GCY31_CAEEL
ID GCY31_CAEEL Reviewed; 702 AA.
AC Q86C56; Q86C57; Q86C58;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Soluble guanylate cyclase gcy-31;
DE EC=4.6.1.2;
GN Name=gcy-31; ORFNames=T07D1.1;
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] (ISOFORMS A; B AND C), AND ALTERNATIVE SPLICING.
RA Hudson M.L., Karow D.S., Chisholm A.D., Marletta M.A., Morton D.B.;
RT "Soluble guanylyl cyclases in Caenorhabditis elegans.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 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 [4]
RP POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RA Hudson M.L., Karow D.S., Riviere K.H., Marletta M.A., Morton D.B.;
RT "A possible role for gcy-31 in embryogenesis.";
RL (In) Proceedings of the 13th international C. elegans meeting, pp.494-494,
RL Los Angeles (2001).
CC -!- FUNCTION: Synthesizes cyclic GMP (cGMP) from GTP. May play a role in
CC embryogenesis.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b; Synonyms=GCY-31a;
CC IsoId=Q86C56-1; Sequence=Displayed;
CC Name=a; Synonyms=GCY-31c;
CC IsoId=Q86C56-2; Sequence=VSP_011682;
CC Name=c; Synonyms=GCY-31b;
CC IsoId=Q86C56-3; Sequence=VSP_011680, VSP_011681;
CC -!- TISSUE SPECIFICITY: Expressed in a pair of bilaterally symmetric
CC neurons in the head. {ECO:0000269|PubMed:9096403, ECO:0000269|Ref.4}.
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; AY275182; AAP32290.1; -; mRNA.
DR EMBL; AY275183; AAP32291.1; -; mRNA.
DR EMBL; AY275184; AAP32292.1; -; mRNA.
DR EMBL; FO080846; CCD67189.1; -; Genomic_DNA.
DR EMBL; FO080846; CCD67190.1; -; Genomic_DNA.
DR EMBL; FO080846; CCD67191.1; -; Genomic_DNA.
DR RefSeq; NP_001024888.1; NM_001029717.1. [Q86C56-2]
DR RefSeq; NP_001024889.1; NM_001029718.1. [Q86C56-1]
DR RefSeq; NP_001024890.1; NM_001029719.1. [Q86C56-3]
DR AlphaFoldDB; Q86C56; -.
DR SMR; Q86C56; -.
DR BioGRID; 56156; 1.
DR STRING; 6239.T07D1.1b; -.
DR EPD; Q86C56; -.
DR PaxDb; Q86C56; -.
DR EnsemblMetazoa; T07D1.1a.1; T07D1.1a.1; WBGene00001551. [Q86C56-2]
DR EnsemblMetazoa; T07D1.1b.1; T07D1.1b.1; WBGene00001551. [Q86C56-1]
DR EnsemblMetazoa; T07D1.1c.1; T07D1.1c.1; WBGene00001551. [Q86C56-3]
DR GeneID; 191655; -.
DR KEGG; cel:CELE_T07D1.1; -.
DR UCSC; T07D1.1c; c. elegans. [Q86C56-1]
DR CTD; 191655; -.
DR WormBase; T07D1.1a; CE36318; WBGene00001551; gcy-31. [Q86C56-2]
DR WormBase; T07D1.1b; CE36319; WBGene00001551; gcy-31. [Q86C56-1]
DR WormBase; T07D1.1c; CE36320; WBGene00001551; gcy-31. [Q86C56-3]
DR eggNOG; KOG4171; Eukaryota.
DR InParanoid; Q86C56; -.
DR OMA; KDMREPP; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q86C56; -.
DR PRO; PR:Q86C56; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001551; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q86C56; baseline.
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:0070026; F:nitric oxide binding; IBA:GO_Central.
DR GO; GO:0019826; F:oxygen sensor activity; IMP:WormBase.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; cGMP biosynthesis; Coiled coil; Cytoplasm;
KW GTP-binding; Heme; Iron; Lyase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..702
FT /note="Soluble guanylate cyclase gcy-31"
FT /id="PRO_0000074122"
FT DOMAIN 435..564
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 614..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..406
FT /evidence="ECO:0000255"
FT COMPBIAS 641..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
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 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011680"
FT VAR_SEQ 125..133
FT /note="SRTGLTLHY -> MENLPGQRL (in isoform c)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011681"
FT VAR_SEQ 230..337
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_011682"
SQ SEQUENCE 702 AA; 81162 MW; 7FF3D9F1025F3420 CRC64;
MYGLIIDHIA TYIKEKYGES TWSEVKFVSG VTDDTFQMDK KFSEGLSHKL IWACHDVTGD
PVDELMTNIG TSFYKFLTKF EFNKVLRVLG RTFPQFLNGL DNLHEYLRFT FPKLKPPSFY
CEHESRTGLT LHYRSKRRGF LHYVQGQIRN ISQELFQTEV VIELLDIEHD LNLEHVIMRL
HFNNLDFNRQ GTAYRNLNDS ILEKVKITSD IFFDIFPFII VFNRGMRIRN IGIGLLRVMA
GIVGKKINQT FLLMRPFIRF RWEEIMLHSN NIFELISSDP IQEDEDGILV YKTTDVDQMT
EERHRMGDGE REKFLSLKGQ MFYMEEWESI CFVGIPVMSH LPQMYKSGLF INDFALHDSS
RDLVLASTQQ SAELKLLLHQ EAQKSRNMRE NMNRLKKERR RTDKLLYQML PKSVANQLRH
GESAVACCER FDSVTILFTD IVEFTKMCSS LTPLEVIEFL KVIYTNFDKI IDTHGVYKVE
TIGDAYMVVS GAPTKTEHDA EFILDCASQF LVEAGKMVNM NNKIHKIDIR AGVHSGSVVA
GVVGLSMPRY CLFGETVYVA NKMEQNSSPM KILVSETTHN KIEESDPGLY QFERREEIEI
KDDQTIQTFF VVSRHGPHRV PSPRNCESRQ DDSQTEDDDD DELLLPRKSG RKSPTSEAEE
ELKKKGQLSF TPVSDAGIEC HSRNSNKTPR QSQDLTPRKS IT
