GCY32_CAEEL
ID GCY32_CAEEL Reviewed; 684 AA.
AC Q6DNF7; Q17707; Q9BI80;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Soluble guanylate cyclase gcy-32;
DE EC=4.6.1.2;
GN Name=gcy-32; ORFNames=C06B3.8;
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].
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 [MRNA].
RA Hudson M.L.;
RT "Soluble guanylate cyclases in Caenorhabditis elegans.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=9096403; DOI=10.1073/pnas.94.7.3384;
RA Yu S., Avery L., Baude E., Garbers D.L.;
RT "Guanylyl cyclase expression in specific sensory neurons: a new family of
RT chemosensory receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3384-3387(1997).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15916947; DOI=10.1016/j.cub.2005.04.017;
RA Cheung B.H., Cohen M., Rogers C., Albayram O., de Bono M.;
RT "Experience-dependent modulation of C. elegans behavior by ambient
RT oxygen.";
RL Curr. Biol. 15:905-917(2005).
CC -!- FUNCTION: Synthesizes cyclic GMP (cGMP) from GTP (By similarity).
CC Influences aerotaxis responses, aggregation and bordering behaviors
CC (gathering around the edge of a bacterial lawn) in combination with
CC other soluble guanylate cyclases. {ECO:0000250,
CC ECO:0000269|PubMed:15916947}.
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:9096403}.
CC -!- DISRUPTION PHENOTYPE: No response to varying levels of oxygen.
CC Significantly reduced aggregation and bordering behaviors.
CC {ECO:0000269|PubMed:15916947}.
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; AY652942; AAT73709.1; -; mRNA.
DR EMBL; AJ133597; CAC35530.1; -; mRNA.
DR EMBL; Z77652; CAB01118.3; -; Genomic_DNA.
DR PIR; T18984; T18984.
DR RefSeq; NP_506452.5; NM_074051.5.
DR AlphaFoldDB; Q6DNF7; -.
DR SMR; Q6DNF7; -.
DR STRING; 6239.C06B3.8; -.
DR PaxDb; Q6DNF7; -.
DR EnsemblMetazoa; C06B3.8.1; C06B3.8.1; WBGene00001552.
DR GeneID; 179887; -.
DR KEGG; cel:CELE_C06B3.8; -.
DR UCSC; C06B3.8.1; c. elegans.
DR CTD; 179887; -.
DR WormBase; C06B3.8; CE44168; WBGene00001552; gcy-32.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; Q6DNF7; -.
DR OMA; FRCEANS; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q6DNF7; -.
DR PRO; PR:Q6DNF7; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001552; Expressed in larva 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: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..684
FT /note="Soluble guanylate cyclase gcy-32"
FT /id="PRO_0000074123"
FT DOMAIN 454..582
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 396..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 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 353
FT /note="I -> V (in Ref. 2; CAC35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="K -> R (in Ref. 2; CAC35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="Q -> H (in Ref. 2; CAC35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="N -> S (in Ref. 2; CAC35530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 77879 MW; 29F8FC8A945DDD77 CRC64;
MFGFIHESIR QLVIRNYGED TWTQVLERSG FESGKENIMN HYYSDTDTYV LVDSVSLVLK
VTKDQVWEMY GGFLITYSME IGWDELVRSM SPNLKGFLDN LDSLHYFIDH VVYKANLRGP
SFRCEETPDG TLLLHYFTGR PGLYHIVKGV VKEVAKRVFD LDITLVVQGR TQRSVHMNNG
ERVEEHVVFL INNLSEPRRD SEGSEVSLLT STNANFPTIV DDTLGISLDD FSKALPYHFV
IDESCKLVQC GSELHNHIPN ELLQPGTPIL RIFEINRPQI PLDFENICNF INAVFVLQVK
TSPLKKKHMD AMSQEELKQE METLDEDATN ELTQGHHLKL KGQMMLLASK KHIIYLCSPY
VTSINELMQY GMRLTAMPLH DATRDLILLN QQRLSDVEVN LQLEANNEQL ETMTRELELE
RQKTDSILKD MLPRRIAQQL LSGEHIEACE HEATVMFCDL PAFQQAIPQC SPKDIVNMLN
EIFRKLDRIV VIRGVYKVET VSDSYMAVSG IPDYTPEHAE NMCHVALGMM WEARSVIDPV
SKTPFLLRIG IHSGTITAGV VGTVHPKYCL FGETVTLASQ MESLGMAGKI QCSKWAYQKA
METGRFEFSP RGRIDVKQRG LTETYFLTRS LKKSIWEIID HDRDINVNSI EGYEELETAI
ENAVTIKSAL PRPDQRNSAA CSIS
