ANPRB_MOUSE
ID ANPRB_MOUSE Reviewed; 1047 AA.
AC Q6VVW5; B1AWI8; Q6VVW3; Q6VVW4; Q8CGA9;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Atrial natriuretic peptide receptor 2;
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:P20594};
DE AltName: Full=Atrial natriuretic peptide receptor type B;
DE Short=ANP-B;
DE Short=ANPR-B;
DE Short=NPR-B;
DE AltName: Full=Guanylate cyclase B;
DE Short=GC-B;
DE Flags: Precursor;
GN Name=Npr2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=129S6/SvEvTac; TISSUE=Spleen;
RX PubMed=14514678; DOI=10.1074/jbc.m308680200;
RA Tamura N., Garbers D.L.;
RT "Regulation of the guanylyl cyclase-B receptor by alternative splicing.";
RL J. Biol. Chem. 278:48880-48889(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15572448; DOI=10.1073/pnas.0407894101;
RA Tamura N., Doolittle L.K., Hammer R.E., Shelton J.M., Richardson J.A.,
RA Garbers D.L.;
RT "Critical roles of the guanylyl cyclase B receptor in endochondral
RT ossification and development of female reproductive organs.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17300-17305(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
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).
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:0000269|PubMed:15572448}.
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:0000250|UniProtKB:P20594};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20594};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20594}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=GC-B1;
CC IsoId=Q6VVW5-1; Sequence=Displayed;
CC Name=2; Synonyms=GC-B2;
CC IsoId=Q6VVW5-2; Sequence=VSP_013583;
CC Name=3; Synonyms=GC-B3;
CC IsoId=Q6VVW5-3; Sequence=VSP_013584, VSP_013585;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the columnar
CC proliferating and prehypertrophic chondrocyte layers of the tibia.
CC {ECO:0000269|PubMed:15572448}.
CC -!- PTM: Phosphorylated. Phosphorylation of the protein kinase-like domain
CC is required for full activation by CNP. {ECO:0000250|UniProtKB:P16067}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P20594}.
CC -!- DISRUPTION PHENOTYPE: Mice mainly display dwarfism associated with
CC impairment of endochondral ossification, reduced growth of longitudinal
CC vertebra and limb-bone. Self-clasping and priapism that could be due to
CC neuronal disorder are detected. The development of the female
CC reproductive organ is affected. {ECO:0000269|PubMed:15572448}.
CC -!- MISCELLANEOUS: [Isoform 2]: Binds ligand, but no cyclase activation.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Fail to bind the ligand. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AY323833; AAQ02634.1; -; Genomic_DNA.
DR EMBL; AY323832; AAQ02634.1; JOINED; Genomic_DNA.
DR EMBL; AY323833; AAQ02635.1; -; Genomic_DNA.
DR EMBL; AY323832; AAQ02635.1; JOINED; Genomic_DNA.
DR EMBL; AY323833; AAQ02636.1; -; Genomic_DNA.
DR EMBL; AY323832; AAQ02636.1; JOINED; Genomic_DNA.
DR EMBL; AL732626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02456.1; -; Genomic_DNA.
DR EMBL; BC042470; AAH42470.1; -; mRNA.
DR CCDS; CCDS18105.1; -. [Q6VVW5-1]
DR RefSeq; NP_776149.1; NM_173788.3. [Q6VVW5-1]
DR RefSeq; XP_006537896.1; XM_006537833.3.
DR AlphaFoldDB; Q6VVW5; -.
DR SMR; Q6VVW5; -.
DR BioGRID; 230934; 4.
DR STRING; 10090.ENSMUSP00000030191; -.
DR GlyGen; Q6VVW5; 7 sites.
DR iPTMnet; Q6VVW5; -.
DR PhosphoSitePlus; Q6VVW5; -.
DR MaxQB; Q6VVW5; -.
DR PaxDb; Q6VVW5; -.
DR PeptideAtlas; Q6VVW5; -.
DR PRIDE; Q6VVW5; -.
DR ProteomicsDB; 282116; -. [Q6VVW5-1]
DR ProteomicsDB; 282117; -. [Q6VVW5-2]
DR ProteomicsDB; 282118; -. [Q6VVW5-3]
DR Antibodypedia; 1647; 243 antibodies from 32 providers.
DR DNASU; 230103; -.
DR Ensembl; ENSMUST00000030191; ENSMUSP00000030191; ENSMUSG00000028469. [Q6VVW5-1]
DR GeneID; 230103; -.
DR KEGG; mmu:230103; -.
DR UCSC; uc008sqm.1; mouse. [Q6VVW5-1]
DR CTD; 4882; -.
DR MGI; MGI:97372; Npr2.
DR VEuPathDB; HostDB:ENSMUSG00000028469; -.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156985; -.
DR InParanoid; Q6VVW5; -.
DR OMA; AAKSEHY; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; Q6VVW5; -.
DR TreeFam; TF106338; -.
DR Reactome; R-MMU-5578768; Physiological factors.
DR BioGRID-ORCS; 230103; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Npr2; mouse.
DR PRO; PR:Q6VVW5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6VVW5; protein.
DR Bgee; ENSMUSG00000028469; Expressed in retinal neural layer and 218 other tissues.
DR ExpressionAtlas; Q6VVW5; baseline and differential.
DR Genevisible; Q6VVW5; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:MGI.
DR GO; GO:0042562; F:hormone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; IDA:MGI.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISO:MGI.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:MGI.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:MGI.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IMP:MGI.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR GO; GO:0022414; P:reproductive process; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
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 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; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00458; ANF_RECEPTORS; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; cGMP biosynthesis; Disulfide bond;
KW Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding;
KW Osteogenesis; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1047
FT /note="Atrial natriuretic peptide receptor 2"
FT /id="PRO_0000012365"
FT TOPO_DOM 17..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..1047
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 513..786
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 861..991
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20594"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20594"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20594"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16066"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20594"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20594"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20594"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..101
FT /evidence="ECO:0000250"
FT DISULFID 439
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 448
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 407..418
FT /note="PAAHYSGAEKQI -> VMGERTGRRDWS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_013584"
FT VAR_SEQ 419..1047
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_013585"
FT VAR_SEQ 520..544
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_013583"
FT CONFLICT 990
FT /note="M -> K (in Ref. 1; AAQ02634/AAQ02635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 117060 MW; 34E6C00E561D6D87 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
HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH VSSTTKDALD ELGCFQLELR
GDVEMKGKGK MRTYWLLGEQ KGPPGLL
