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Database: UniProt
Entry: Q7T040_ORYCU
LinkDB: Q7T040_ORYCU
Original site: Q7T040_ORYCU 
ID   Q7T040_ORYCU            Unreviewed;       804 AA.
AC   Q7T040;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   22-FEB-2023, entry version 86.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   Name=OcGCS-alpha2 {ECO:0000313|EMBL:BAC80221.1};
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:BAC80221.1};
RN   [1] {ECO:0000313|EMBL:BAC80221.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAC80221.1};
RX   PubMed=15465675; DOI=10.1016/j.cbpc.2004.08.001;
RA   Shiga T., Suzuki N.;
RT   "Expression of guanylyl cyclase genes in medaka hybrids (Oryzias curvinotus
RT   x Oryzias latipes).";
RL   Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 139:281-286(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000256|RuleBase:RU000405}.
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DR   EMBL; AB115704; BAC80221.1; -; mRNA.
DR   AlphaFoldDB; Q7T040; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 6.10.250.780; -; 1.
DR   Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR   Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR038158; H-NOX_domain_sf.
DR   InterPro; IPR011644; Heme_NO-bd.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR042463; HNOB_dom_associated_sf.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45655:SF7; GUANYLATE CYCLASE SOLUBLE SUBUNIT ALPHA-2; 1.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134}.
FT   DOMAIN          589..716
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          530..561
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   804 AA;  89053 MW;  239A58CE86F93F24 CRC64;
     MSSSSRKISS ESFSSSVGSD CGLESPGGDG GGGGPELAEE NRGCPFSSLP FSQRALLWNG
     RSSAERSACA ASEEQQQQQG PFIPHKRVTR RRRVNLDSLG ESLKRLTSPT TQTVQEALQR
     TLQFYRKQEI RCQEVKSAER RRERTEEKCP FLESSGSEED VLQILQYMAT ILGVPFCELR
     EHFGEEFFGL CFEENERVLR AVGGNLQDFF NGFDAILEHI RTSTGRRASS ESPSFQCKDP
     REEEKGRRKL DKVGNHGKVL LLHCFNPAPV VGLVMPGLIR AVARRIFHSE VEVEEVPPLT
     PLLPNEDTAH TGFDSTTPTP TASPTASPSS SPSPPSLFPT SIPTVCLSFQ IQEVCPSSLL
     SSPSSSSDSI KRPPLSLSTN PSDLRIGLAT FCRAFPFHLV LGPHMELLQL GEGLRRQARI
     EPHRSFSFRD CFEIVSPKME PSFQGILLRL ASPFTIRTRP DSTQAGTKEK VMELKGQMIH
     VPESCSLMFL GSPRVDKLEE LMGRGLHLSD IPIHDATRDV ILVGEQAKAQ DGLKKRMDKL
     KATLERTHQA LEEEKRRTVD LLYSIFPGDV AQKLWQGQPV PARKFDDVTM LFSDIVGFTA
     VCAHCTPMQV ISMLNELYTR FDYQCGILDV YKIETIGDAY CVAGGLHKKV ESHAKPIAHM
     ALKMMELSEE VLTPDGKPIK LRIGIHTGSV LAGVVGVKMP RYCLFGNNVT LASKFESGSH
     PRCINVSPTT YQLLKDDRSF SFVPRSRMDL PENFPKEIPG ACYFLEAGTS HSHASLTSSR
     SAPPASMRKV SYSIGTMFLR ETSL
//
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