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Protein

Atrial natriuretic peptide receptor 1

Gene

Npr1

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

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)DescriptionActionsGraphical viewLength
Binding sitei81Chloride2 Publications1
Binding sitei113Chloride; via amide nitrogen2 Publications1
Binding sitei114Chloride; via amide nitrogen2 Publications1

GO - Molecular functioni

  • ATP binding Source: InterPro
  • GTP binding Source: RGD
  • guanylate cyclase activity Source: RGD
  • natriuretic peptide receptor activity Source: RGD
  • peptide hormone binding Source: RGD
  • protein kinase activity Source: InterPro
  • protein kinase binding Source: RGD

GO - Biological processi

  • cell surface receptor signaling pathway Source: RGD
  • cGMP biosynthetic process Source: RGD
  • dopamine metabolic process Source: RGD
  • intracellular signal transduction Source: RGD
  • negative regulation of smooth muscle cell proliferation Source: RGD
  • positive regulation of cGMP biosynthetic process Source: RGD
  • receptor guanylyl cyclase signaling pathway Source: GO_Central
  • regulation of blood vessel size Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Receptor, Vasoactive

Keywords - Biological processi

cGMP biosynthesis

Keywords - Ligandi

Chloride, GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.2. 5301.
ReactomeiR-RNO-5578768. Physiological factors.

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
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi3195. Npr1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini29 – 469ExtracellularSequence analysisAdd BLAST441
Transmembranei470 – 490HelicalSequence analysisAdd BLAST21
Topological domaini491 – 1057CytoplasmicSequence analysisAdd BLAST567

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi197E → K: Abolishes hormone binding. 1 Publication1
Mutagenesisi213H → D: Abolishes hormone binding. 1 Publication1
Mutagenesisi522S → A: No effect on phosphorylation, 15% loss of ANP-dependent activity. 1 Publication1
Mutagenesisi525S → A: Reduced phosphorylation, 80% loss of ANP-dependent activity. 1 Publication1
Mutagenesisi525S → E: No effect on ANP-dependent activity. 1 Publication1
Mutagenesisi528T → A: Reduced phosphorylation, 50% loss of ANP-dependent activity. 1 Publication1
Mutagenesisi530S → A: Reduced phosphorylation, 50% loss of ANP-dependent activity. 1 Publication1
Mutagenesisi534S → A: Reduced phosphorylation, 50% loss of ANP-dependent activity. 1 Publication1
Mutagenesisi538S → A: Reduced phosphorylation, 60% loss of CNP-dependent activity. 1 Publication1
Mutagenesisi541T → A: Markedly reduced phosphorylation, 50% loss of CNP-dependent activity. 1 Publication1
Mutagenesisi542T → A: No effect on phosphorylation, 30% loss of ANP-dependent activity. 1 Publication1

Chemistry databases

GuidetoPHARMACOLOGYi1747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Add BLAST28
ChainiPRO_000001236229 – 1057Atrial natriuretic peptide receptor 1Add BLAST1029

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...)1
Disulfide bondi88 ↔ 1141 Publication
Disulfide bondi192 ↔ 2411 Publication
Glycosylationi208N-linked (GlcNAc...)2 Publications1
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Glycosylationi375N-linked (GlcNAc...)Sequence analysis1
Glycosylationi382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi423N-linked (GlcNAc...)1
Disulfide bondi451 ↔ 4601 Publication
Modified residuei515Phosphoserine1 Publication1
Modified residuei525Phosphoserine2 Publications1
Modified residuei528Phosphothreonine2 Publications1
Modified residuei530Phosphoserine2 Publications1
Modified residuei534Phosphoserine2 Publications1
Modified residuei538Phosphoserine2 Publications1
Modified residuei541Phosphothreonine2 Publications1

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

iPTMnetiP18910.
PhosphoSitePlusiP18910.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014684.
GenevisibleiP18910. RN.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

IntActiP18910. 2 interactors.
STRINGi10116.ENSRNOP00000020307.

Structurei

Secondary structure

11057
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 37Combined sources8
Helixi48 – 63Combined sources16
Beta strandi73 – 80Combined sources8
Beta strandi86 – 88Combined sources3
Helixi92 – 104Combined sources13
Beta strandi107 – 110Combined sources4
Helixi115 – 128Combined sources14
Beta strandi132 – 135Combined sources4
Helixi140 – 143Combined sources4
Turni145 – 147Combined sources3
Beta strandi151 – 153Combined sources3
Helixi158 – 172Combined sources15
Beta strandi176 – 183Combined sources8
Beta strandi186 – 188Combined sources3
Helixi191 – 207Combined sources17
Beta strandi210 – 216Combined sources7
Helixi221 – 223Combined sources3
Helixi224 – 234Combined sources11
Beta strandi236 – 242Combined sources7
Helixi244 – 256Combined sources13
Turni261 – 263Combined sources3
Beta strandi265 – 269Combined sources5
Beta strandi291 – 293Combined sources3
Helixi295 – 301Combined sources7
Helixi302 – 304Combined sources3
Beta strandi305 – 310Combined sources6
Helixi316 – 333Combined sources18
Helixi341 – 343Combined sources3
Helixi344 – 365Combined sources22
Helixi373 – 378Combined sources6
Turni379 – 382Combined sources4
Beta strandi383 – 387Combined sources5
Beta strandi390 – 394Combined sources5
Beta strandi398 – 400Combined sources3
Beta strandi404 – 409Combined sources6
Turni411 – 413Combined sources3
Beta strandi416 – 422Combined sources7
Turni424 – 426Combined sources3
Beta strandi429 – 432Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DP4X-ray2.00A/C29-463[»]
1T34X-ray2.95A/B29-463[»]
3A3KX-ray2.50A/B29-463[»]
ProteinModelPortaliP18910.
SMRiP18910.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18910.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini524 – 801Protein kinasePROSITE-ProRule annotationAdd BLAST278
Domaini872 – 1002Guanylate cyclasePROSITE-ProRule annotationAdd BLAST131

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

eggNOGiKOG1023. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG051862.
InParanoidiP18910.
KOiK12323.
OMAiQYSELVV.
OrthoDBiEOG091G02QS.
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.
IPR001170. ANPR/GUC.
IPR011009. Kinase-like_dom.
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.

