ID F1QNR4_DANRE Unreviewed; 608 AA. AC F1QNR4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 07-APR-2021, entry version 73. DE RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202}; DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202}; GN Name=gucy1b1 {ECO:0000313|Ensembl:ENSDARP00000105472, GN ECO:0000313|ZFIN:ZDB-GENE-090313-160}; GN Synonyms=sgc1b1 {ECO:0000313|EMBL:CCD30519.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OG Plasmid pET21a {ECO:0000313|EMBL:CCD30519.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000105472, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000105472} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105472}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|EMBL:CCD30519.1} RP NUCLEOTIDE SEQUENCE. RC PLASMID=pET21a {ECO:0000313|EMBL:CCD30519.1}; RC TISSUE=Brain {ECO:0000313|EMBL:CCD30519.1}; RA Shaik T.B., Meena Lakshmi M.G., Idris M.M., Pal B.; RT "Danio rerio soluble guanylate cyclase small subunit beta 1."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSDARP00000105472, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105472, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). 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|ARBA:ARBA00001436}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU571168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; HE583294; CCD30519.1; -; mRNA. DR RefSeq; NP_001238874.1; NM_001251945.1. DR STRING; 7955.ENSDARP00000105472; -. DR Ensembl; ENSDART00000129471; ENSDARP00000105472; ENSDARG00000086790. DR GeneID; 100150304; -. DR KEGG; dre:100150304; -. DR CTD; 2983; -. DR ZFIN; ZDB-GENE-090313-160; gucy1b1. DR eggNOG; KOG4171; Eukaryota. DR GeneTree; ENSGT00940000157483; -. DR HOGENOM; CLU_011614_4_0_1; -. DR OMA; EFLCEAP; -. DR OrthoDB; 531253at2759; -. DR TreeFam; TF351403; -. DR Proteomes; UP000000437; Chromosome 1. DR Bgee; ENSDARG00000086790; Expressed in swim bladder and 20 other tissues. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central. 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:0019934; P:cGMP-mediated signaling; IBA:GO_Central. DR GO; GO:0099555; P:trans-synaptic signaling by nitric oxide, modulating synaptic transmission; IBA:GO_Central. DR CDD; cd07302; CHD; 1. DR Gene3D; 3.30.450.260; -; 1. DR Gene3D; 3.30.70.1230; -; 1. DR Gene3D; 3.90.1520.10; -; 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 Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF07700; HNOB; 1. DR Pfam; PF07701; HNOBA; 1. DR SMART; SM00044; CYCc; 1. DR SUPFAM; SSF111126; SSF111126; 1. DR SUPFAM; SSF55073; SSF55073; 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:ARBA00022741}; KW Plasmid {ECO:0000313|EMBL:CCD30519.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 421..554 FT /note="Guanylate cyclase" FT /evidence="ECO:0000259|PROSITE:PS50125" FT COILED 366..393 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 608 AA; 69197 MW; 69200EB84DC67648 CRC64; MYGFVNHALE LLVLRNYGPD VWEDIKREAQ VDVEGQFLVR IIYEDAKTYD LVAAASKVLK MDAGGILQMF GKMFFEFCQE SGYDTILRVL GSNVREFLQN LDALHDHLGT IYPGMRAPSF RCTDAEKGNN LILHYYSERE GLQDIVIGII KTVAQQIHGT EIEMKVIQPK SEECDHIKFL IEEKDSEEEA FYEDLDGFEE NGTQETRISP YTFCKAFPFH LMFDKDLMLT QCGNAIFRVL PQLQPGVCNL SSVFSLVRPH IDFSFHGILS HINTVFVLRS KEGLLNVETA ENEDELTGTE ISCLRLKGQM ISLPETENIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR DLVLLGEQFR EEYKLTQELE ILTDRLQHTL RALEDEKKKT DRLLYSVLPP SVANELRHKR PVPAKRYDNV TILFSGIVGF NAFCSKHASA EGAIKIVNLL NDIYTRFDIL TDSRKNPYVY KVETVGDKYM TVSGLPEPCT HHAKSICHLA LDMMEIAGQV KVDEDPVQIT IGIHTGEVVT GVIGQRMPRY CLFGNTVNLT SRTETTGEKG KINVSEYTYR CLQSVENADP QFHLEYRGPV TMKGKKEPMK VWFLSRKT //