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Database: UniProt
Entry: H2M420_ORYLA
LinkDB: H2M420_ORYLA
Original site: H2M420_ORYLA 
ID   H2M420_ORYLA            Unreviewed;       806 AA.
AC   H2M420;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   Name=gucy1a2 {ECO:0000313|Ensembl:ENSORLP00000013181.1};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000013181.1, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000013181.1, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000013181.1,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000013181.1}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000013181.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; H2M420; -.
DR   STRING; 8090.ENSORLP00000013181; -.
DR   Ensembl; ENSORLT00000013182.2; ENSORLP00000013181.1; ENSORLG00000010515.2.
DR   eggNOG; KOG4171; Eukaryota.
DR   GeneTree; ENSGT00940000157765; -.
DR   HOGENOM; CLU_011614_5_0_1; -.
DR   InParanoid; H2M420; -.
DR   OMA; SLMLHYF; -.
DR   TreeFam; TF351403; -.
DR   Proteomes; UP000001038; Chromosome 13.
DR   Bgee; ENSORLG00000010515; Expressed in sexually immature organism and 4 other cell types or tissues.
DR   GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
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   3: Inferred from homology;
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001038}.
FT   DOMAIN          591..718
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          532..563
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  89147 MW;  EB271ADCC67547C7 CRC64;
     MSSSSRKISS ESFSSSVGSD CGLESPGGDG GGGGPELAEE NRGCPFSSLP SSQRALLWNG
     RSSAERSACA AGEEQQQQQQ QGPFIPHKRV TRRRRVNLDS LGESLKRLTS PTTQTVQEAL
     QRTLQFYRKQ EIRCQEVKSA ERRRERTEEK CPFLESSGSE EDVLQILQYM ATILGVPFCE
     LREHFGEEFF GLCFEENERV LRAVGGNLQD FFNGFDAILE HIRTSTGRRA SSESPSFQCK
     DPREEEKGKR KLDKVGNHGK VLLLHCFNPA PVVGLVMPGL IRAVARRIFH SEVEVEEVPP
     LTPLLPNEDT AHTGFDSTTP TPTASPTASP SSSPSPPSLF PTSIPTVCLS FQIQEVCPSS
     LSSCPSSSSV SIKRPPPSLS TNPSDLRIGL ATFCRAFPFH LVLGPHMELL QLGEGLRRQA
     RIEPHRSFSF RDCFEIVSPK MEPSFQGILL RLASPFTIRT RPDSTQAGTK EKVMELKGQM
     IHVPESCSLM FLGSPRVDKL EELMGRGLYL SDIPIHDATR DVILVGEQAK AQDGLKKRMD
     KLKATLERTH QALEEEKRRT VDLLYSIFPG DVAQKLWQGQ PVPARKFDDV TMLFSDIVGF
     TAVCAHCTPM QVISMLNELY TRFDYQCGIL DVYKIETIGD AYCVAGGLHK KVDSHAKPIA
     HMALKMMELS DEVLTPDGKP IKLRIGIHTG SVLAGVVGVK MPRYCLFGNN VTLASKFESG
     SHPRCINVSP TTYQLLKDDR SFSFVPRSRM DLPENFPKEI PGACYFLEAG TSHSHASLTS
     SRSAPPASMR KVSYSIGTMF LRETSL
//
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