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   01-SEP-2009, entry version 42.
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; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; 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
RT   guanylate cyclase homologue.";
RL   Nature 430:317-322(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Synthesizes cyclic GMP (cGMP) from GTP (By similarity).
CC       May play a role in sensory neurons.
CC   -!- CATALYTIC ACTIVITY: GTP = 3',5'-cyclic GMP + diphosphate.
CC   -!- COFACTOR: Binds 1 or 2 heme groups per heterodimer (By
CC       similarity).
CC   -!- ENZYME REGULATION: May be regulated by molecular oxygen. Probably
CC       not activated by nitric oxide (NO) (By similarity).
CC   -!- SUBUNIT: Heterodimer; with other soluble guanylate cyclases (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in a small number of neurons,
CC       corresponding to URX, AQR and PQR neurons.
CC   -!- MISCELLANEOUS: There are two types of guanylate cyclases: soluble
CC       forms and membrane-associated receptor forms.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 1 guanylate cyclase domain.
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DR   EMBL; AY652946; AAT73713.1; -; mRNA.
DR   EMBL; AF038609; AAU87824.1; -; Genomic_DNA.
DR   PIR; F88642; F88642.
DR   RefSeq; NP_500171.2; -.
DR   UniGene; Cel.25261; -.
DR   HSSP; P26769; 1AZS.
DR   Ensembl; C54E4.3; C54E4.3; C54E4.3; Caenorhabditis elegans.
DR   GeneID; 191658; -.
DR   KEGG; cel:C54E4.3; -.
DR   UCSC; C54E4.3; c. elegans.
DR   CTD; 191658; -.
DR   WormBase; WBGene00001557; gcy-37.
DR   WormPep; C54E4.3; CE37494.
DR   OMA; Q6DNF3; IAFKSEM.
DR   BRENDA; 4.6.1.2; 672.
DR   NextBio; 949860; -.
DR   ArrayExpress; Q6DNF3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0007242; P:intracellular signaling cascade; IEA:InterPro.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR011644; Haem_NO-bd.
DR   InterPro; IPR011645; Haem_no_assoc_bd.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 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; Complete proteome; Cytoplasm;
KW   GTP-binding; Heme; Iron; Lyase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN         1    708       Soluble guanylate cyclase gcy-37.
FT                                /FTId=PRO_0000074128.
FT   DOMAIN      434    562       Guanylate cyclase.
FT   COILED      368    409       Potential.
FT   METAL       105    105       Iron (heme proximal ligand) (By
FT                                similarity).
FT   METAL       439    439       Magnesium (By similarity).
FT   METAL       483    483       Magnesium (By similarity).
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
//