GCY36_CAEEL
ID GCY36_CAEEL Reviewed; 675 AA.
AC Q6DNF4; Q9XTE0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Soluble guanylate cyclase gcy-36;
DE EC=4.6.1.2;
GN Name=gcy-36; ORFNames=C46E1.2;
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, HETERODIMERIZATION, AND MUTAGENESIS OF ASP-499; ASN-572 AND
RP CYS-672.
RX PubMed=15203005; DOI=10.1016/j.cub.2004.06.027;
RA Cheung B.H.H., Arellano-Carbajal F., Rybicki I., de Bono M.;
RT "Soluble guanylate cyclases act in neurons exposed to the body fluid to
RT promote C. elegans aggregation behavior.";
RL Curr. Biol. 14:1105-1111(2004).
CC -!- FUNCTION: Plays a central role in social feeding behavior by
CC synthesizing 3',5'-cyclic guanosine monophosphate (cGMP) from GTP.
CC Oxygen, which probably binds to its heme-binding sites, may regulate
CC social behavior by modulating its activity. cGMP is a common second
CC messenger in sensory transduction and is implicated in oxygen
CC sensation. Indeed, C.elegans exhibits a strong behavioral preference
CC for 5-12% oxygen, avoiding higher and lower oxygen levels; a higher
CC level of oxygen inducing a naturally polymorphic social feeding
CC behavior. Involved in avoidance of hyperoxia and for oxygen-induced
CC aggregation and bordering, probably by mediating oxygen sensing in URX,
CC AQR and PQR sensory neurons. {ECO:0000269|PubMed:15203005}.
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:0000305};
CC Note=Binds 1 or 2 heme groups per heterodimer. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Regulated by molecular oxygen, which binds to the
CC heme binding site. Probably not activated by nitric oxide (NO) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with gcy-35, and possibly with
CC other soluble guanylate cyclases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in 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; AY652945; AAT73712.1; -; mRNA.
DR EMBL; AL008867; CAD56232.2; -; Genomic_DNA.
DR EMBL; Z99942; CAD56232.2; JOINED; Genomic_DNA.
DR PIR; T19968; T19968.
DR RefSeq; NP_510557.3; NM_078156.5.
DR AlphaFoldDB; Q6DNF4; -.
DR SMR; Q6DNF4; -.
DR STRING; 6239.C46E1.2; -.
DR PaxDb; Q6DNF4; -.
DR PeptideAtlas; Q6DNF4; -.
DR EnsemblMetazoa; C46E1.2.1; C46E1.2.1; WBGene00001556.
DR GeneID; 191657; -.
DR KEGG; cel:CELE_C46E1.2; -.
DR UCSC; C46E1.2; c. elegans.
DR CTD; 191657; -.
DR WormBase; C46E1.2; CE39007; WBGene00001556; gcy-36.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00970000196348; -.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; Q6DNF4; -.
DR OMA; VYPERLW; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q6DNF4; -.
DR PRO; PR:Q6DNF4; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001556; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; ISS:WormBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019826; F:oxygen sensor activity; IMP:WormBase.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007631; P:feeding behavior; IGI:WormBase.
DR GO; GO:0070482; P:response to oxygen levels; IMP:WormBase.
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 1: Evidence at protein level;
KW Behavior; cGMP biosynthesis; Coiled coil; Cytoplasm; GTP-binding; Heme;
KW Iron; Lyase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..675
FT /note="Soluble guanylate cyclase gcy-36"
FT /id="PRO_0000074127"
FT DOMAIN 450..578
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 384..427
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 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 499
FT /note="D->A: Little or no effect, suggesting that it acts
FT as an beta-like subunit."
FT /evidence="ECO:0000269|PubMed:15203005"
FT MUTAGEN 572
FT /note="N->A: Loss of function, suggesting that it acts as
FT an beta-like subunit."
FT /evidence="ECO:0000269|PubMed:15203005"
FT MUTAGEN 672
FT /note="C->S: Reduced activity."
FT /evidence="ECO:0000269|PubMed:15203005"
SQ SEQUENCE 675 AA; 76651 MW; F11AE2A0C9A3950A CRC64;
MFGFIHESIR QLMIRTYGEA FWSKVLERAG FEAGKENIIN HYYSDADTFS LVDAVSVILK
VTREQVWEMY GCFLIQYTME TGWDDLIRSM SPNLKGFLDN LDSLHYFIDH VVYKANLRGP
SFRCEDNPDG TITLHYYTGR PGLYPIVKGV LREAAKRVFK LDVSMTITGR TQRSVQMATG
ERIEEHVIFL VKTLNTDQSN EEALGTAVVQ HSNNYKIRLT HMDFISTFPY HMVVDQDCKI
VQVGRELYNH IPKDLLSVGT PLMRIFEVTR PQIPLDFDSI CNFINAVFVL QVKTTPMEFQ
RNANKRAAQA IEASENLYED NNGALALSQS QHLKLKGQMM LMSSGGHIMY LCSPYVTSIP
ELLQYGLRLT AMPIHDPTRD LILLNQQRLS DVEMNLQLEA NNEQLENMAK DLEVEKGKTD
ALLREMLPPS VAQQLKQGLS VEAREYEEAT VMFTDVPTFQ QIVPLCTPKD IVHLLNELFT
KFDRLIGIQK AYKVETVGDS YMSVGGIPDL VDDHCEVICH LALGMVMEAR TVCDPITNTP
LHIRAGIHSG PVVAGVVGAK MPRYCLFGDT VNTSSRMESH SPIGRIHCSE NAKKCAESTG
RFEFEPRGRV QIKGKGEMNT YFLLRSFKRS IWEIIDRRRD ENCNSIDGYN ELREGYVDDV
LNKVTQKNSK TCSIS
