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P18910

- ANPRA_RAT

UniProt

P18910 - ANPRA_RAT

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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

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 kinase activity Source: InterPro
  7. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 469441ExtracellularSequence AnalysisAdd
BLAST
Transmembranei470 – 49021HelicalSequence AnalysisAdd
BLAST
Topological domaini491 – 1057567CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: RGD
  3. receptor complex Source: Ensembl
Complete GO annotation...

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 – 378Combined sources
Helixi48 – 6316Combined sources
Beta strandi73 – 808Combined sources
Beta strandi86 – 883Combined sources
Helixi92 – 10413Combined sources
Beta strandi107 – 1104Combined sources
Helixi115 – 12814Combined sources
Beta strandi132 – 1354Combined sources
Helixi140 – 1434Combined sources
Turni145 – 1473Combined sources
Beta strandi151 – 1533Combined sources
Helixi158 – 17215Combined sources
Beta strandi176 – 1838Combined sources
Beta strandi186 – 1883Combined sources
Helixi191 – 20717Combined sources
Beta strandi210 – 2167Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 23411Combined sources
Beta strandi236 – 2427Combined sources
Helixi244 – 25613Combined sources
Turni261 – 2633Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi291 – 2933Combined sources
Helixi295 – 3017Combined sources
Helixi302 – 3043Combined sources
Beta strandi305 – 3106Combined sources
Helixi316 – 33318Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 36522Combined sources
Helixi373 – 3786Combined sources
Turni379 – 3824Combined sources
Beta strandi383 – 3875Combined sources
Beta strandi390 – 3945Combined sources
Beta strandi398 – 4003Combined sources
Beta strandi404 – 4096Combined sources
Turni411 – 4133Combined sources
Beta strandi416 – 4227Combined sources
Turni424 – 4263Combined sources
Beta strandi429 – 4324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000118959.
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.
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)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:
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_006232591.2.
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 .
PIRi S03348. OYRTR.
RefSeqi NP_036745.1. NM_012613.1.
XP_006232653.1. XM_006232591.2.
UniGenei Rn.10463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000118959.
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.
IPR029787. Nucleotide_cyclase.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 143 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