GCY9_CAEEL
ID GCY9_CAEEL Reviewed; 1081 AA.
AC E7EAU8; Q23496;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Receptor-type guanylate cyclase gcy-9 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-9 {ECO:0000312|WormBase:ZK455.2};
GN ORFNames=ZK455.2 {ECO:0000312|WormBase:ZK455.2};
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:ADV03673.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:ADV03673.1};
RX PubMed=21173231; DOI=10.1073/pnas.1017354108;
RA Hallem E.A., Spencer W.C., McWhirter R.D., Zeller G., Henz S.R., Ratsch G.,
RA Miller D.M., Horvitz H.R., Sternberg P.W., Ringstad N.;
RT "Receptor-type guanylate cyclase is required for carbon dioxide sensation
RT by Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:254-259(2011).
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).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=24240097; DOI=10.1074/jbc.m113.517367;
RA Smith E.S., Martinez-Velazquez L., Ringstad N.;
RT "A chemoreceptor that detects molecular carbon dioxide.";
RL J. Biol. Chem. 288:37071-37081(2013).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). Involved in the sensing of CO2 levels
CC and acidity by the BAG neurons. May act as a direct receptor for CO2
CC and H+ (PubMed:21173231, PubMed:24240097).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:21173231,
CC ECO:0000269|PubMed:24240097}.
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:21173231}. Note=Localizes in cilium of sensory
CC neurons. {ECO:0000269|PubMed:21173231}.
CC -!- TISSUE SPECIFICITY: Expressed in BAG sensory neurons.
CC {ECO:0000269|PubMed:21173231}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA91488.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HQ636455; ADV03673.1; -; mRNA.
DR EMBL; BX284606; CAA91488.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_509897.3; NM_077496.3.
DR AlphaFoldDB; E7EAU8; -.
DR SMR; E7EAU8; -.
DR STRING; 6239.ZK455.2; -.
DR PaxDb; E7EAU8; -.
DR EnsemblMetazoa; ZK455.2.1; ZK455.2.1; WBGene00001536.
DR GeneID; 191645; -.
DR KEGG; cel:CELE_ZK455.2; -.
DR CTD; 191645; -.
DR WormBase; ZK455.2; CE50244; WBGene00001536; gcy-9.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR OMA; SCIEACW; -.
DR OrthoDB; 112993at2759; -.
DR PRO; PR:E7EAU8; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001536; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
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:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0071468; P:cellular response to acidic pH; IMP:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0003031; P:detection of carbon dioxide; IMP:UniProtKB.
DR GO; GO:0050907; P:detection of chemical stimulus involved in sensory perception; IMP:UniProtKB.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:1904457; P:positive regulation of neuronal action potential; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 SMART; SM00220; S_TKc; 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 ATP-binding; Cell membrane; Cell projection; cGMP biosynthesis;
KW Coiled coil; Glycoprotein; GTP-binding; Lyase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1081
FT /note="Receptor-type guanylate cyclase gcy-9"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433278"
FT TOPO_DOM 22..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..1081
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 520..826
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 898..1028
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 834..874
FT /evidence="ECO:0000255"
FT BINDING 526..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 903
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 903
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 904
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 947
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 947
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1081 AA; 121791 MW; 644F46E91B19A2C7 CRC64;
MRLYLFFISS LLLAESRRSI SKISHDEINQ HVKTTLSSEG IVRIGHLHPT NPIIAHEPDV
LKMCADDLKM RNILPQNYTL TVFTMESCNK YSGVEHAAFL HYLKNASVYF GPGCNNEMLV
IGRLAPRWNV PIIAHMSGDD ALSDRVQFPT LGSVALTSAS EMAKATVTYL NLNNWDQIGI
VRPSVGYERL SVYSLQHQIK KRDINLNVIL DIEPFSSPEE IISTGKLTTL KSMARIIVVE
LGMDIHSVTN FMLAIHRSEI KNEEFVFVIP WLAHQNDHYP WEAANVDKQE VKLAFENTII
ITAHGYDKKF FDDFQMKFSA VTGVLANHYA TLSYMSLYDA LFLYGLALRD AFEDGGGYNV
HMNGSLIWSR MTNRQFIGMT GQVLMNNKAI RVPSYATYHA INGTLKIVVE LEAKNNDRGQ
CEKNEEMCSE HVAHETIQYY WPSDSGKLPP AVPKCGFTGA ECDYRPYFIG ASLLAFILTV
GPLSYFIYLK QKERLLYDMT WRIPRESIKM LEGKSKSEHS LASKSQSSGS FSGSMNSKQN
GLIAAKQAVS NGVKLAIKRY QQVRNITFPK SELRLLKELK ICENDNLNKF YGISFNQQNE
FIVMWVLCSR GSLEDILFND ELKLGRNFQV SFAKDVVKGL NFLHTSPLLH HGMLCLQNCL
VDSNWTVKLT NFATEAVIFE KLDHNELRPF INTDSESADD VSDPTKDFAR KKYLQQAPEI
IREIVTTKTI PEGSQSADIY ALGMVLYQIL FRVEPFHERN KSINKLMETL AMANDDDQLI
RPTFPSSNTG EGYNLQLLSC IEACWLEIPE MRPPIKKVRT MVNANLKSTG KGSLVDQMMK
MMEEYTANLE NMVRDRTALL EEAQKQADRL LNSMLPKSIA EDLKIGKPVL PQLYSCATVL
FSDIRGFTRI SSTSTPLQVV TFLNDMFSGF DAIIAKHDAY KVETIGDAYM IVSGVPTENG
NSHAQNIADV ALKMRAFICN FKLAHRPEEL MMVRIGFHSG PVAAGVVGLA APRYCLFGDT
VNTASRMEST GVANKIQISE GAYNLLHCFF PQFQMVERGK IEVKGKGECL TYYLEGRTGK
Q
