ID   B1AWI7_MOUSE            Unreviewed;      1033 AA.
AC   B1AWI7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   RecName: Full=Atrial natriuretic peptide receptor 2 {ECO:0000256|ARBA:ARBA00044153};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
DE   AltName: Full=Atrial natriuretic peptide receptor type B {ECO:0000256|ARBA:ARBA00044222};
DE   AltName: Full=Guanylate cyclase B {ECO:0000256|ARBA:ARBA00044260};
GN   Name=Npr2 {ECO:0000313|Ensembl:ENSMUSP00000103506.3,
GN   ECO:0000313|MGI:MGI:97372};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000103506.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000103506.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103506.3,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000103506.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103506.3,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000103506.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103506.3};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone.
CC       Has guanylate cyclase activity upon binding of its ligand. May play a
CC       role in the regulation of skeletal growth.
CC       {ECO:0000256|ARBA:ARBA00043880}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001436};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|PROSITE-ProRule:PRU00099}.
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DR   AlphaFoldDB; B1AWI7; -.
DR   SMR; B1AWI7; -.
DR   jPOST; B1AWI7; -.
DR   PeptideAtlas; B1AWI7; -.
DR   ProteomicsDB; 348761; -.
DR   Antibodypedia; 1647; 259 antibodies from 34 providers.
DR   Ensembl; ENSMUST00000107874.9; ENSMUSP00000103506.3; ENSMUSG00000028469.16.
DR   AGR; MGI:97372; -.
DR   MGI; MGI:97372; Npr2.
DR   VEuPathDB; HostDB:ENSMUSG00000028469; -.
DR   GeneTree; ENSGT00940000156985; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000028469; Expressed in retinal neural layer and 221 other cell types or tissues.
DR   ExpressionAtlas; B1AWI7; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0042060; P:wound healing; IEA:UniProtKB-ARBA.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06384; PBP1_NPR_B; 1.
DR   CDD; cd14042; PK_GC-A_B; 1.
DR   FunFam; 1.10.510.10:FF:000270; Guanylate cyclase; 1.
DR   FunFam; 3.30.200.20:FF:001106; Guanylate cyclase; 1.
DR   FunFam; 3.30.70.1230:FF:000102; Guanylate cyclase; 1.
DR   FunFam; 3.40.50.2300:FF:000101; Guanylate cyclase; 1.
DR   FunFam; 3.40.50.2300:FF:000245; Guanylate cyclase; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR001170; ANPR/GUC.
DR   InterPro; IPR050401; Cyclic_nucleotide_synthase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF494; ATRIAL NATRIURETIC PEPTIDE RECEPTOR 2; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00255; NATPEPTIDER.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00458; ANF_RECEPTORS; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00099};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B1AWI7,
KW   ECO:0007829|ProteomicsDB:B1AWI7}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1033
FT                   /note="Atrial natriuretic peptide receptor 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002760009"
FT   DOMAIN          513..786
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          861..963
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   COILED          798..825
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         866
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         866
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         867
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         910
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
FT   BINDING         910
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00099"
SQ   SEQUENCE   1033 AA;  115772 MW;  87F1DA1FD1641ABF CRC64;
     MALPSLLLVV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL
     PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL
     TAGAVASGFA AKNEHYRTLV RTGPSAPKLG EFVVTLHGHF NWTARAALLY LDARTDDRPH
     YFTIEGVFEA LQGSNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA
     QRENLTNGDY VFFYLDVFGE SLRAGPTRAT GRPWQDNRTQ EQAQALREAF QTVLVITYRE
     PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAQVLNE TIQEGGTRED
     GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL DSGDFQPAAH YSGAEKQIWW
     TGRPIPWVKG APPLDNPPCA FDLDDPSCDK TPLSTLAIVA LGTGVTFIMF GVSSFLIFRK
     LMLEKELASM LWRIRWEELQ FGNSDRYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT
     GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP
     RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC VVDSRFVLKI
     TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF AIILQEIALR
     SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPTERPDFG
     QIKGFIRRFN KEGGTSILDN LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH
     SVAEQLKRGE TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF
     DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP HDQLRLRIGV
     HTGKADSHLA LVSTFPDLSQ PVCFYRASLC WGGWPEDAPV LSFWRHSKHC FSNGVEWPSS
     KDPCLLDHQG RPG
//