ANPRB_ANGJA
ID ANPRB_ANGJA Reviewed; 1050 AA.
AC P55202;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Anguilla japonica (Japanese eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC Anguilla.
OX NCBI_TaxID=7937;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gill;
RX PubMed=7913035; DOI=10.1111/j.1432-1033.1994.tb18930.x;
RA Katafuchi T., Takashima A., Kashiwagi M., Hagiwara H., Takei Y., Hirose S.;
RT "Cloning and expression of eel natriuretic-peptide receptor B and
RT comparison with its mammalian counterparts.";
RL Eur. J. Biochem. 222:835-842(1994).
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 -!- TISSUE SPECIFICITY: High levels found in liver, atrium and gill.
CC Moderate levels found in brain and ventricle, and low levels in
CC esophageal sphincter, stomach, posterior intestine and kidney.
CC -!- INDUCTION: By osmotic stress; levels decrease under saline conditions.
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; D25417; BAA05007.1; -; mRNA.
DR PIR; S45636; S45636.
DR AlphaFoldDB; P55202; -.
DR SMR; P55202; -.
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:0016941; F:natriuretic peptide receptor activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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 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; 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; Signal; Stress response; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1050
FT /note="Atrial natriuretic peptide receptor 2"
FT /id="PRO_0000012367"
FT TOPO_DOM 20..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 517..790
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 865..995
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..110
FT /evidence="ECO:0000250"
FT DISULFID 236..339
FT /evidence="ECO:0000250"
FT DISULFID 443
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 452
FT /note="Interchain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 119858 MW; F3AC6DDD17BD3832 CRC64;
MDLGHSLFVV FTCFLMARCR TEIGKNITVV VMLPDNHLKY SFAFPRVFPA IRMAHDDIQK
KGKLLRGYTI NLLNHSTESQ GAGCSESQAQ IMAVDTKLYE KPDAFFGPGC VYSVASVGRF
VNHWKLPLIT AWAPAFGFDS KEEYRTIVRT GLSTTKLGEF AHYLHSHFNW TTRAFMLFHD
LKVDDRPYYF ISEGVFLVLR RENITVEAVP YDDQKNSDYR EMISSLKSNG RIVYICGPLD
TFLEFMRIFQ NEGLPPEDYA IFYLDMFAKS ILDKDYKPWE SSDINWTDPI KLFKSVFVIT
AKEPDNPEYK AFQRELHARA KQEFSVQLEP SLEDIIAGCF YDGFMLYAQA LNETLAEGGS
QNDGINITQK MQNRRFWGVT GLVSTDKNND RDIDFNLWAM TNHKTGQYGI VAYYNGTNKE
IVWSETEKIQ WPKGSPPLDN PPCVFSMDEP FCNEDQLPVL GIVAVGSGLA LIIFGISSFL
IYRKLKLEKE LAGMLWRIRW EELQFESPNK YHKCAGSRLT ISQRGSSYGS LITAHGKYQL
FAKTGYFKGN LVAIKHVNKK RIELTRQVLF ELKHMRDVQF NHLTRFIGAC IDPPNICIVT
EYCPRGSLQD ILENESINLD WMFRYSLIND IVKGMNFLHN SYIGSHGNLK SSNCVVDSRF
VLKITDYGLA SFRSSCENED SHALYAKKLW TAPELLIYDR HPPQGTQKGD VYSFGIILQE
IALRNGPFYV DGMDLSPKEI VQKVRNGQKP YFRPTTDTSC HSEELSILME GCWAEDPADR
PDFSYIKIFV MKLNKEGSTS ILNNLLSRME QYANNLENLV EERTQAYLEE KRKAENLLYQ
ILPHSVAEQL KRGETVQAEA FDSVTIYFSD IVGFTSMSAE STPLQVVTLL NDLYTCFDAI
IDNFDVYKVE TIGDAYMVVS DSQSRNGKLH AREIAGMSLA LLEQVKTFKI RHRPNDQLRL
RIGIHTGPVC AGVVGLKMPR YCLFGDTVNT ASRMESNGEA LKIHLSSATK EVLDEFGYFD
LQLRGDVEMK GKGKMRTYWL LGEKTDVYVI
