ANPRB_BOVIN
ID ANPRB_BOVIN Reviewed; 1047 AA.
AC P46197;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7845391; DOI=10.1007/bf00944079;
RA Fenrick R., Babinski K., McNicoll N., Therrien N., Drouin J., de Lean A.;
RT "Cloning and functional expression of the bovine natriuretic peptide
RT receptor-B (natriuretic factor R1c subtype).";
RL Mol. Cell. Biochem. 137:173-182(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 551-1047.
RC TISSUE=Retina;
RX PubMed=8103329;
RA Shmukler B.E., Zubov D.V., Abdulaev N.G.;
RT "Detection of expression of a membrane form of the guanylate cyclase type
RT of GC-B in cattle retina.";
RL Bioorg. Khim. 19:682-685(1993).
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:0000250|UniProtKB:P20594}.
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 -!- 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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; L26359; AAC41619.1; -; mRNA.
DR EMBL; X66865; CAA47334.1; -; mRNA.
DR PIR; I45882; I45882.
DR RefSeq; NP_776551.1; NM_174126.2.
DR RefSeq; XP_010806265.1; XM_010807963.2.
DR AlphaFoldDB; P46197; -.
DR SMR; P46197; -.
DR STRING; 9913.ENSBTAP00000015204; -.
DR BindingDB; P46197; -.
DR ChEMBL; CHEMBL2156; -.
DR PaxDb; P46197; -.
DR PRIDE; P46197; -.
DR Ensembl; ENSBTAT00000015204; ENSBTAP00000015204; ENSBTAG00000011434.
DR GeneID; 281357; -.
DR KEGG; bta:281357; -.
DR CTD; 4882; -.
DR VEuPathDB; HostDB:ENSBTAG00000011434; -.
DR VGNC; VGNC:106847; NPR2.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156985; -.
DR HOGENOM; CLU_013995_0_0_1; -.
DR InParanoid; P46197; -.
DR OMA; AAKSEHY; -.
DR OrthoDB; 229634at2759; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000011434; Expressed in uterine horn and 104 other tissues.
DR ExpressionAtlas; P46197; baseline and differential.
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; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:AgBase.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; ISS:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:AgBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell membrane; cGMP biosynthesis; Disulfide bond; Glycoprotein;
KW GTP-binding; Lyase; Membrane; Nucleotide-binding; Osteogenesis;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1047
FT /note="Atrial natriuretic peptide receptor 2"
FT /id="PRO_0000012363"
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:0000305"
FT DISULFID 448
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT CONFLICT 958
FT /note="I -> L (in Ref. 2; CAA47334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 117146 MW; 1A3814D02F22D64F CRC64;
MALPSLLLVV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAMEALGRAL
PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL
TAGAVASGFS AKSEHYRTLV RTGPSAPKLG EFVVMLHGHF NWTARAALLY LDARTDDRPH
YFTIEGVFEA LQGSNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA
QRENLTNGDY VFFYLDVFGE SLRAGPTRSM GRPWQDNRTR EQAQALREAF QTVLVITYRE
PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAEVLNE TIQEGGTRED
GLRIVEKMQG RRYRGVTGLV VMDKNNDRET DFVLWAMGDL VSGDFQPAAH YSGAEKQIWW
TGRPIPWVKG VPPLDNPPCA FDMDDPSCDK TPLSTLAIVA LGTGITFIMF GVSSFLIFRK
LMLEKELASM LWRIRWEELQ FGNSERCHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT
GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP
RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIA SHGSLKSSNC VVDSRFVLKI
TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF GIILQEIALR
SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPAERPDFG
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 MRTYWLLGER KGPAGLL
