ID F1QNR4_DANRE Unreviewed; 608 AA. AC F1QNR4; G4V4I7; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 29-MAY-2024, entry version 88. DE RecName: Full=Guanylate cyclase soluble subunit beta-1 {ECO:0000256|ARBA:ARBA00039698}; DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202}; DE AltName: Full=Guanylate cyclase soluble subunit beta-3 {ECO:0000256|ARBA:ARBA00041698}; DE AltName: Full=Soluble guanylate cyclase small subunit {ECO:0000256|ARBA:ARBA00043208}; GN Name=gucy1b1 {ECO:0000313|Ensembl:ENSDARP00000105472, GN ECO:0000313|RefSeq:NP_001238874.1, GN ECO:0000313|ZFIN:ZDB-GENE-090313-160}; GN Synonyms=gucy1b3 {ECO:0000313|RefSeq:NP_001238874.1}, sGC GN {ECO:0000313|RefSeq:NP_001238874.1}, sgc1b1 GN {ECO:0000313|EMBL:CCD30519.1, ECO:0000313|RefSeq:NP_001238874.1}, GN si:ch73-34b5.3 {ECO:0000313|RefSeq:NP_001238874.1}; 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|EMBL:CCD30519.1}; RN [1] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=18335061; RA Sreenivasan R., Cai M., Bartfai R., Wang X., Christoffels A., Orban L.; RT "Transcriptomic analyses reveal novel genes with sexually dimorphic RT expression in the zebrafish gonad and brain."; RL PLoS ONE 3:e1791-e1791(2008). RN [2] {ECO:0000313|Ensembl:ENSDARP00000105472} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105472}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {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 [4] {ECO:0000313|Ensembl:ENSDARP00000105472, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000105472}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; 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., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA 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). RN [5] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=25147559; RA Freeman J.L., Weber G.J., Peterson S.M., Nie L.H.; RT "Embryonic ionizing radiation exposure results in expression alterations of RT genes associated with cardiovascular and neurological development, RT function, and disease and modified cardiovascular function in zebrafish."; RL Front. Genet. 5:268-268(2014). RN [6] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=24396069; RA Ge L., Zhang R.P., Wan F., Guo D.Y., Wang P., Xiang L.X., Shao J.Z.; RT "TET2 plays an essential role in erythropoiesis by regulating lineage- RT specific genes via DNA oxidative demethylation in a zebrafish model."; RL Mol. Cell. Biol. 34:989-1002(2014). RN [7] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=26108469; RA Saraiva L.R., Ahuja G., Ivandic I., Syed A.S., Marioni J.C., RA Korsching S.I., Logan D.W.; RT "Molecular and neuronal homology between the olfactory systems of zebrafish RT and mouse."; RL Sci. Rep. 5:11487-11487(2015). RN [8] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [9] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [10] {ECO:0000313|RefSeq:NP_001238874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RX PubMed=29627575; RA Li J., Zhou W., Wang Y., Niu C.; RT "The dual role of cGMP in oocyte maturation of zebrafish."; RL Biochem. Biophys. Res. Commun. 499:998-1003(2018). RN [11] {ECO:0000313|RefSeq:NP_001238874.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001238874.1}; RG RefSeq; RL Submitted (FEB-2024) to UniProtKB. CC -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the CC biosynthesis of the signaling molecule cGMP. CC {ECO:0000256|ARBA:ARBA00037442}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; 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_001251945.2. DR STRING; 7955.ENSDARP00000105472; -. DR PaxDb; 7955-ENSDARP00000105472; -. DR Ensembl; ENSDART00000129471.3; ENSDARP00000105472.2; ENSDARG00000086790.3. DR GeneID; 100150304; -. DR KEGG; dre:100150304; -. DR AGR; ZFIN:ZDB-GENE-090313-160; -. DR CTD; 2983; -. DR ZFIN; ZDB-GENE-090313-160; gucy1b1. DR eggNOG; KOG4171; Eukaryota. DR HOGENOM; CLU_011614_4_0_1; -. DR OMA; PCEDHAK; -. DR OrthoDB; 2898719at2759; -. DR TreeFam; TF351403; -. DR Reactome; R-DRE-445355; Smooth Muscle Contraction. DR Proteomes; UP000000437; Alternate scaffold 1. DR Proteomes; UP000000437; Chromosome 1. DR Bgee; ENSDARG00000086790; Expressed in swim bladder and 13 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:0006182; P:cGMP biosynthetic process; IBA:GO_Central. 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:SF2; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1; 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}; 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 //