GCY18_CAEEL
ID GCY18_CAEEL Reviewed; 1113 AA.
AC G5EFQ0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Receptor-type guanylate cyclase gcy-18 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-18 {ECO:0000312|WormBase:ZK896.8};
GN ORFNames=ZK896.8 {ECO:0000312|WormBase:ZK896.8};
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:BAE78829.1}
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; AB201389; BAE78829.1; -; mRNA.
DR EMBL; Z82288; CAB05325.2; -; Genomic_DNA.
DR RefSeq; NP_502449.2; NM_070048.4.
DR AlphaFoldDB; G5EFQ0; -.
DR SMR; G5EFQ0; -.
DR STRING; 6239.ZK896.8; -.
DR PaxDb; G5EFQ0; -.
DR PeptideAtlas; G5EFQ0; -.
DR PRIDE; G5EFQ0; -.
DR EnsemblMetazoa; ZK896.8.1; ZK896.8.1; WBGene00001543.
DR GeneID; 178237; -.
DR KEGG; cel:CELE_ZK896.8; -.
DR CTD; 178237; -.
DR WormBase; ZK896.8; CE42602; WBGene00001543; gcy-18.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; G5EFQ0; -.
DR OMA; GNSPDCH; -.
DR OrthoDB; 90908at2759; -.
DR PhylomeDB; G5EFQ0; -.
DR PRO; PR:G5EFQ0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001543; Expressed in larva and 3 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:0031528; C:microvillus membrane; IDA:WormBase.
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; IGI:UniProtKB.
DR GO; GO:0043052; P:thermotaxis; IGI: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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1113
FT /note="Receptor-type guanylate cyclase gcy-18"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433286"
FT TOPO_DOM 19..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..1113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 543..848
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 918..1048
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 853..884
FT /evidence="ECO:0000255"
FT BINDING 923
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 923
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 924
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 967
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 967
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1113 AA; 125822 MW; C95D77DE676A0F6D CRC64;
MLKTLLFILI FFNIPIIAIE EIPDIKENGE KSSYTQFDNG AKLEVNKEHK RVIKIGHIGA
VGVMPNDARI LNISKENLIE EGLVGDDIEF EIVSRQACSE SFEGVAVAAE LYHVHQVRAF
IGPYCAAELE AVTKMATFWN IPIISYSSVP NAVSDRSVYK TLARVSSKNT NSIAEATVAL
LLHYKWLKVA IATNTGSTAF ERVSIFEEIM HREGVTIVKK VMFDENTDAN EMMNSGQLGD
LAANARIIIC LFSSTKELSK EFMQATYTMR MNNAEYAYII PWLQSGTKDL TPWIGADGEM
LQRVKDHYAN AIIVDDVNGF DDSVVSSFVE KIEKHGMQKS DIDVTNINGY LHLFDSLKLY
ALAIRKVLNE TDNEAYVTNG QFIWNRMRRM KFEGVVSRSS SEENKDAGAI GTVLMDDVAD
RAPIFSAFYI SPNRDKVMKM VNMESELISN CDGLKNKSGC FQLKINDIKS GFWPSEDGSM
PLDEPICGYR GQRCSYLLEI SVGSLIILLI LISVVFFFLF RYCENKQLEK MPWRIFHDDL
QFIDEEQVKS MMSVGSVTTK LSNIQTGQKQ HAIIGVNTHT TYHRYKQRRP IKFIKEDMQL
LTQMKQAVHD NLNPFLGAAF NEKEEMLVLW KFCSRGTIQD IIYNANVVLD EKFHGAFVRD
ITLGLEYLHA SPIGYHGSLT PWCCLIDRNW MVKLSDYGIA NPLERWEKQG AIEIAAAKDS
DDKSQASQAT SIIYMAPELL KNRETNKRRG MDQSWVKQSM LRRQAGDIYS FGMVMYEILF
RSLPFRDNTN ISELVDYLAD GSKTVSPEIQ NQMGLHPDLN ALLRDCWSEN PEIRPSIRRV
RLNTEMVLKT KGSLVDQMMK MMEQYANNLE KLVAERTGML EEANIRADQL LTQLLPAYVA
NELKMGRSVA PKLYSSATIL FSDIVGFTTI CSGSTPLEVV NMLNGLYTGF DECITRNKSY
KVETIGDAYM VVSGIPEENE YNHSRNIANT ALDMRQYLTG YQIPHRPTHR VRCRWGFHTG
SVAAGVVGLT CPRYCLFGDT VNVSSRMEST GTPGMIQMSE EAHMHIRAHH PVFTTTERGE
VQVKGKGTCR TFWLEDRVGD ASTTNYIQNV EGV
