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Atrial natriuretic peptide receptor 1 (EC 4.6.1.2) (Atrial natriuretic peptide receptor type A) (ANP-A) (ANPR-A) (NPR-A) (Guanylate cyclase A) (GC-A)

 ANPRA_MOUSE             Reviewed;        1057 AA.
P18293;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
05-DEC-2018, entry version 179.
RecName: Full=Atrial natriuretic peptide receptor 1;
EC=4.6.1.2;
AltName: Full=Atrial natriuretic peptide receptor type A;
Short=ANP-A;
Short=ANPR-A;
Short=NPR-A;
AltName: Full=Guanylate cyclase A;
Short=GC-A;
Flags: Precursor;
Name=Npr1; Synonyms=Npra;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=1973687;
Pandey K.N., Singh S.;
"Molecular cloning and expression of murine guanylate cyclase/atrial
natriuretic factor receptor cDNA.";
J. Biol. Chem. 265:12342-12348(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7838126;
Schoenfeld J.R., Sehl P., Quan C., Burnier J.P., Lowe D.G.;
"Agonist selectivity for three species of natriuretic peptide
receptor-A.";
Mol. Pharmacol. 47:172-180(1995).
[3]
DISRUPTION PHENOTYPE.
PubMed=9405681; DOI=10.1073/pnas.94.26.14730;
Oliver P.M., Fox J.E., Kim R., Rockman H.A., Kim H.S., Reddick R.L.,
Pandey K.N., Milgram S.L., Smithies O., Maeda N.;
"Hypertension, cardiac hypertrophy, and sudden death in mice lacking
natriuretic peptide receptor A.";
Proc. Natl. Acad. Sci. U.S.A. 94:14730-14735(1997).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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.
-!- CATALYTIC ACTIVITY:
Reaction=GTP = 3',5'-cyclic GMP + diphosphate;
Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
ChEBI:CHEBI:57746; EC=4.6.1.2;
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- PTM: Phosphorylation of the protein kinase-like domain is required
for full activation by ANP. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display systemic hypertension
associated with cardiac hypertrophy and ventricular enlargement.
{ECO:0000269|PubMed:9405681}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-----------------------------------------------------------------------
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EMBL; J05504; AAA37670.1; -; mRNA.
EMBL; L31932; AAA66945.1; -; mRNA.
CCDS; CCDS17529.1; -.
PIR; A36568; OYMSAR.
PIR; I57963; I57963.
RefSeq; NP_032753.5; NM_008727.5.
UniGene; Mm.4627; -.
ProteinModelPortal; P18293; -.
SMR; P18293; -.
BioGrid; 201830; 3.
ComplexPortal; CPX-34; ANPR-A receptor complex.
STRING; 10090.ENSMUSP00000029540; -.
iPTMnet; P18293; -.
PhosphoSitePlus; P18293; -.
PaxDb; P18293; -.
PRIDE; P18293; -.
Ensembl; ENSMUST00000029540; ENSMUSP00000029540; ENSMUSG00000027931.
GeneID; 18160; -.
KEGG; mmu:18160; -.
UCSC; uc008qcg.1; mouse.
CTD; 4881; -.
MGI; MGI:97371; Npr1.
eggNOG; KOG1023; Eukaryota.
eggNOG; COG2114; LUCA.
GeneTree; ENSGT00940000156223; -.
HOGENOM; HOG000293307; -.
HOVERGEN; HBG051862; -.
InParanoid; P18293; -.
KO; K12323; -.
OMA; REDPSML; -.
OrthoDB; EOG091G02QS; -.
PhylomeDB; P18293; -.
TreeFam; TF106338; -.
BRENDA; 4.6.1.2; 3474.
Reactome; R-MMU-5578768; Physiological factors.
ChiTaRS; Npr1; mouse.
PRO; PR:P18293; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027931; Expressed in 70 organ(s), highest expression level in female gonad.
CleanEx; MM_NPR1; -.
ExpressionAtlas; P18293; baseline and differential.
Genevisible; P18293; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IDA:MGI.
GO; GO:0042562; F:hormone binding; ISO:MGI.
GO; GO:0016941; F:natriuretic peptide receptor activity; ISS:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0006182; P:cGMP biosynthetic process; ISO:MGI.
GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
GO; GO:0042417; P:dopamine metabolic process; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:MGI.
GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISO:MGI.
GO; GO:0050880; P:regulation of blood vessel size; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 3.30.70.1230; -; 1.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR001170; ANPR/GUC.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR029787; Nucleotide_cyclase.
InterPro; IPR028082; Peripla_BP_I.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00211; Guanylate_cyc; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR00255; NATPEPTIDER.
SMART; SM00044; CYCc; 1.
SUPFAM; SSF53822; SSF53822; 1.
