ID   GCYB1_MOUSE             Reviewed;         620 AA.
AC   O54865;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Guanylate cyclase soluble subunit beta-1;
DE            Short=GCS-beta-1;
DE            EC=4.6.1.2 {ECO:0000250|UniProtKB:Q02153};
DE   AltName: Full=Guanylate cyclase soluble subunit beta-3;
DE            Short=GCS-beta-3;
DE   AltName: Full=Soluble guanylate cyclase small subunit;
GN   Name=Gucy1b1; Synonyms=Gucy1b3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RA   Gansemans Y., Brouckaert P., Fiers W.;
RT   "Murine soluble guanylate cyclase, beta-1 subunit.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/10;
RX   PubMed=10984516; DOI=10.1073/pnas.190331697;
RA   Sharina I.G., Krumenacker J.S., Martin E., Murad F.;
RT   "Genomic organization of alpha 1 and beta 1 subunits of the mammalian
RT   soluble guanylyl cyclase genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10878-10883(2000).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC       biosynthesis of the signaling molecule cGMP.
CC       {ECO:0000250|UniProtKB:P16068}.
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:0000250|UniProtKB:Q02153};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P16068};
CC       Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for
CC       responding to nitric oxide, but not for catalytic activity.
CC       {ECO:0000250|UniProtKB:P16068};
CC   -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC       magnesium or manganese ions. {ECO:0000250|UniProtKB:Q02153}.
CC   -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC       beta subunit. Heterodimer with GUCY1A1. Can also form inactive
CC       homodimers in vitro. {ECO:0000250|UniProtKB:Q02153}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
CC   -!- MISCELLANEOUS: There are two types of guanylate cyclases: soluble forms
CC       and membrane-associated receptor forms.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; AF020339; AAB94876.1; -; mRNA.
DR   EMBL; AF297083; AAG17447.1; -; mRNA.
DR   CCDS; CCDS38460.1; -.
DR   RefSeq; NP_059497.1; NM_017469.4.
DR   AlphaFoldDB; O54865; -.
DR   SMR; O54865; -.
DR   BioGRID; 207595; 13.
DR   IntAct; O54865; 2.
DR   MINT; O54865; -.
DR   STRING; 10090.ENSMUSP00000029635; -.
DR   iPTMnet; O54865; -.
DR   PhosphoSitePlus; O54865; -.
DR   SwissPalm; O54865; -.
DR   MaxQB; O54865; -.
DR   PaxDb; 10090-ENSMUSP00000029635; -.
DR   PeptideAtlas; O54865; -.
DR   ProteomicsDB; 273034; -.
DR   Antibodypedia; 4395; 332 antibodies from 36 providers.
DR   DNASU; 54195; -.
DR   Ensembl; ENSMUST00000029635.14; ENSMUSP00000029635.9; ENSMUSG00000028005.14.
DR   GeneID; 54195; -.
DR   KEGG; mmu:54195; -.
DR   UCSC; uc008por.2; mouse.
DR   AGR; MGI:1860604; -.
DR   CTD; 2983; -.
DR   MGI; MGI:1860604; Gucy1b1.
DR   VEuPathDB; HostDB:ENSMUSG00000028005; -.
DR   eggNOG; KOG4171; Eukaryota.
DR   GeneTree; ENSGT00940000157483; -.
DR   HOGENOM; CLU_011614_4_0_1; -.
DR   InParanoid; O54865; -.
DR   OMA; PCEDHAK; -.
DR   OrthoDB; 2898719at2759; -.
DR   PhylomeDB; O54865; -.
DR   TreeFam; TF351403; -.
DR   Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR   BioGRID-ORCS; 54195; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Gucy1b1; mouse.
DR   PRO; PR:O54865; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; O54865; Protein.
DR   Bgee; ENSMUSG00000028005; Expressed in olfactory tubercle and 258 other cell types or tissues.
DR   ExpressionAtlas; O54865; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0008074; C:guanylate cyclase complex, soluble; ISS:UniProtKB.
DR   GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR   GO; GO:0098831; C:presynaptic active zone cytoplasmic component; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:Ensembl.
DR   GO; GO:0047805; F:cytidylate cyclase activity; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR   GO; GO:0043167; F:ion binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IMP:SynGO.
DR   GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR   GO; GO:0099555; P:trans-synaptic signaling by nitric oxide, modulating synaptic transmission; IMP:SynGO.
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.
DR   Genevisible; O54865; MM.
PE   1: Evidence at protein level;
KW   cGMP biosynthesis; Cytoplasm; GTP-binding; Heme; Iron; Lyase;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Guanylate cyclase soluble subunit beta-1"
FT                   /id="PRO_0000074117"
FT   DOMAIN          421..554
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         105
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P16068"
SQ   SEQUENCE   620 AA;  70598 MW;  EED89ABF539F4EF9 CRC64;
     MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN
     LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN LDALHDHLAT IYPGMRAPSF
     RCTDAEKGKG LILHYYSERE GLQDIVIGII KTVAQQIHGT EIDMKVIQQR NEECDHTQFL
     IEEKESKEED FYEDLDRFEE NGTQESRISP YTFCKAFPFH IIFDRNLVVT QCGNAIYRVL
     PQLQPGNCSL LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL ECEDELTGAE
     ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR DLVLLGEQFR
     EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP SVANELRHKR PVPAKRYDNV
     TILFSGIVGF NAFCSKHASG EGAMKIVNLL NDLYTRFDTL TDSRKNPFVY KVETVGDKYM
     TVSGLPEPCI HHARSICHLA LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY
     CLFGNTVNLT SRTETTGEKG KINVSEYTYR CLMSPENSDP LFHLEHRGPV SMKGKKEPMQ
     VWFLSRKNTG TEETNEEDEN
//