ID GCY6_CAEEL Reviewed; 1086 AA.
AC N1NVB7; Q9XVV4;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Receptor-type guanylate cyclase gcy-6 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-6 {ECO:0000312|WormBase:B0024.6b};
GN ORFNames=B0024.6 {ECO:0000312|WormBase:B0024.6b};
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|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 [2] {ECO:0000305}
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 [3] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=16099833; DOI=10.1073/pnas.0505530102;
RA Johnston R.J. Jr., Chang S., Etchberger J.F., Ortiz C.O., Hobert O.;
RT "MicroRNAs acting in a double-negative feedback loop to control a neuronal
RT cell fate decision.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12449-12454(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=19523832; DOI=10.1016/j.cub.2009.05.043;
RA Ortiz C.O., Faumont S., Takayama J., Ahmed H.K., Goldsmith A.D., Pocock R.,
RA McCormick K.E., Kunimoto H., Iino Y., Lockery S., Hobert O.;
RT "Lateralized gustatory behavior of C. elegans is controlled by specific
RT receptor-type guanylyl cyclases.";
RL Curr. Biol. 19:996-1004(2009).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). Regulates chemotaxis responses toward
CC the salt ion Mg(2+) and to a lesser extent toward Cl(1-) in ASE left
CC (ASEL) sensory neuron (PubMed:19523832). {ECO:0000250|UniProtKB:Q19187,
CC ECO:0000269|PubMed:19523832}.
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:B0024.6a};
CC IsoId=N1NVB7-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:B0024.6b};
CC IsoId=N1NVB7-2; Sequence=VSP_057699;
CC -!- TISSUE SPECIFICITY: Expressed in both ASEL and ASER neurons throughout
CC late embryonic and early larval stages. In adults, expressed
CC asymmetrically in ASE left (ASEL) sensory neuron.
CC {ECO:0000269|PubMed:16099833, ECO:0000269|PubMed:9096403}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284605; CAA94879.4; -; Genomic_DNA.
DR EMBL; BX284605; CCW45984.1; -; Genomic_DNA.
DR RefSeq; NP_001294696.1; NM_001307767.1. [N1NVB7-1]
DR RefSeq; NP_505650.3; NM_073249.3. [N1NVB7-2]
DR AlphaFoldDB; N1NVB7; -.
DR SMR; N1NVB7; -.
DR STRING; 6239.B0024.6b.1; -.
DR GlyCosmos; N1NVB7; 4 sites, No reported glycans.
DR EPD; N1NVB7; -.
DR PaxDb; 6239-B0024-6b; -.
DR EnsemblMetazoa; B0024.6a.1; B0024.6a.1; WBGene00001533. [N1NVB7-2]
DR EnsemblMetazoa; B0024.6b.1; B0024.6b.1; WBGene00001533. [N1NVB7-1]
DR GeneID; 191644; -.
DR KEGG; cel:CELE_B0024.6; -.
DR AGR; WB:WBGene00001533; -.
DR WormBase; B0024.6a; CE47853; WBGene00001533; gcy-6. [N1NVB7-2]
DR WormBase; B0024.6b; CE46160; WBGene00001533; gcy-6. [N1NVB7-1]
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; N1NVB7; -.
DR OMA; GFLHCDV; -.
DR OrthoDB; 2877804at2759; -.
DR PRO; PR:N1NVB7; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; 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: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:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0010035; P:response to inorganic substance; IMP:UniProtKB.
DR GO; GO:0032026; P:response to magnesium ion; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IMP:UniProtKB.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06352; PBP1_NPR_GC-like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011645; HNOB_dom_associated.
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 PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR PANTHER; PTHR11920:SF76; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-6; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07701; HNOBA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Alternative splicing; ATP-binding; Cell membrane; cGMP biosynthesis;
KW Chemotaxis; Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1086
FT /note="Receptor-type guanylate cyclase gcy-6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433275"
FT TOPO_DOM 22..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..1086
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 560..836
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 894..1024
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 566..574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 37..40
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057699"
SQ SEQUENCE 1086 AA; 122390 MW; B9C28158733BD1CF CRC64;
MIGVYLRSVI FPLLFVIQTI CQPPGNVFHL GFLHCDVLEN NVEGSTTYIN YRTSASAASI
AIDKIKREGL LLGYDFKFTI LYDQCDENIA AGNAIKLFAE HNVDVLFGPT TNNAAMPVFI
LATYYNIPLI TWGITSSATL DDESRFPTAG MLSIGSRSLA VTFREVMKEY GWDQFVFAYS
LEMNDEKCET LRDDFQNMVA YYGDIVLSYA VQIMDHSEEG LLAILKDVST RGRIIVPCFH
EGNSRGLHRR WMLVAARNGF VNDEYVYIFP SLRSRGYAVP QADGTFRYPW TEATGPQPGD
QEALLGFQKS IFIVDMQGQG NVGSNYTQFE HEIIQRMKEP PYNCTDACAS PEYQTAATYA
GQLHDSVYIY GVVMDQIMKT VPNQYKNGTA FPRKMAGVFN GVGGTVAIDE GGGLQPTLFV
LTLDSNNNSS LIMTVDVDQQ EAVVTKHYTN EATALWSHRK GIRPPDQPIC GYTGSLCPAN
VFFQYIGWFI AAIIIIFFTI MGAILAFIYL CHAKQQEVER QNALWQIPFK SMMTVTKKGK
GEHSMRSISS VPSTISSTRS STLSEVGETR NYLFFQIQND VEMERVAAKK HSIRMVFDNK
TCATMRQMRL IDHANLNKFI GMSLDAPQLY SVWRFCSRGS LADVIRKASM QMDGFFIYSL
MKDIINGLTW IHESSHEFHG MLTSKNCLLN DRWQLKITDF GLRIFRTHDQ YNKSDRLWTS
PELLRTDDIL GSREGDIYSF GIISAELITR SSVFDLENRK EDAEEIIYML KKGGLQSPRP
SLEHDESIEI NPALLHLVRD CWTERPSERP DIKQVASQLR SMNTNRNDNL MDHVFNVLES
YASTLEDEVA ERMKELVEEK KKSDVLLYRM LPRQVADKLK LGQTVEPETF DIVTLFFSDV
VSFTTLAGKC TPLQVVNLLN GLYTIFDGII EQHDVYKVET IGDGYFVASG VPRRNGNEHT
RNIASMSINF VKSLADFSIP HLPGEKIKIR VGFHCGSVVA GVVGLTMPRY CLFGDAVNTA
SRMESNSKPG QIHLSEEANQ MLMRLGGFTT EPRGEVIIKG KGVMATYWLL KMDESAAPKI
LKKKQD
//
