ID   GCC1_ARATH              Reviewed;         274 AA.
AC   Q8L870; Q8LFJ7; Q9FI93;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Guanylyl cyclase 1 {ECO:0000303|PubMed:12482758};
DE            Short=AtGC1 {ECO:0000303|PubMed:12482758};
DE            EC=4.6.1.2 {ECO:0000269|PubMed:12482758};
GN   Name=GC1 {ECO:0000303|PubMed:12482758};
GN   OrderedLocusNames=At5g05930 {ECO:0000312|Araport:AT5G05930};
GN   ORFNames=K18J17.8 {ECO:0000312|EMBL:BAB10798.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY,
RP   AND COFACTOR.
RX   PubMed=12482758; DOI=10.1074/jbc.m210983200;
RA   Ludidi N., Gehring C.;
RT   "Identification of a novel protein with guanylyl cyclase activity in
RT   Arabidopsis thaliana.";
RL   J. Biol. Chem. 278:6490-6494(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Magnesium-dependent guanylyl cyclase that catalyzes the
CC       formation of guanosine 3',5'-cyclic monophosphate (cGMP) from guanosine
CC       5'-triphosphate (GTP) (PubMed:12482758). Can also use ATP as substrate
CC       with a low activity (PubMed:12482758). {ECO:0000269|PubMed:12482758}.
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:0000269|PubMed:12482758};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:12482758};
CC   -!- PATHWAY: Nucleotide metabolism. {ECO:0000269|PubMed:12482758}.
CC   -!- SUBUNIT: Functions both as monomer and homooligomer.
CC       {ECO:0000269|PubMed:12482758}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY118140; AAM51559.1; -; mRNA.
DR   EMBL; AB017060; BAB10798.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90941.1; -; Genomic_DNA.
DR   EMBL; BT024499; ABD19680.1; -; mRNA.
DR   EMBL; AK229272; BAF01136.1; -; mRNA.
DR   EMBL; AY084807; AAM61373.1; -; mRNA.
DR   RefSeq; NP_568159.1; NM_120675.5.
DR   AlphaFoldDB; Q8L870; -.
DR   STRING; 3702.AT5G05930.1; -.
DR   PaxDb; Q8L870; -.
DR   EnsemblPlants; AT5G05930.1; AT5G05930.1; AT5G05930.
DR   GeneID; 830478; -.
DR   Gramene; AT5G05930.1; AT5G05930.1; AT5G05930.
DR   KEGG; ath:AT5G05930; -.
DR   Araport; AT5G05930; -.
DR   TAIR; locus:2153674; AT5G05930.
DR   eggNOG; KOG4621; Eukaryota.
DR   HOGENOM; CLU_064395_1_0_1; -.
DR   OMA; KRYAGHY; -.
DR   OrthoDB; 1348354at2759; -.
DR   PhylomeDB; Q8L870; -.
DR   PRO; PR:Q8L870; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L870; baseline and differential.
DR   GO; GO:0004383; F:guanylate cyclase activity; IDA:UniProtKB.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR018616; GUCD1.
DR   PANTHER; PTHR31400; PTHR31400; 1.
DR   Pfam; PF09778; Guanylate_cyc_2; 1.
PE   1: Evidence at protein level;
KW   cGMP biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Guanylyl cyclase 1"
FT                   /id="PRO_0000447483"
SQ   SEQUENCE   274 AA;  30914 MW;  2EBDB5A1783918CE CRC64;
     MWPLCFLLNK LLRVEERNQG ILDGNGDSTF PKYCLFDDPL VSDGKYRDAG LPSSSHMDVP
     HVHQLASWDC GLACVLMVLR ASGIASCTLE DLAEICSTNS IWTVDLAYLL QKFCVEFSYY
     TITFGANPNY SIEEFYKEQL PEDLVRVDLL FRKAHESGII IQCRSVSIHE ISCLLLSGNY
     IAIALVDQDK LSKSWLEEVL VSGLHSSNSC YTGHYVVICG YDAVRDEFEI RDPASSKIHE
     RISSKCLENA RKSFGTDEDL LLINLENMRN QNGY