ANPRC_RAT
ID ANPRC_RAT Reviewed; 535 AA.
AC P41740; Q64156;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Atrial natriuretic peptide receptor 3;
DE AltName: Full=Atrial natriuretic peptide clearance receptor;
DE AltName: Full=Atrial natriuretic peptide receptor type C;
DE Short=ANP-C;
DE Short=ANPR-C;
DE Short=NPR-C;
DE Flags: Precursor;
GN Name=Npr3; Synonyms=Npr-c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7911802; DOI=10.1016/s0021-9258(17)32511-5;
RA Engel A.M., Schoenfeld J.R., Lowe D.G.;
RT "A single residue determines the distinct pharmacology of rat and human
RT natriuretic peptide receptor-C.";
RL J. Biol. Chem. 269:17005-17008(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-443.
RX PubMed=7554122; DOI=10.1161/01.res.77.4.750;
RA Lin X., Hanze J., Heese F., Sodmann R., Lang R.E.;
RT "Gene expression of natriuretic peptide receptors in myocardial cells.";
RL Circ. Res. 77:750-758(1995).
CC -!- FUNCTION: Receptor for the natriuretic peptide hormones, binding with
CC similar affinities atrial natriuretic peptide NPPA/ANP, brain
CC natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP.
CC May function as a clearance receptor for NPPA, NPPB and NPPC,
CC regulating their local concentrations and effects. May regulate
CC diuresis, blood pressure and skeletal development. Does not have
CC guanylate cyclase activity. {ECO:0000250|UniProtKB:P70180}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with OSTN.
CC {ECO:0000250|UniProtKB:P17342, ECO:0000250|UniProtKB:P70180}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17342};
CC Single-pass type I membrane protein.
CC -!- MISCELLANEOUS: Has low affinity for peptide hormones in the absence of
CC bound chloride. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ANF receptor family. {ECO:0000305}.
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DR EMBL; L27339; AAA41721.1; -; mRNA.
DR EMBL; S79624; AAB35354.1; -; mRNA.
DR PIR; A54155; A54155.
DR RefSeq; NP_037000.1; NM_012868.1.
DR AlphaFoldDB; P41740; -.
DR SMR; P41740; -.
DR STRING; 10116.ENSRNOP00000025966; -.
DR GlyGen; P41740; 3 sites.
DR iPTMnet; P41740; -.
DR PhosphoSitePlus; P41740; -.
DR PaxDb; P41740; -.
DR PRIDE; P41740; -.
DR GeneID; 25339; -.
DR KEGG; rno:25339; -.
DR CTD; 4883; -.
DR RGD; 3196; Npr3.
DR VEuPathDB; HostDB:ENSRNOG00000019184; -.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_013995_1_0_1; -.
DR InParanoid; P41740; -.
DR OMA; ENNIGKH; -.
DR OrthoDB; 1423201at2759; -.
DR PhylomeDB; P41740; -.
DR PRO; PR:P41740; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019184; Expressed in adult mammalian kidney and 16 other tissues.
DR Genevisible; P41740; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0031404; F:chloride ion binding; ISO:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:BHF-UCL.
DR GO; GO:0042562; F:hormone binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IDA:BHF-UCL.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0017046; F:peptide hormone binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:RGD.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0002158; P:osteoclast proliferation; ISS:UniProtKB.
DR GO; GO:0030157; P:pancreatic juice secretion; IMP:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IMP:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:RGD.
DR GO; GO:0033688; P:regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR PRINTS; PR00255; NATPEPTIDER.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00458; ANF_RECEPTORS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..40
FT /evidence="ECO:0000255"
FT /id="PRO_0000012373"
FT CHAIN 41..535
FT /note="Atrial natriuretic peptide receptor 3"
FT /id="PRO_0000012374"
FT TOPO_DOM 41..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..131
FT /evidence="ECO:0000250|UniProtKB:P10730"
FT DISULFID 208..256
FT /evidence="ECO:0000250|UniProtKB:P10730"
FT DISULFID 468
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P10730"
FT CONFLICT 120
FT /note="G -> R (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="D -> H (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="P -> R (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="D -> H (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="V -> A (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="AV -> VA (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="G -> R (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..300
FT /note="KRG -> SRE (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="Y -> H (in Ref. 2; AAB35354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59728 MW; 236272DCD2352C40 CRC64;
MRSLLLFTFS ACVLLARALL AGGASSGGGD TGPGNRRRER EALAAQKIEV LVLLPRDDSY
LFSLARVRPA IEYALRSVEG NGTGRKLLPP GTRFQVAYED SDCGNRALFS LVDRVAAARG
AKPDLILGPV CEYAAAPVAR LASHWDLPML SAGALAAGFQ HKDTEYSHLT RVAPAYAKMG
EMMLALFRHH HWSRAALLYS DDKLERNCYF TLEGVHEVFQ EEGLHTSAYN FDETKDLDLD
DIVRYIQGSE RVVIMCASGD TIRRIMLAVH RHGMTSGDYA FFNIELFNSS SYGDGSWKRG
DKHDFEAKQA YSSLQTVTLL RTAKPEFEKF SMEVKSSVEK QGLNEEDYVN MFVEGFHDAI
LLYVLALHEV LRAGYSKKDG GKIIQQTWNR TFEGIAGQVS IDANGDRYGD FSVVAMTDTE
AGTQEVIGDY FGKEGRFKMR SNVKYPWGSL KLRIDETRIV EHTNSSPCKS CGLEESAVTG
IVVGALLGAG LLMAFYFFRK KYRITIERRN HQEESNIGKH RELREDSIRS HFSVA
