GCY34_CAEEL
ID GCY34_CAEEL Reviewed; 686 AA.
AC P92006;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Soluble guanylate cyclase gcy-34;
DE EC=4.6.1.2;
GN Name=gcy-34; ORFNames=M04G12.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15220933; DOI=10.1038/nature02714;
RA Gray J.M., Karow D.S., Lu H., Chang A.J., Chang J.S., Ellis R.E.,
RA Marletta M.A., Bargmann C.I.;
RT "Oxygen sensation and social feeding mediated by a C. elegans guanylate
RT cyclase homologue.";
RL Nature 430:317-322(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=23874221; DOI=10.1371/journal.pgen.1003619;
RA Krzyzanowski M.C., Brueggemann C., Ezak M.J., Wood J.F., Michaels K.L.,
RA Jackson C.A., Juang B.T., Collins K.D., Yu M.C., L'etoile N.D.,
RA Ferkey D.M.;
RT "The C. elegans cGMP-dependent protein kinase EGL-4 regulates nociceptive
RT behavioral sensitivity.";
RL PLoS Genet. 9:E1003619-E1003619(2013).
CC -!- FUNCTION: Synthesizes cyclic GMP (cGMP) from GTP (By similarity). May
CC be involved in sensitivity to quinine by regulating egl-4 activity
CC through the production of cGMP (PubMed:23874221).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:23874221}.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 or 2 heme groups per heterodimer. {ECO:0000250};
CC -!- ACTIVITY REGULATION: May be regulated by molecular oxygen. Probably not
CC activated by nitric oxide (NO) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with other soluble guanylate cyclases.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in a small number of neurons,
CC corresponding to URX, AQR and PQR neurons.
CC {ECO:0000269|PubMed:15220933}.
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; AY652943; AAT73710.1; -; mRNA.
DR EMBL; Z81103; CAB03210.1; -; Genomic_DNA.
DR PIR; T23721; T23721.
DR RefSeq; NP_506319.1; NM_073918.5.
DR AlphaFoldDB; P92006; -.
DR SMR; P92006; -.
DR STRING; 6239.M04G12.3; -.
DR PaxDb; P92006; -.
DR EnsemblMetazoa; M04G12.3.1; M04G12.3.1; WBGene00001554.
DR GeneID; 191656; -.
DR KEGG; cel:CELE_M04G12.3; -.
DR UCSC; M04G12.3; c. elegans.
DR CTD; 191656; -.
DR WormBase; M04G12.3; CE12426; WBGene00001554; gcy-34.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00970000196348; -.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; P92006; -.
DR OMA; YEATVMF; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; P92006; -.
DR PRO; PR:P92006; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001554; Expressed in pharyngeal muscle cell (C elegans) and 2 other 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; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR GO; GO:0050913; P:sensory perception of bitter taste; IMP:UniProtKB.
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; Coiled coil; Cytoplasm; GTP-binding; Heme; Iron; Lyase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..686
FT /note="Soluble guanylate cyclase gcy-34"
FT /id="PRO_0000074125"
FT DOMAIN 455..583
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 306..335
FT /evidence="ECO:0000255"
FT COILED 398..432
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 686 AA; 78588 MW; 65AE352DB53CBA57 CRC64;
MFGFIHESIR QLVIRKYGED VWLQVLERSG FENGKENIVN HYYSDTDTYV LVDSVSIVLK
VTKDQIWEMY GGFLITYSME IGWDELVRSM SPNLKGFLDN LDSLHYFIDH VVYKANLRGP
SFRCEENPDG TLMLHYFTGR PGLYHIVKGV VKEVAKLVFN LDISLVVQGR TQRSVHMNNG
ERVEEHVIFL IKNVEEPRRD SDTSTTSALT SVEPDFGEII DDNLKVSLQD FSRALPYHFV
LDESCRLVQC GDELYNHIPN ELLQPGTPIL RIFEINRPQI PLDFENICNF INAVFVLQVK
TSPLRKKHMN AMTKEEREQE VEAMEEEVES NELTQGCHLK LKGQMMMLST KKHIIYLCSP
YVTSINELMQ FGMRLTAMPL HDATRDLILL NQQRLSDVEV NLQLEANNEQ LETMTHELEV
ERQKTDSILK DMLPRKIAKQ LLSGEHLEPC EYEATVMFCD LPAFQQIIPV CQPKNIVKLL
NEVFFKLDRI VVLRGVYKVE TVSDSYMTVS GIPDYTSEHA ENMCHVALGM MWEARSVMDP
VNKTPFLLRI GLHSGTIIAG VVGTKMPRYC LFGETVTLAS QMESLGVAGK IQCSSWTYSK
AMETGRFEFS PRGRINVKGR GDVETYFLMR SLKKSIWEIT DHERDVNVNS IEGYEELEIF
IENAQTVKHD GHPKANQNHS ATCTIA