P18910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGSRRVRPR LRALLLLPPL LLLRGGHASD LTVAVVLPLT NTSYPWSWAR
60 70 80 90 100
VGPAVELALA RVKARPDLLP GWTVRMVLGS SENAAGVCSD TAAPLAAVDL
110 120 130 140 150
KWEHSPAVFL GPGCVYSAAP VGRFTAHWRV PLLTAGAPAL GIGVKDEYAL
160 170 180 190 200
TTRTGPSHVK LGDFVTALHR RLGWEHQALV LYADRLGDDR PCFFIVEGLY
210 220 230 240 250
MRVRERLNIT VNHQEFVEGD PDHYPKLLRA VRRKGRVIYI CSSPDAFRNL
260 270 280 290 300
MLLALNAGLT GEDYVFFHLD VFGQSLKSAQ GLVPQKPWER GDGQDRSARQ
310 320 330 340 350
AFQAAKIITY KEPDNPEYLE FLKQLKLLAD KKFNFTVEDG LKNIIPASFH
360 370 380 390 400
DGLLLYVQAV TETLAQGGTV TDGENITQRM WNRSFQGVTG YLKIDRNGDR
410 420 430 440 450
DTDFSLWDMD PETGAFRVVL NYNGTSQELM AVSEHKLYWP LGYPPPDVPK
460 470 480 490 500
CGFDNEDPAC NQDHFSTLEV LALVGSLSLI SFLIVSFFIY RKMQLEKELV
510 520 530 540 550
SELWRVRWED LQPSSLERHL RSAGSRLTLS GRGSNYGSLL TTEGQFQVFA
560 570 580 590 600
KTAYYKGNLV AVKRVNRKRI ELTRKVLFEL KHMRDVQNEH LTRFVGACTD
610 620 630 640 650
PPNICILTEY CPRGSLQDIL ENESITLDWM FRYSLTNDIV KGMLFLHNGA
660 670 680 690 700
ICSHGNLKSS NCVVDGRFVL KITDYGLESF RDPEPEQGHT LFAKKLWTAP
710 720 730 740 750
ELLRMASPPA RGSQAGDVYS FGIILQEIAL RSGVFYVEGL DLSPKEIIER
760 770 780 790 800
VTRGEQPPFR PSMDLQSHLE ELGQLMQRCW AEDPQERPPF QQIRLALRKF
810 820 830 840 850
NKENSSNILD NLLSRMEQYA NNLEELVEER TQAYLEEKRK AEALLYQILP
860 870 880 890 900
HSVAEQLKRG ETVQAEAFDS VTIYFSDIVG FTALSAESTP MQVVTLLNDL
910 920 930 940 950
YTCFDAVIDN FDVYKVETIG DAYMVVSGLP VRNGQLHARE VARMALALLD
960 970 980 990 1000
AVRSFRIRHR PQEQLRLRIG IHTGPVCAGV VGLKMPRYCL FGDTVNTASR
1010 1020 1030 1040 1050
MESNGEALKI HLSSETKAVL EEFDGFELEL RGDVEMKGKG KVRTYWLLGE

RGCSTRG
Length:1,057
Mass (Da):118,951
Last modified:November 1, 1990 - v1
Checksum:i9EA9AE685AC05816
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti366Q → H in AAA41202 (PubMed:1679239).Curated1
Sequence conflicti392L → P in AAA41202 (PubMed:1679239).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006232591.3.
UniGeneiRn.10463.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006232591.3.
UniGeneiRn.10463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DP4X-ray2.00A/C29-463[»]
1T34X-ray2.95A/B29-463[»]
3A3KX-ray2.50A/B29-463[»]
ProteinModelPortaliP18910.
SMRiP18910.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18910. 2 interactors.
STRINGi10116.ENSRNOP00000020307.

Chemistry databases

GuidetoPHARMACOLOGYi1747.

PTM databases

iPTMnetiP18910.
PhosphoSitePlusiP18910.

Proteomic databases

PaxDbiP18910.
PRIDEiP18910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4881.
RGDi3195. Npr1.

Phylogenomic databases

eggNOGiKOG1023. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000118959.
HOGENOMiHOG000293307.
HOVERGENiHBG051862.
InParanoidiP18910.
KOiK12323.
OMAiQYSELVV.
OrthoDBiEOG091G02QS.
PhylomeDBiP18910.
TreeFamiTF106338.

Enzyme and pathway databases

BRENDAi4.6.1.2. 5301.
ReactomeiR-RNO-5578768. Physiological factors.

Miscellaneous databases

EvolutionaryTraceiP18910.
PROiP18910.

Gene expression databases

BgeeiENSRNOG00000014684.
GenevisibleiP18910. RN.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR001828. ANF_lig-bd_rcpt.
IPR001170. ANPR/GUC.
IPR011009. Kinase-like_dom.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.