ID A0A3B5B8S1_9TELE Unreviewed; 1049 AA.
AC A0A3B5B8S1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Guanylate cyclase {ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|RuleBase:RU003431};
GN Name=npr2 {ECO:0000313|RefSeq:XP_008287267.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000029271.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000029271.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008287267.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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|RuleBase:RU003431};
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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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DR RefSeq; XP_008287267.1; XM_008289045.1.
DR AlphaFoldDB; A0A3B5B8S1; -.
DR STRING; 144197.ENSSPAP00000029271; -.
DR Ensembl; ENSSPAT00000029740.1; ENSSPAP00000029271.1; ENSSPAG00000021993.1.
DR GeneID; 103362640; -.
DR CTD; 4882; -.
DR GeneTree; ENSGT00940000156223; -.
DR OrthoDB; 3683909at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
DR GO; GO:0016020; C: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; -; 2.
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; 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 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; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW ECO:0000256|RuleBase:RU003431}; Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW Receptor {ECO:0000313|RefSeq:XP_008287267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1049
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041074847"
FT DOMAIN 516..789
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 864..994
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 801..828
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1049 AA; 118853 MW; 30A1AB1B3D00CC67 CRC64;
MGCRSALGCC LLAALSCCLP PGCRGNITVA VMLPDNHHKY PWALPRVFPA ILMAHEDLHG
KHKLLLGRSI NILNYSTEDP VAGSCAVSRA QVVAVDAKLY IRPDAFFGPG CVYPLASVGR
FASHWKLPLF TAGGPAYGFD KREEYRTIVR SGPSTTKLGD FANVLHTHFN WTSRAVVIFH
DLRQDDRPHY FLSEGIFLNL KEEMNVTVEA QPYEDDFKYY KDLITFMKER GRIVYICGPL
ETFLNIMKLF QSEIQDPENY AIFYLDVFAE SLADRKPWQN TESDWADPIE VFKSVFVITY
RPPDNPEYKD FQRKLHARAQ KDFGVHLEPS LMDYIAGSFY DGFVLYAMAL EETLADGGAQ
NDGINITMRT QNRNFWGVTG LVSMDDKNAR NIDVNLWAMT NQQTGEYGLV AYYNGTTKDI
IWSQMEKIHW PSGAPPLDNP PCVFSTDDPS CNDGHLPVLG IVAVGSGLAL IIFGISSFLI
YRKLKLEKEL AGMLWRIRWE DLQFESPNKY HKRAGSRLTL SQRGSSYGSL ITAHGKYQLF
AKTGYFKGNL VAIKHVNKKR IELTRQVLLE LKHMRDVQFN HLTRFIGACI DPPNICIVTE
YCPRGSLQDI LENESINLDW MFRYSLINDI VKGMNCLHNS YFGCHGNLKS SNCVVDSRFV
LKITDYGLAS FRSSCENDDS HALYAKKLWT APELLIYDRH PPQGTQKGDV YSFGIILQEI
GLRNGPFYVE GMDLSPKEIV QKVRNGQKPY FRPTTDNRCH SEELTILMEG CWAEDPAERP
DFGHIKIYMA KLNKEGSTSI LNNLLSRMEQ YANNLENLVE ERTQAYLEEK RKAENLLYQI
LPHSVAEQLK RGETVQAEAF DSVTIYFSDI VGFTSMSAES TPLQVVTLLN DLYTCFDAII
DNFDVYKVET IGDAYMVVSG LPVRNGKLHA REIAGMSLAL LEQVKTFKIR HRPNDQLRLR
IGIHTGPVCA GVVGLKMPRY CLFGDTVNTA SRMESNGEAL KIHVSSATKE VLDEFGYFDL
QLRGDVEMKG KGKMRTYWLL GEKTDVYVI
//