GCYA2_RAT
ID GCYA2_RAT Reviewed; 730 AA.
AC Q9WVI4; Q54A43;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Guanylate cyclase soluble subunit alpha-2;
DE Short=GCS-alpha-2;
DE EC=4.6.1.2 {ECO:0000305|PubMed:11121588};
GN Name=Gucy1a2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP FUNCTION.
RC STRAIN=Wistar Kyoto; TISSUE=Aorta;
RX PubMed=11121588; DOI=10.1016/s0167-4781(00)00211-6;
RA Koglin M., Behrends S.;
RT "Cloning and functional expression of the rat alpha(2) subunit of soluble
RT guanylyl cyclase.";
RL Biochim. Biophys. Acta 1494:286-289(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yao Y., Yamamoto T., Suzuki N.;
RT "Rat soluble guanylate cyclase alpha 2 subunit.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has guanylyl cyclase on binding to the beta-1 subunit.
CC {ECO:0000305|PubMed:11121588}.
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:0000305|PubMed:11121588};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000305|PubMed:11121588};
CC -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions. {ECO:0000250,
CC ECO:0000269|PubMed:11121588}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9WVI4; P31016: Dlg4; NbExp=7; IntAct=EBI-7665590, EBI-375655;
CC Q9WVI4; Q62108: Dlg4; Xeno; NbExp=3; IntAct=EBI-7665590, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AF109963; AAD42949.2; -; mRNA.
DR EMBL; AB096080; BAC24017.1; -; mRNA.
DR RefSeq; NP_076446.1; NM_023956.1.
DR AlphaFoldDB; Q9WVI4; -.
DR SMR; Q9WVI4; -.
DR IntAct; Q9WVI4; 5.
DR MINT; Q9WVI4; -.
DR STRING; 10116.ENSRNOP00000040361; -.
DR iPTMnet; Q9WVI4; -.
DR PhosphoSitePlus; Q9WVI4; -.
DR PaxDb; Q9WVI4; -.
DR PRIDE; Q9WVI4; -.
DR DNASU; 66012; -.
DR GeneID; 66012; -.
DR KEGG; rno:66012; -.
DR UCSC; RGD:621655; rat.
DR CTD; 2977; -.
DR RGD; 621655; Gucy1a2.
DR VEuPathDB; HostDB:ENSRNOG00000029876; -.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_5_0_1; -.
DR InParanoid; Q9WVI4; -.
DR OMA; SLMLHYF; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q9WVI4; -.
DR PRO; PR:Q9WVI4; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000029876; Expressed in testis and 15 other tissues.
DR Genevisible; Q9WVI4; RN.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IEA:Ensembl.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; ISO:RGD.
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 1: Evidence at protein level;
KW cGMP biosynthesis; Cytoplasm; GTP-binding; Lyase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..730
FT /note="Guanylate cyclase soluble subunit alpha-2"
FT /id="PRO_0000074114"
FT DOMAIN 519..646
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 81787 MW; B8D790BFF81FB8F9 CRC64;
MSRRKISSES FSSLGSDYLE TSPEEEGECP LSKLCWNGSR SPPGPPGSRA AAMAATPVPA
ASVAAAAAAV AAGSKRAQRR RRVNLDSLGE SISLLTAPSP QTIHMTLKRT LQYYEHQVIG
YRDAEKNFHN ISNRCSSADH SNKEEIEDVS GILRCTANVL GLKFQEIQER FGEEFFKICF
DENERVLRAV GSTLQDFFNG FDALLEHIRT SFGKQATLES PSFLCKELPE GTLKLHYFHP
HHTVGFAMLG MIKAAGKRIY HLNVEVEQIE NEKFCSDGST PSNYSCLTFL IKECETTQIT
KNIPQGTSQI PTDLRISINT FCRTFPFHLM FDPNMVVLQL GEGLRKQLRC DNHKVLKFED
CFEIVSPKVN ATFDRVLLRL STPFVIRTKP EASGTDNEDK VMEIKGQMIH VPESNAILFL
GSPCVDKLDE LIGRGLHLSD IPIHDATRDV ILVGEQAKAQ DGLKKRMDKL KATLEKTHQA
LEEEKKKTVD LLYSIFPGDV AQQLWQRQQV QARKFDDVTM LFSDIVGFTA ICAQCTPMQV
ISMLNELYTR FDHQCGFLDI YKVETIGDAY CVASGLHRKS LCHAKPIALM ALKMMELSEE
VLTPDGRPIQ MRIGIHSGSV LAGVVGVRMP RYCLFGNNVT LASKFESGSH PRRINISPTT
YQLLKREDSF TFIPRSREEL PDNFPKEIPG VCYFLELRTG PKPPKPSLSS SRIKKVSYNI
GTMFLRETSL