SUPFAM; SSF55073; SSF55073; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00458; ANF_RECEPTORS; 1.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
cGMP biosynthesis; Chloride; Complete proteome; Disulfide bond;
Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Vasoactive.
SIGNAL 1 28
CHAIN 29 1057 Atrial natriuretic peptide receptor 1.
/FTId=PRO_0000012361.
TOPO_DOM 29 469 Extracellular. {ECO:0000255}.
TRANSMEM 470 490 Helical. {ECO:0000255}.
TOPO_DOM 491 1057 Cytoplasmic. {ECO:0000255}.
DOMAIN 524 801 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 872 1002 Guanylate cyclase. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
BINDING 81 81 Chloride. {ECO:0000250}.
BINDING 113 113 Chloride; via amide nitrogen.
{ECO:0000250}.
BINDING 114 114 Chloride; via amide nitrogen.
{ECO:0000250}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000250|UniProtKB:P16066}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000250|UniProtKB:P16066}.
MOD_RES 528 528 Phosphothreonine.
{ECO:0000250|UniProtKB:P16066}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000250|UniProtKB:P16066}.
MOD_RES 534 534 Phosphoserine.
{ECO:0000250|UniProtKB:P16066}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000250|UniProtKB:P18910}.
MOD_RES 541 541 Phosphothreonine.
{ECO:0000250|UniProtKB:P18910}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 375 375 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 88 114 {ECO:0000250}.
DISULFID 192 241 {ECO:0000250}.
DISULFID 451 460 {ECO:0000250}.
CONFLICT 3 3 G -> R (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 39 39 L -> V (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 122 122 G -> D (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 130 130 V -> L (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 285 285 R -> E (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 301 301 A -> R (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 404 405 FS -> SP (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 590 590 H -> Q (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 652 652 G -> C (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 833 833 A -> P (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 958 958 R -> G (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 1044 1044 T -> S (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 1050 1050 E -> D (in Ref. 1; AAA37670).
{ECO:0000305}.
CONFLICT 1055 1057 TRG -> SRA (in Ref. 1; AAA37670).
{ECO:0000305}.
SEQUENCE 1057 AA; 119109 MW; 53A544FB2C8EF253 CRC64;
MPGSRRVRPR LRALLLLPPL LLLRSGHASD LTVAVVLPLT NTSYPWSWAR VGPAVELALG
RVKARPDLLP GWTVRMVLGS SENAAGVCSD TAAPLAAVDL KWEHSPAVFL GPGCVYSAAP
VGRFTAHWRV PLLTAGAPAL GIGVKDEYAL TTRTGPSHVK LGDFVTALHR RLGWEHQALV
LYADRLGDDR PCFFIVEGLY MRVRERLNIT VNHQEFVEGD PDHYTKLLRT VQRKGRVIYI
CSSPDAFRNL MLLALDAGLT GEDYVFFHLD VFGQSLQGAQ GPVPRKPWER DDGQDRRARQ
AFQAAKIITY KEPDNPEYLE FLKQLKLLAD KKFNFTMEDG LKNIIPASFH DGLLLYVQAV
TETLAQGGTV TDGENITQRM WNRSFQGVTG YLKIDRNGDR DTDFSLWDMD PETGAFRVVL
NFNGTSQELM AVSEHRLYWP LGYPPPDIPK CGFDNEDPAC NQDHFSTLEV LALVGSLSLV
SFLIVSFFIY RKMQLEKELV SELWRVRWED LQPSSLERHL RSAGSRLTLS GRGSNYGSLL
TTEGQFQVFA KTAYYKGNLV AVKRVNRKRI ELTRKVLFEL KHMRDVQNEH LTRFVGACTD
PPNICILTEY CPRGSLQDIL ENESITLDWM FRYSLTNDIV KGMLFLHNGA IGSHGNLKSS
NCVVDGRFVL KITDYGLESF RDPEPEQGHT LFAKKLWTAP ELLRMASPPA RGSQAGDVYS
FGIILQEIAL RSGVFYVEGL DLSPKEIIER VTRGEQPPFR PSMDLQSHLE ELGQLMQRCW
AEDPQERPPF QQIRLALRKF NKENSSNILD NLLSRMEQYA NNLEELVEER TQAYLEEKRK
AEALLYQILP HSVAEQLKRG ETVQAEAFDS VTIYFSDIVG FTALSAESTP MQVVTLLNDL
YTCFDAVIDN FDVYKVETIG DAYMVVSGLP VRNGQLHARE VARMALALLD AVRSFRIRHR
PQEQLRLRIG IHTGPVCAGV VGLKMPRYCL FGDTVNTASR MESNGEALRI HLSSETKAVL
EEFDGFELEL RGDVEMKGKG KVRTYWLLGE RGCSTRG


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