GCY23_CAEEL
ID GCY23_CAEEL Reviewed; 1073 AA.
AC G5EEE9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Receptor-type guanylate cyclase gcy-23 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-23 {ECO:0000312|WormBase:T26C12.4};
GN ORFNames=T26C12.4 {ECO:0000312|WormBase:T26C12.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAE78830.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16415369; DOI=10.1534/genetics.105.050013;
RA Inada H., Ito H., Satterlee J., Sengupta P., Matsumoto K., Mori I.;
RT "Identification of guanylyl cyclases that function in thermosensory neurons
RT of Caenorhabditis elegans.";
RL Genetics 172:2239-2252(2006).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). Regulates thermotaxis responses in AFD
CC sensory neurons. May regulate AFD neuronal activity such as calcium
CC responses to temperature gradients (PubMed:16415369).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:16415369}.
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 Evidence={ECO:0000250|UniProtKB:Q19187};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell projection, cilium
CC {ECO:0000269|PubMed:16415369}. Note=Localizes exclusively to the
CC sensory ending, known as cilium, in AFD neurons.
CC {ECO:0000269|PubMed:16415369}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in AFD sensory neurons.
CC {ECO:0000269|PubMed:16415369}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AB201390; BAE78830.1; -; mRNA.
DR EMBL; FO081749; CCD74008.1; -; Genomic_DNA.
DR RefSeq; NP_500309.3; NM_067908.4.
DR AlphaFoldDB; G5EEE9; -.
DR SMR; G5EEE9; -.
DR STRING; 6239.T26C12.4; -.
DR EPD; G5EEE9; -.
DR PaxDb; G5EEE9; -.
DR PRIDE; G5EEE9; -.
DR EnsemblMetazoa; T26C12.4.1; T26C12.4.1; WBGene00001548.
DR GeneID; 191652; -.
DR KEGG; cel:CELE_T26C12.4; -.
DR CTD; 191652; -.
DR WormBase; T26C12.4; CE41702; WBGene00001548; gcy-23.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; G5EEE9; -.
DR OMA; INKHSAY; -.
DR OrthoDB; 90908at2759; -.
DR PhylomeDB; G5EEE9; -.
DR PRO; PR:G5EEE9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001548; Expressed in anatomical system and 4 other tissues.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044306; C:neuron projection terminus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; ISS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016048; P:detection of temperature stimulus; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0040040; P:thermosensory behavior; IMP:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IMP:UniProtKB.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; cGMP biosynthesis; Coiled coil;
KW Glycoprotein; GTP-binding; Lyase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1073
FT /note="Receptor-type guanylate cyclase gcy-23"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433292"
FT TOPO_DOM 16..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..1073
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 508..808
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 878..1008
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 813..844
FT /evidence="ECO:0000255"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 927
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 927
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1073 AA; 121128 MW; 8B7DD98D84D3A46C CRC64;
MRRELFIFLL LLGECANVKV KVGHIGAVGS MRNAEKILQL SKEQLTQEGV LGNDFDIEIL
NQMGCGESYE GVAVGADMYH VQGVRAFIGP YCNAELDAVA KMATFWNIPV VGYMASSNSF
ADKTIFKTLA RVSLRTTNSL AEAAAALIKH YGWNKVAIAT NTGAVAFERV QSFEEVFHQR
GINVVRKIML EEYTNAKAIM NSGLLQELEN SARVVVCAFS STRDMNKEFM QAVTLSGMNN
ANYAWILPWL QLETKDMAPW LGENGEYQQN VKDHFANSFI IDDVNGFDNT LVTPFKERLE
ASGYSTDDLE MKNIYGYIHL YDALRLYALA VRATMNETGN ENSYLNGKEV WNHMRRITFP
GLVSNAGVTS GTVMMDDIAE RAPVYAAFYV PPNSDTVRKV CELEPVMLTN CDGTKTGNGC
YELQVTDLST GFWPSIDGSL PADEPACGFR NEKCDYTTLI IGGCIVLLII LLIICFFILS
RVCENRALAN TPWRIYRDDF RTIQENEMKS MLSIGSSKTK MSNMSMFVKH HAVVGTNTHA
SFHLYPQRRP IVFNRQDLQL LNQMKQAVHD NLNPFLGMSF NEKEEMVVLW KFCSRGTIQD
MIYNQEVSLD SKFHGAFIRD ITLGLEYLHS SIIGYHGSLT PWSCLIDRNW MIKLTDYGIA
NPLERWEKLG LISTETLKEG DDKSGSAQKT SLLYQPPEML KNKESNRTRR MDQSWVKQSQ
ARRQMGDIYA FGMVMHEILF RALPFPNGTN VSEVMDYIRD GTKTFRPTVH DRTQIHPDLV
ALLLDCWNEN PEVRPSIRRV RLNTENYLKV KGSLVDQMMR MMEQYANNLE KLVAERTGML
EEANVRADKL LGQLLPKYVA NELKMGRSVP AKTFDMATVM FSDIVGFTTI CSSSTPLEVV
SMLNSIYSKF DDAINKHGSY KVETIGDAYM IVSGIPEENG NEHIRNICNT ALELMLLLKT
YEIPHRRNVK LRIRLGIHTG TVAAGVVGLT APRYCLFGDT VNVASRMEST SEPEKIQMSQ
EARDFCVRYY SEFQITLRGT VEAKGKGPVT SYWLLGKQSE SQMQQQNFSQ LGI
