ID   F8VQK3_MOUSE            Unreviewed;       730 AA.
AC   F8VQK3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 88.
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:ENSMUSP00000111398.2,
GN   ECO:0000313|MGI:MGI:2660877};
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 {ECO:0000313|Ensembl:ENSMUSP00000111398.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000111398.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111398.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000111398.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111398.2};
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}.
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   RefSeq; NP_001028494.1; NM_001033322.2.
DR   AlphaFoldDB; F8VQK3; -.
DR   SMR; F8VQK3; -.
DR   IntAct; F8VQK3; 1.
DR   MINT; F8VQK3; -.
DR   STRING; 10090.ENSMUSP00000111398; -.
DR   GlyGen; F8VQK3; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; F8VQK3; -.
DR   PhosphoSitePlus; F8VQK3; -.
DR   SwissPalm; F8VQK3; -.
DR   MaxQB; F8VQK3; -.
DR   PaxDb; 10090-ENSMUSP00000111398; -.
DR   PeptideAtlas; F8VQK3; -.
DR   ProteomicsDB; 371483; -.
DR   Antibodypedia; 4028; 141 antibodies from 18 providers.
DR   DNASU; 234889; -.
DR   Ensembl; ENSMUST00000115733.3; ENSMUSP00000111398.2; ENSMUSG00000041624.11.
DR   GeneID; 234889; -.
DR   KEGG; mmu:234889; -.
DR   UCSC; uc009obc.2; mouse.
DR   AGR; MGI:2660877; -.
DR   CTD; 2977; -.
DR   MGI; MGI:2660877; Gucy1a2.
DR   VEuPathDB; HostDB:ENSMUSG00000041624; -.
DR   eggNOG; KOG4171; Eukaryota.
DR   GeneTree; ENSGT00940000157765; -.
DR   HOGENOM; CLU_011614_5_0_1; -.
DR   InParanoid; F8VQK3; -.
DR   OMA; SLMLHYF; -.
DR   OrthoDB; 2898719at2759; -.
DR   PhylomeDB; F8VQK3; -.
DR   TreeFam; TF351403; -.
DR   Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR   BioGRID-ORCS; 234889; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Gucy1a2; mouse.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; F8VQK3; Protein.
DR   Bgee; ENSMUSG00000041624; Expressed in embryonic post-anal tail and 46 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; ISO:MGI.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0007263; P:nitric oxide mediated signal transduction; IMP:MGI.
DR   GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IMP:MGI.
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.
DR   Genevisible; F8VQK3; MM.
PE   1: Evidence at protein 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   Proteomics identification {ECO:0007829|MaxQB:F8VQK3,
KW   ECO:0007829|PeptideAtlas:F8VQK3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          519..646
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          460..491
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  81831 MW;  C3907834F882505C CRC64;
     MSRRKISSES FSSLSSDYLE TSPEEEGECP LSRLCWNGSR SPPGPPGSRE AAKAATSAPA
     ASAAAASAAV AAEYKRAQRR GRVNLDSLGE SISLLTAPLP QTIHMTLKRT LQYYEHQVIG
     YRDAEKNFHN ISKRCSYADH SNKEEIEDVS GILQCTANVL GLQFQEIQER FGEEFFKICF
     DENERVLRAV GSTLQDFFNG FDALLEHIRT SFGKQATLES SSFLCKELPE GTLMLHYFHP
     HHTVGFAMLG MIKAAGKRIY HLNVEVEQIE NEKLCFDGSN PSNCSCLTFL IKECETTQIT
     KDNPQGTSQV PADLRISINT FCRAFPFHLM FDSNMVVLQL GEGLRKQLRY DTHRALKFED
     CFEIVSPMIN ATFDRVLLRL STPFVIRTKP EASGTENEDK VMEIKGQMIH VPESSAILFL
     GSPCVDKLDE LMGRGLHLSD IPIHDATRDV ILVGEQAKAQ DGLKKRMDKL KATLERTHQA
     LEEEKKKTVD LLYSIFPGDV AQQLWQGQQV QARKFDDVTM LFSDIVGFTA ICAQCTPMQV
     ISMLNELYTR FDHQCGLLDI YKVETIGDAY CVASGLHRKS LCHAKPIALM ALKMMELSEE
     VLTPDGKAIQ MRIGIHSGSV LAGVVGVRMP RYCLFGNNVT LASKFESGSH PRRINVSPTT
     YQLLKREDSF TFIPRSREEL PDNFPKEIPG VCYFLELRTD PKPPKPSLSS SRIKKVSYNI
     GTMFLRETSL
//