ID I3IZ62_ORENI Unreviewed; 1050 AA.
AC I3IZ62;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
GN Name=NPR2 {ECO:0000313|Ensembl:ENSONIP00000001902.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001902.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000001902.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane 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 AlphaFoldDB; I3IZ62; -.
DR Ensembl; ENSONIT00000001901.2; ENSONIP00000001902.2; ENSONIG00000001521.2.
DR GeneTree; ENSGT00940000156985; -.
DR Proteomes; UP000005207; Linkage group LG11.
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; 6.10.250.780; -; 1.
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:SF483; GUANYLATE CYCLASE; 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; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1050
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025421081"
FT TRANSMEM 463..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 519..793
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 868..998
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT COILED 805..836
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1050 AA; 119026 MW; DFCC49DBD7ACB6DE CRC64;
MARWKEGAAL LLALPVLFSL RPEARTHGPG QTQRDHERLQ NITLAVILPE NNTRYPWAWP
RIGPAVDRAI RDINADPTLL PNHHLIYFFK NSQDKDGMCS ESVAPLMAVD LKLAYNPWAF
IGPGCSYSSS PVGLFTTHWG VPMVTAGAPA VAFSSGTYLS ITNTGPTHKK LGRFAVRICE
HFGWREQVMV VFSDDKKDDR PCYFAIEGLY MELSNINISV EESVFIEDKS VIYSQILSKI
QDNGRGESVT GRQINLMVEF RRENLTHEQY VFSTSTCLLT ALKSEHRQPW RRGDREDAIA
KEAFQSVKIL TYREPQNPEY QEFVQNLKAD AKDMFNYTIE DSLMNIIAGG FYDGLMLYAH
ALNESMLASN ERPNGKDVTP RMWNRTFPGQ CSPFVSFKAD SGDRETDFAL WDIVDTNSTT
FQEHLTAVPG THLHWLGGAP PPDFPVCGFK NDIPVCLAKT ITIYQMVSIV VFFFVILILT
VVIFIYRMKL EKELVAQLWR ISWDDIQMSN LNKVLRSGSK LTLSLRGSNY GSLMTGDGNL
QIFAKTGYHK GNIVAIKYIN KKRIELNRKV LFELKHMRDV QNEHLTRFIG ACIDPPNCCI
VTEYCSRGSL QDILENDSIT LDWMFKYSLI NDIVKGMLFL HNSVILSHGK LKSSNCVVDN
RFVLKITDYG LSSFRSESDA ASDAHAYYAQ KLWMAPELLR MECPPPQGTQ KGDVYSFGII
LQEVALRRGA FYLEGDPLSP KEIVDRVILG EWPCLRPTID PQSDRPQLGQ LMERCWAEEP
TERPEFNQIR VLLRKQNKES RTNILDNLLS RMEQYANNLE ELVEERTQAY HEEKRKAEAL
LYQILPHSVA EQLKRGETVQ AEAFDSVTIY FSDIVGFTAI SAESTPMEVV TLLNDLYTCF
DAIIDNFDVY KVETIGDAYM VVSGLPVRNG KLHGREIARM ALALLDAVRA FKIRHRPEQQ
LKLRIGIHSG PVCAGVVGLK MPRYCLFGDT VNTSSRMEST GEALKIHVSA ATRDVLLEFN
CFQLELRGEI DIKGKGKMTT YWLLGESDSQ
//
