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Database: UniProt
Entry: Q8JIE7_ORYCU
LinkDB: Q8JIE7_ORYCU
Original site: Q8JIE7_ORYCU 
ID   Q8JIE7_ORYCU            Unreviewed;       859 AA.
AC   Q8JIE7;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 119.
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=OcGC8 {ECO:0000313|EMBL:BAC10588.1};
OS   Oryzias curvinotus (Hynann ricefish) (Aplocheilus curvinotus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=104658 {ECO:0000313|EMBL:BAC10588.1};
RN   [1] {ECO:0000313|EMBL:BAC10588.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAC10588.1};
RA   Shiga T., Suzuki N.;
RT   "Oryzias curvinotus mRNA for membrane guanylyl cyclase OcGC8, partial
RT   cds.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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: Photoreceptor outer segment membrane
CC       {ECO:0000256|ARBA:ARBA00004451}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004451}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; AB090274; BAC10588.1; -; mRNA.
DR   AlphaFoldDB; Q8JIE7; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd14045; PK_GC_unk; 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; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF458; GUANYLATE CYCLASE; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 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   2: Evidence at transcript level;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW   ECO:0000256|RuleBase:RU003431};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
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}; Vision {ECO:0000256|ARBA:ARBA00023305}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..859
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004309214"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          278..568
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          638..768
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          822..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  96027 MW;  82DD226179A3FD60 CRC64;
     MKKWVQVLVL VCVCCVGPVC CWHDLDNSEY DCWPLQGPNE FNMIDCGGLE MAWVVRPPEL
     VKSGEVFSVT YSVTARDSFY DWAIQNHIFT QSYITDAASA RSFCEHHECP ANWKDANGEN
     CCIHHANIHS CPLGYMTTES ICGPWIPDDG KIFTHTISTS GKMSQTNWTA KVVLLHAGLT
     SLIAHIRVGI MQAALEAKST VLPAVVCGNN VCEEGEFCST CPADCGDCPM TMTTKMAIGL
     PVSLFCLSFI LTAVWLRYQK EKLLWDESWI IDFSMIKQDQ ESRMTMGSIM SVPVGNSDSN
     TSCLTGLNSC TGQPGTRKTP FICTGIYDGR TVAIKRIQTK MFSLSKTIRQ EVKQVRELDH
     PNLCKFIGGC IEVPNIAIIT EYCPKGSLND VLLNEEIPIN WGFRFSFAAD IARGMSYLHQ
     HKICHGRLKS MNCVLDDRWV CKITDYGLRM YCRDDGTEPL STYQQRLMEV YMPPEFQNSN
     MEPTLAGDVF SYSIILLEIA TRNDPVPAEE SSLDCGWCPP LPELISSKTD NTCPCPADYV
     DLIRRCRSHN PAHRPTFEQI KKFVHRINPI KVSPVDMMMN LMEKYSKHLE VLVAERTQDL
     THEKQKTDRL LYSMLPKQVA DDLRQGKPSQ AQSYVSATVF FSDIVGFTQL SSSSTPYQVV
     DFLNKLYTTF DNIIDNYDVY KVETIGDAYM VVSGVPQENG ILHASEIASM ALDLVGVCRT
     FRIPHKPSMQ LQIRAGIHSG PVVAGVVGTK MPRYCLFGDT VNTASRMEST STALKIQCSS
     STFYLLEEIG GYVLECRGVQ QVKGKGDMVT YWLQGKKTTP VTKDVKESEP PKAVTMETEA
     EREASIPGFL SDDLLMDPV
//
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