GCY35_CAEEL
ID GCY35_CAEEL Reviewed; 688 AA.
AC O02298;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Soluble guanylate cyclase gcy-35;
DE EC=4.6.1.2;
GN Name=gcy-35; ORFNames=T04D3.4;
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], FUNCTION, ACTIVITY REGULATION, AND TISSUE
RP 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, TISSUE SPECIFICITY, HETERODIMERIZATION, AND MUTAGENESIS OF
RP ASP-473 AND ASN-546.
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).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=29879119; DOI=10.1371/journal.pgen.1007435;
RA McLachlan I.G., Beets I., de Bono M., Heiman M.G.;
RT "A neuronal MAP kinase constrains growth of a Caenorhabditis elegans
RT sensory dendrite throughout the life of the organism.";
RL PLoS Genet. 14:E1007435-E1007435(2018).
CC -!- FUNCTION: Plays a central role in social feeding behavior and oxygen
CC sensation by synthesizing 3',5'-cyclic guanosine monophosphate (cGMP)
CC from GTP. Oxygen, which binds to its heme-binding sites, probably
CC regulates social behavior by modulating its activity. cGMP is a common
CC second 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 ECO:0000269|PubMed:15220933}.
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).
CC {ECO:0000269|PubMed:15220933}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with gcy-36, and possibly with
CC other soluble guanylate cyclases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection,
CC dendrite {ECO:0000269|PubMed:29879119}. Note=Enriched localization at
CC the URX dendrite ending. {ECO:0000269|PubMed:29879119}.
CC -!- TISSUE SPECIFICITY: Expressed in URX, AQR and PQR neurons. Also
CC expressed in ALN, SDQ and BDU neurons, and variably in AVM, PLM and PLN
CC neurons, pharyngeal and body wall muscles, and the excretory cell.
CC {ECO:0000269|PubMed:15203005, 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; AY652944; AAT73711.1; -; mRNA.
DR EMBL; Z81114; CAB03288.2; -; Genomic_DNA.
DR PIR; T24458; T24458.
DR RefSeq; NP_001252131.1; NM_001265202.1.
DR AlphaFoldDB; O02298; -.
DR SMR; O02298; -.
DR BioGRID; 38597; 2.
DR STRING; 6239.T04D3.4a; -.
DR PaxDb; O02298; -.
DR PRIDE; O02298; -.
DR EnsemblMetazoa; T04D3.4a.1; T04D3.4a.1; WBGene00001555.
DR GeneID; 173202; -.
DR KEGG; cel:CELE_T04D3.4; -.
DR UCSC; T04D3.4; c. elegans.
DR CTD; 173202; -.
DR WormBase; T04D3.4a; CE34497; WBGene00001555; gcy-35.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_4_0_1; -.
DR InParanoid; O02298; -.
DR OMA; TEMNAPS; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; O02298; -.
DR PRO; PR:O02298; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001555; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O02298; baseline and differential.
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:0070025; F:carbon monoxide binding; IDA:WormBase.
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:0070026; F:nitric oxide binding; IDA:WormBase.
DR GO; GO:0019825; F:oxygen binding; IDA:WormBase.
DR GO; GO:0019826; F:oxygen sensor activity; IMP:WormBase.
DR GO; GO:0009454; P:aerotaxis; IMP:WormBase.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0019934; P:cGMP-mediated signaling; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:WormBase.
DR GO; GO:0055093; P:response to hyperoxia; IMP: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; Cell projection; cGMP biosynthesis; Coiled coil; Cytoplasm;
KW GTP-binding; Heme; Iron; Lyase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..688
FT /note="Soluble guanylate cyclase gcy-35"
FT /id="PRO_0000074126"
FT DOMAIN 424..552
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 644..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..401
FT /evidence="ECO:0000255"
FT COMPBIAS 644..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000305"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 473
FT /note="D->A: Loss of function, suggesting that it acts as
FT an alpha-like subunit."
FT /evidence="ECO:0000269|PubMed:15203005"
FT MUTAGEN 546
FT /note="N->A: Little or no effect, suggesting that it acts
FT as an alpha-like subunit."
FT /evidence="ECO:0000269|PubMed:15203005"
SQ SEQUENCE 688 AA; 78403 MW; 5431C9B5F935C8D9 CRC64;
MFGWIHESFR QLVTRKYGKD IWEKIVHMSK FELGTESEIA HYYNDDETLR LVNSMANVIG
IPIEEIWEAY GGFLIQFTME TGWDELLRAM APDLEGFLDS LDSLHYFIDH VVYKTKLRGP
SFRCDVQADG TLLLHYYSKR SGLYPIVKGV VREVARRIYD TEVVMKVQER KQEHLDAFVT
EHVVFVITQI ENANSTQPKS ISSKADSQID LSTGIYEISS SDFSLAFPYH ICFDPDLFVE
HFGNFIKKTF PNAMRQETRV TDLLELVHPE VPFSYESIKY YKNSLFVFRL KGLGDIVHNA
NDEAKTVLLK GSMVFIDEGK YILYMCSVNV TTVRELIERN LHLSDMQRHD GTRDVIMLNQ
SRMSQVELNR TLEETTKKLK KMAQELEIEK QKTDELLCEL MPASVADSLR SGKAMDAKEF
ADCTLLFTDI VTFTNICAMC TPYDVVTLLN DLYLRFDRLV GLHDAYKVET IGDAYMIVGG
VPERCENHAE RVLNISIGML MESKLVLSPI THKPIKIRLG VHCGPVVAGV VGIKMPRYCL
FGDTVNVANK MESNGIQCKI HVSETGKLNG LKANPSYVFI DRGNTEIRGK GMMYTYFLER
NDRKSVWELC SRPRSGEQTI DGYMELHDQS IYQEEGGQQE NLTVENGNSA QNNHNNNNNT
HHSGRKLMNG SSVDPGSHHI RSPTCTIS
