GCY33_CAEEL
ID GCY33_CAEEL Reviewed; 945 AA.
AC P90895; Q18791; Q86C59;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 4.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Soluble guanylate cyclase gcy-33;
DE EC=4.6.1.2;
GN Name=gcy-33; ORFNames=F57F5.2;
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].
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].
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 FUNCTION.
RX PubMed=23874221; DOI=10.1371/journal.pgen.1003619;
RA Krzyzanowski M.C., Brueggemann C., Ezak M.J., Wood J.F., Michaels K.L.,
RA Jackson C.A., Juang B.T., Collins K.D., Yu M.C., L'etoile N.D.,
RA Ferkey D.M.;
RT "The C. elegans cGMP-dependent protein kinase EGL-4 regulates nociceptive
RT behavioral sensitivity.";
RL PLoS Genet. 9:E1003619-E1003619(2013).
CC -!- FUNCTION: Synthesizes cyclic GMP (cGMP) from GTP (By similarity). May
CC be involved in sensitivity to quinine by regulating egl-4 activity
CC through the production of cGMP (PubMed:23874221).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:23874221}.
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 BAG sensory neuron.
CC {ECO:0000269|PubMed:9096403}.
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; AY275181; AAP32289.1; -; mRNA.
DR EMBL; Z75953; CAB00103.2; -; Genomic_DNA.
DR EMBL; Z78012; CAB00103.2; JOINED; Genomic_DNA.
DR PIR; T20156; T20156.
DR RefSeq; NP_001256391.1; NM_001269462.1.
DR AlphaFoldDB; P90895; -.
DR SMR; P90895; -.
DR STRING; 6239.F57F5.2c; -.
DR EPD; P90895; -.
DR PaxDb; P90895; -.
DR EnsemblMetazoa; F57F5.2a.1; F57F5.2a.1; WBGene00001553.
DR GeneID; 179644; -.
DR KEGG; cel:CELE_F57F5.2; -.
DR UCSC; F57F5.2; c. elegans.
DR CTD; 179644; -.
DR WormBase; F57F5.2a; CE34891; WBGene00001553; gcy-33.
DR eggNOG; KOG4171; Eukaryota.
DR HOGENOM; CLU_011614_4_1_1; -.
DR InParanoid; P90895; -.
DR PhylomeDB; P90895; -.
DR PRO; PR:P90895; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001553; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; P90895; baseline and differential.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
DR GO; GO:0070027; F:carbon monoxide sensor activity; 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:0019826; F:oxygen sensor activity; IDA:WormBase.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
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 GO; GO:0050913; P:sensory perception of bitter taste; IMP:UniProtKB.
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 Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..945
FT /note="Soluble guanylate cyclase gcy-33"
FT /id="PRO_0000074124"
FT DOMAIN 437..567
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 639..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 388..413
FT /evidence="ECO:0000255"
FT COILED 763..802
FT /evidence="ECO:0000255"
FT COMPBIAS 639..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..930
FT /note="Basic and acidic 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"
SQ SEQUENCE 945 AA; 106829 MW; 91910EB89BF63BF2 CRC64;
MYGLVIEGVR FMIQENWGPQ VLLQVQKLTS LSEKSVSTHD QYSEHVVPQM FKAIHEITGT
PYEQIGVLAG RFFVQFLIRN GYGDLMNVMG RRFSDFIKGL DNIHEYFRFS YPKLRAPSFY
CKSESEDGLI LHYRSRRTGY LSYVIGQLVE LARVFYQLDI GIQVLKKKEK GRFTFVVLKI
SFDNVGLGQD LKLKERVKNL NEYLPVDTKS FLQMFPFHIA FNKKLEILMA GQGLLNLMPN
IQGLLMTDVF DLQRPCIKFT AEGIMVHQNC VFQIESLHPV VKQTEENITV QINDITEDKV
SLEKKTVMDN EYESLPYVTL RGPITVLKSS ETFLLLATCV VDTLDTMFKM GLYLNDFGES
DCNREIIMAT IQKSDTLKTM LENEKRRSEV LTEMTREISE AKKTARTLLT QMMPYEVAQT
MMRSGSVDHC EAFECVSIGF IRVCDFSKIS LFIEAFEVVN LLNTIYSHLD SIVDTHGVYK
VETIGESYMI SAGCPYRDDY DAEMVSDCCL EMVSHIKSFE YQSHDAVKKV LIKCGIFTGP
VVGGVVGVRT PRYCLFGDTV NTASRMESSN QTPMTIQIGQ RTKDRVEKQA SGAFRIKPKG
NVFVKGKGDM RVYEIEKKKG RARYKKSDPL RKKMVAEKKE AEELLDEDNE GHRSSALSRM
SLGESIDSSS SRRGSLSGSQ LELNKTIAQT IELTSKASAA LDLNMQDENN RPPTWSASHS
QDIRKPRKTE SKITLNSRLS SSDLAVSRVE TSKDSDGETP RPTSSELKEV NRIREEALAQ
EKEEERTTKE ENQKIEEVGE DHVSEATSLL DSEVSHGDNN ISFSQMPSDS IPHEDRTSLP
SATPSEIGDA ISKKKLEKED SNSSMSSLDE RTTVSAKPTT TRRLLNQKDL EKEKKRSSMA
GSSVTSSSAH SHSIRSKKDT RDKSRCKCED IRADNKLKTK VCSIM
