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Database: UniProt
Entry: V8N9Z5_OPHHA
LinkDB: V8N9Z5_OPHHA
Original site: V8N9Z5_OPHHA 
ID   V8N9Z5_OPHHA            Unreviewed;       771 AA.
AC   V8N9Z5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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};
DE   Flags: Fragment;
GN   Name=NPR2 {ECO:0000313|EMBL:ETE58463.1};
GN   ORFNames=L345_15815 {ECO:0000313|EMBL:ETE58463.1};
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE58463.1, ECO:0000313|Proteomes:UP000018936};
RN   [1] {ECO:0000313|EMBL:ETE58463.1, ECO:0000313|Proteomes:UP000018936}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Blood {ECO:0000313|EMBL:ETE58463.1};
RX   PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA   Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA   McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA   Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA   de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA   Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA   Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA   Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT   "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT   snake venom system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETE58463.1}.
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DR   EMBL; AZIM01006707; ETE58463.1; -; Genomic_DNA.
DR   Proteomes; UP000018936; Unassembled WGS sequence.
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   CDD; cd07302; CHD; 1.
DR   CDD; cd14042; PK_GC-A_B; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
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; 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:SF508; 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; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW   Receptor {ECO:0000313|EMBL:ETE58463.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..771
FT                   /note="Atrial natriuretic peptide receptor 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004770586"
FT   TRANSMEM        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          316..663
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          681..725
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          500..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          618..645
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        500..521
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETE58463.1"
SQ   SEQUENCE   771 AA;  86113 MW;  4CB0E4D577F48C1A CRC64;
     MGGKGWRLSC RGTWASMSLG QWPFLQTVLV ITYHEPQTLE YRDFQNKLIL RARQEYQVEL
     SGSLKNLVAG CFHDGLLLYA LALNETLHEG DTKLNNSRIL EKMKGRRFQG VTGTVSMDQN
     NDRDTDFNLW AMTEGDSGAY QVVGHYVGSE KQLKWLGPIY WVKGQPPLDN PPCFDMDDPS
     CDKSALSTLA ILALGAGLTF IMFGVSSFLI FRCLSKLLGG LEYSGREGGV PWPDRQCAAR
     EEEGHSALNP AWVQLQGTGG RGVSHGAMAW SGSSGAIVGL GRKLMLEKEL ASMLWRIRWE
     DLQFGGTERY HKGAGSRLTL SLRGSSYGSL MTAHGKYQIF ANTGLFKGNV VAIKHINKKR
     IELTRQVLFE LKHMRDIQFN HLTRFIGACI DPPNICIVTE YCPRGSLQDI LENESINLDW
     MFRYALINDI VKGMAFLHNS IIGYHGSLKS CNCVVDSRFV LKITDYGLAS FRQGHESEGN
     HALYASECLA SPPPXXPPWL PPCLSPGEAQ APHPLTPDSP APAPEKLWTA PELLQKGTLL
     PLPLAMQKAD VYSFGIILQE IALRSGAFYV EGIELSPKEI VQKVGNSQLP YFRPTIDTRL
     HSEELAVLME REGSTSILDN LLSRMEQYAN NLEKLVEERT QAYLEEKRKA ENLLYQILPH
     SVAEQLKRGE TVQAEAFDCV TIYFSDIVGF TSLSAESTPM QVVTLLNDLY TCFDAIIDNF
     DVYKIHISAA TKEILDEFGC FLLELRGDVE MKGKGKMRTY WLLGEEKASV I
//
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