GCY37_CAEEL
ID GCY37_CAEEL Reviewed; 708 AA.
AC Q6DNF3; O44468; Q65CM4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Soluble guanylate cyclase gcy-37;
DE EC=4.6.1.2;
GN Name=gcy-37; ORFNames=C54E4.3;
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).
CC -!- FUNCTION: Synthesizes cyclic GMP (cGMP) from GTP (By similarity). May
CC play a role in sensory neurons. {ECO:0000250}.
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; AY652946; AAT73713.1; -; mRNA.
DR EMBL; FO080949; CCD68037.1; -; Genomic_DNA.
DR PIR; F88642; F88642.
DR RefSeq; NP_500171.2; NM_067770.3.
DR AlphaFoldDB; Q6DNF3; -.
DR SMR; Q6DNF3; -.
DR STRING; 6239.C54E4.3; -.
DR PaxDb; Q6DNF3; -.
DR EnsemblMetazoa; C54E4.3.1; C54E4.3.1; WBGene00001557.
DR GeneID; 191658; -.
DR KEGG; cel:CELE_C54E4.3; -.
DR UCSC; C54E4.3; c. elegans.
DR CTD; 191658; -.
DR WormBase; C54E4.3; CE37494; WBGene00001557; gcy-37.
DR eggNOG; KOG1573; Eukaryota.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; Q6DNF3; -.
DR OMA; MPMHDAT; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q6DNF3; -.
DR PRO; PR:Q6DNF3; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001557; Expressed in pharyngeal muscle cell (C elegans) and 3 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: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; Coiled coil; Cytoplasm; GTP-binding; Heme; Iron; Lyase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..708
FT /note="Soluble guanylate cyclase gcy-37"
FT /id="PRO_0000074128"
FT DOMAIN 434..562
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 368..409
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 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 708 AA; 81104 MW; 34CBFD592F48B715 CRC64;
MIGWTHVCVS ALILRKYGPE VLEEILRKAG YQEDIKFDIQ CYYDDTETMR IFRVAATVLG
LSVDDMWEMY GEFLITHACE TGWQKMLFCM ANNLQEFLDN LNSMHYFIDQ IAFKSEMKGP
TFQCEPFGES GLKLHYFSFR QGLFPIVKGL VRKTARTLFE MDVKVCMLER NQERRKSGMV
EHVIFSVEPD DNHRKGKRLF HKFRNTKTTE NAPSFTLSST ILVGLRDFKN IFPYHVCFNK
QMIIEHIGIY LLREYGLENK KTLKVSDLMQ LVQPSDIQLT YKNVLSYLNT LFIFQLKHHS
KRNEVQEGSS EAFQQPLVLK GEMMPINDGN SIIFICSPHV TTVRDILNLK LYISDMPMHD
ATRDLVMLNQ SRICQMELNK KLEETMKKMK KMTEELEVKK SQTDRLLFEF VPPVIAEALR
AAKTVPAQEF SDCSVIFTDI PDFFTISVNC SPTEIITVVT DLFHRFDRII EKHKGYKVLS
LMDSYLIVGG VPNANQYHCE DSLNLALGLL FEAKQVVVPK LERSVRLRIG VHCGPVVAGI
VSQQKPRFCV LGNTVNVTKS ICSHSSPGKV LVSNAVRTMV TKHLKSIFVF NANGYLELQS
GKVLTHFLEK NEKCSVWDIV DRDKATNDSI DGYRELHSDN GTEEWQEATV AAYRVISVVD
ALENKQSRTR KALTRLRSVK RKFRTIQSND SGVSVSEPNV ESAVCSIM
