ID   GCYA1_CANLF             Reviewed;         690 AA.
AC   Q4ZHS0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Guanylate cyclase soluble subunit alpha-1;
DE            Short=GCS-alpha-1;
DE            EC=4.6.1.2 {ECO:0000250|UniProtKB:Q02108};
DE   AltName: Full=Guanylate cyclase soluble subunit alpha-3;
DE            Short=GCS-alpha-3;
DE   AltName: Full=Soluble guanylate cyclase large subunit;
GN   Name=GUCY1A1; Synonyms=GUCY1A3;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16113048; DOI=10.1152/ajplung.00186.2005;
RA   Kwak Y.L., Jones K.A., Warner D.O., Perkins W.J.;
RT   "NO responsiveness in pulmonary artery and airway smooth muscle: the role
RT   of cGMP regulation.";
RL   Am. J. Physiol. 290:L200-L208(2006).
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:Q02108};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q02108};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q02108};
CC       Note=Has also activity with Mn(2+) (in vitro).
CC       {ECO:0000250|UniProtKB:Q02108};
CC   -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC       magnesium or manganese ions. {ECO:0000250|UniProtKB:Q02108}.
CC   -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC       beta subunit. Heterodimer with GUCY1B1. {ECO:0000250|UniProtKB:Q02108}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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}.
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; DQ008575; AAY26556.1; -; mRNA.
DR   RefSeq; NP_001018045.1; NM_001018035.1.
DR   AlphaFoldDB; Q4ZHS0; -.
DR   SMR; Q4ZHS0; -.
DR   STRING; 9615.ENSCAFP00000012533; -.
DR   PaxDb; Q4ZHS0; -.
DR   GeneID; 482663; -.
DR   KEGG; cfa:482663; -.
DR   CTD; 2982; -.
DR   eggNOG; KOG4171; Eukaryota.
DR   InParanoid; Q4ZHS0; -.
DR   Proteomes; UP000002254; Unplaced.
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; 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   cGMP biosynthesis; Cytoplasm; GTP-binding; Lyase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..690
FT                   /note="Guanylate cyclase soluble subunit alpha-1"
FT                   /id="PRO_0000074109"
FT   DOMAIN          481..608
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERL9"
SQ   SEQUENCE   690 AA;  77547 MW;  29ABDE9B8E2B4C21 CRC64;
     MFCTKLKDLK ITGECPLSLL APGQVPKEPG EEVAGTSESG KATLPICQDV PEKNVQRSLP
     QRKTSRSRVY LHTLAESICK LIFPELERLN LALQRTLAKH KIKESRKSLE REDLEKIITD
     QAIAAGVPVE IVKESLGEEL FKICYEEDEH ILGVVGGTLK DFLNSFSTLL KQSSHCQEAE
     KRGRFEDASI LCLDKDHDFL NVYYFFPKRI TSLILPGIIK AAAHILYETE VEVSLLPPCF
     RNDCSEFVNQ PYLLYSLHVK STKPSLSPGK PQSSLVIPAS LFCKTFPFHF MFDKDMTILQ
     FGNGIRRLMN RRDFQGKPHF EEYFEVLTPK INQTFSGIMT MLNMQFVVRV RRWDNSVKKS
     SRVMDLKGQM IYIVESSAIL FLGSPCVDRL EDFTGRGLYL SDIPIHNALR DVVLIGEQAR
     AQDGLKKRLG KLKATLEQAH QALEEEKKKT VDLLCSIFPS EVAQQLWQGQ VVQAKKFSNV
     TMLFSDIVGF TAICSQCSPL QVITMLNALY TRFDQQCGEL DVYKVETIGD AYCVAGGLHK
     ESDTHAAQIA LMALKMMELS DEVMSPHGEP IKMRIGLHSG SVFAGVVGVK MPRYCLFGNN
     VTLANKFESC SIPRKINVSP TTYRLLKDCP GFVFTPRSRE ELPPNFPSEI PGICHFLEAY
     EPATNSKPWF QKKDVEDGNA NFLGKASGID