GCYA1_RAT
ID GCYA1_RAT Reviewed; 690 AA.
AC P19686;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 153.
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=Guc1a1, Gucy1a3;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=1698769; DOI=10.1016/s0021-9258(17)44837-x;
RA Nakane M., Arai K., Saheki S., Kuno T., Buechler W., Murad F.;
RT "Molecular cloning and expression of cDNAs coding for soluble guanylate
RT cyclase from rat lung.";
RL J. Biol. Chem. 265:16841-16845(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Corpus striatum;
RX PubMed=8997507; DOI=10.1016/s0165-3806(96)00162-9;
RA Smigrodzki R.M., Levitt P.;
RT "The alpha 1 subunit of soluble guanylyl cyclase is expressed prenatally in
RT the rat brain.";
RL Brain Res. Dev. Brain Res. 97:226-234(1996).
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}.
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DR EMBL; M57405; AAA41206.1; -; mRNA.
DR EMBL; U60835; AAB17953.1; -; mRNA.
DR PIR; A38297; OYRTA1.
DR AlphaFoldDB; P19686; -.
DR SMR; P19686; -.
DR IntAct; P19686; 2.
DR STRING; 10116.ENSRNOP00000017190; -.
DR ChEMBL; CHEMBL4105800; -.
DR iPTMnet; P19686; -.
DR jPOST; P19686; -.
DR PaxDb; P19686; -.
DR UCSC; RGD:68436; rat.
DR RGD; 68436; Gucy1a1.
DR eggNOG; KOG4171; Eukaryota.
DR InParanoid; P19686; -.
DR BRENDA; 4.6.1.2; 5301.
DR PRO; PR:P19686; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; ISO:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0043167; F:ion binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0060087; P:relaxation of vascular associated smooth muscle; ISO:RGD.
DR GO; GO:0009635; P:response to herbicide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR GO; GO:0098925; P:retrograde trans-synaptic signaling by nitric oxide, modulating synaptic transmission; ISO:RGD.
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; 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; 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; Direct protein sequencing; GTP-binding;
KW Lyase; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..690
FT /note="Guanylate cyclase soluble subunit alpha-1"
FT /id="PRO_0000074112"
FT DOMAIN 480..607
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERL9"
SQ SEQUENCE 690 AA; 77567 MW; E4819B2CA4F86401 CRC64;
MFCRKFKDLK ITGECPFSLL APGQVPTEPI EEVAGVSESC QATLPTCQEF AENAEGSHPQ
RKTSRNRVYL HTLAESIGKL IFPEFERLNL ALQRTLAKHK IKENRNSSEK EDLERIIAEE
AIAAGVPVEV LKDSLGEELF KICYEEDEHI LGVVGGTLKD FLNSFSTLLK QSSHCQEAER
RGRLEDASIL CLDKDQDFLN VYYFFPKRTT ALLLPGIIKA AARILYESHV EVSLMPPCFR
SECTEFVNQP YLLYSVHVKS TKPSLSPGKP QSSLVIPTSL FCKTFPFHFM LDRDLAILQL
GNGIRRLVNK RDFQGKPNFE EFFEILTPKI NQTFSGIMTM LNMQFVIRVR RWDNLVKKSS
RVMDLKGQMI YIVESSAILF LGSPCVDRLE DFTGRGLYLS DIPIHNALRD VVLIGEQARA
QDGLKKRLGK LKATLEHAHQ ALEEEKKKTV DLLCSIFPSE VAQQLWQGQI VQAKKFNEVT
MLFSDIVGFT AICSQCSPLQ VITMLNALYT RFDQQCGELD VYKVETIGDA YCVAGGLHRE
SDTHAVQIAL MALKMMELSN EVMSPHGEPI KMRIGLHSGS VFAGVVGVKM PRYCLFGNNV
TLANKFESCS VPRKINVSPT TYRLLKDCPG FVFTPRSREE LPPNFPSDIP GICHFLDAYQ
HQGPNSKPWF QQKDAEDGNA NFLGKASGVD
