.90A44-485[»]
    1JDPX-ray2.00A/B44-485[»]
    1YK0X-ray2.40A/B1-480[»]
    1YK1X-ray2.90A/B2-480[»]
    ProteinModelPortaliP17342.
    SMRiP17342. Positions 46-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17342.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 481455ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini505 – 54137CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei482 – 50423HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ANF receptor family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG255055.
    HOGENOMiHOG000236252.
    HOVERGENiHBG060145.
    InParanoidiP17342.
    KOiK12325.
    OMAiFQVAYED.
    OrthoDBiEOG7BZVS0.
    PhylomeDBiP17342.
    TreeFamiTF106339.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR001170. Ntpep_rcpt.
    IPR028082. Peripla_BP_I.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    [Graphical view]
    PRINTSiPR00255. NATPEPTIDER.
    SUPFAMiSSF53822. SSF53822. 1 hit.
    PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17342-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPSLLVLTFS PCVLLGWALL AGGTGGGGVG GGGGGAGIGG GRQEREALPP    50
    QKIEVLVLLP QDDSYLFSLT RVRPAIEYAL RSVEGNGTGR RLLPPGTRFQ 100
    VAYEDSDCGN RALFSLVDRV AAARGAKPDL ILGPVCEYAA APVARLASHW 150
    DLPMLSAGAL AAGFQHKDSE YSHLTRVAPA YAKMGEMMLA LFRHHHWSRA 200
    ALVYSDDKLE RNCYFTLEGV HEVFQEEGLH TSIYSFDETK DLDLEDIVRN 250
    IQASERVVIM CASSDTIRSI MLVAHRHGMT SGDYAFFNIE LFNSSSYGDG 300
    SWKRGDKHDF EAKQAYSSLQ TVTLLRTVKP EFEKFSMEVK SSVEKQGLNM 350
    EDYVNMFVEG FHDAILLYVL ALHEVLRAGY SKKDGGKIIQ QTWNRTFEGI 400
    AGQVSIDANG DRYGDFSVIA MTDVEAGTQE VIGDYFGKEG RFEMRPNVKY 450
    PWGPLKLRID ENRIVEHTNS SPCKSSGGLE ESAVTGIVVG ALLGAGLLMA 500
    FYFFRKKYRI TIERRTQQEE SNLGKHRELR EDSIRSHFSV A 541
    Length:541
    Mass (Da):59,808
    Last modified:January 10, 2003 - v2
    Checksum:i8A66415F7F7D62B7
    GO
    Isoform 2 (identifier: P17342-2) [UniParc]FASTAAdd to Basket

    Also known as: NPR-C6

    The sequence of this isoform differs from the canonical sequence as follows:
         476-477: SG → C

    Show »
    Length:540
    Mass (Da):59,767
    Checksum:i53EE0020A296D6F5
    GO
    Isoform 3 (identifier: P17342-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:324
    Mass (Da):36,656
    Checksum:iC38DFF9C771B1A8B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti522 – 5221N → D in BAG61896. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040MPSLL…AGIGG → MEPSALGPWSLFPDLAPRDQ EGQVLAPRRCFRRECGQNEK in isoform 3. 1 PublicationVSP_045901Add
    BLAST
    Alternative sequencei41 – 256216Missing in isoform 3. 1 PublicationVSP_045902Add
    BLAST
    Alternative sequencei476 – 4772SG → C in isoform 2 and isoform 3. 3 PublicationsVSP_001812

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS47196.1. [P17342-2]
    CCDS56356.1. [P17342-3]
    CCDS56357.1. [P17342-1]
    PIRiS10150. OYHUCR.
    RefSeqiNP_000899.1. NM_000908.3. [P17342-2]
    NP_001191304.1. NM_001204375.1. [P17342-1]
    NP_001191305.1. NM_001204376.1. [P17342-3]
    UniGeneiHs.13528.
    Hs.619466.

    Genome annotation databases

    EnsembliENST00000265074; ENSP00000265074; ENSG00000113389. [P17342-1]
    ENST00000415167; ENSP00000398028; ENSG00000113389. [P17342-2]
    GeneIDi4883.
    KEGGihsa:4883.
    UCSCiuc003jhv.3. human. [P17342-1]

    Polymorphism databases

    DMDMi27735161.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS47196.1. [P17342-2 ]
    CCDS56356.1. [P17342-3 ]
    CCDS56357.1. [P17342-1 ]
    PIRi S10150. OYHUCR.
    RefSeqi NP_000899.1. NM_000908.3. [P17342-2 ]
    NP_001191304.1. NM_001204375.1. [P17342-1 ]
    NP_001191305.1. NM_001204376.1. [P17342-3 ]
    UniGenei Hs.13528.
    Hs.619466.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JDN X-ray 2.90 A 44-485 [» ]
    1JDP X-ray 2.00 A/B 44-485 [» ]
    1YK0 X-ray 2.40 A/B 1-480 [» ]
    1YK1 X-ray 2.90 A/B 2-480 [» ]
    ProteinModelPortali P17342.
    SMRi P17342. Positions 46-446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110943. 4 interactions.
    STRINGi 9606.ENSP00000398028.

    Chemistry

    BindingDBi P17342.
    ChEMBLi CHEMBL2247.
    DrugBanki DB04899. Nesiritide.
    GuidetoPHARMACOLOGYi 1749.

    PTM databases

    PhosphoSitei P17342.

    Polymorphism databases

    DMDMi 27735161.

    Proteomic databases

    MaxQBi P17342.
    PaxDbi P17342.
    PRIDEi P17342.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265074 ; ENSP00000265074 ; ENSG00000113389 . [P17342-1 ]
    ENST00000415167 ; ENSP00000398028 ; ENSG00000113389 . [P17342-2 ]
    GeneIDi 4883.
    KEGGi hsa:4883.
    UCSCi uc003jhv.3. human. [P17342-1 ]

    Organism-specific databases

    CTDi 4883.
    GeneCardsi GC05P032747.
    HGNCi HGNC:7945. NPR3.
    HPAi HPA031065.
    MIMi 108962. gene.
    neXtProti NX_P17342.
    PharmGKBi PA31737.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255055.
    HOGENOMi HOG000236252.
    HOVERGENi HBG060145.
    InParanoidi P17342.
    KOi K12325.
    OMAi FQVAYED.
    OrthoDBi EOG7BZVS0.
    PhylomeDBi P17342.
    TreeFami TF106339.

    Miscellaneous databases

    EvolutionaryTracei P17342.
    GeneWikii NPR3.
    GenomeRNAii 4883.
    NextBioi 18796.
    PROi P17342.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17342.
    Bgeei P17342.
    CleanExi HS_NPR3.
    Genevestigatori P17342.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR001170. Ntpep_rcpt.
    IPR028082. Peripla_BP_I.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    [Graphical view ]
    PRINTSi PR00255. NATPEPTIDER.
    SUPFAMi SSF53822. SSF53822. 1 hit.
    PROSITEi PS00458. ANF_RECEPTORS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiANPRC_HUMAN
    AccessioniPrimary (citable) accession number: P17342
    Secondary accession number(s): A2RRD1, B4DT84, E7EPG9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 10, 2003
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3