GCY10_CAEEL
ID GCY10_CAEEL Reviewed; 1067 AA.
AC B1Q257; Q21617; Q9NGZ8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Receptor-type guanylate cyclase gcy-10 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE AltName: Full=Odorant response abnormal protein 1 {ECO:0000312|WormBase:R01E6.1b};
DE Flags: Precursor;
GN Name=odr-1 {ECO:0000312|WormBase:R01E6.1b};
GN Synonyms=gcy-10 {ECO:0000312|WormBase:R01E6.1b};
GN ORFNames=R01E6.1 {ECO:0000312|WormBase:R01E6.1b};
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:AAF68380.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF GLU-904.
RX PubMed=10774726; DOI=10.1016/s0896-6273(00)81061-2;
RA L'Etoile N.D., Bargmann C.I.;
RT "Olfaction and odor discrimination are mediated by the C. elegans guanylyl
RT cyclase ODR-1.";
RL Neuron 25:575-586(2000).
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, AND MUTAGENESIS OF GLY-647.
RX PubMed=8348618; DOI=10.1016/0092-8674(93)80053-h;
RA Bargmann C.I., Hartwieg E., Horvitz H.R.;
RT "Odorant-selective genes and neurons mediate olfaction in C. elegans.";
RL Cell 74:515-527(1993).
RN [4] {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 [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=10571181; DOI=10.1016/s0092-8674(00)81525-1;
RA Troemel E.R., Sagasti A., Bargmann C.I.;
RT "Lateral signaling mediated by axon contact and calcium entry regulates
RT asymmetric odorant receptor expression in C. elegans.";
RL Cell 99:387-398(1999).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=20436480; DOI=10.1038/nn.2540;
RA Liu J., Ward A., Gao J., Dong Y., Nishio N., Inada H., Kang L., Yu Y.,
RA Ma D., Xu T., Mori I., Xie Z., Xu X.Z.;
RT "C. elegans phototransduction requires a G protein-dependent cGMP pathway
RT and a taste receptor homolog.";
RL Nat. Neurosci. 13:715-722(2010).
RN [7]
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).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25009271; DOI=10.1523/jneurosci.0012-14.2014;
RA Harris G., Shen Y., Ha H., Donato A., Wallis S., Zhang X., Zhang Y.;
RT "Dissecting the signaling mechanisms underlying recognition and preference
RT of food odors.";
RL J. Neurosci. 34:9389-9403(2014).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). Regulates chemotaxis responses toward
CC volatile odorants in AWC sensory neurons and their avoidance in AWB
CC sensory neurons (PubMed:8348618, PubMed:10774726). May be involved in
CC sensitivity to quinine by regulating egl-4 activity through the
CC production of cGMP (PubMed:23874221). Involved in phototransduction in
CC ASJ neurons downstream of G protein coupled-photoreceptor lite-1
CC (PubMed:20436480). Required to maintain the expression of putative
CC olfactory receptor str-2 in AWC neurons in adults (PubMed:10571181). In
CC AWB and AWC sensory neurons, mediates the recognition of food oders
CC which subsequently allows for the detection of preferred food sources
CC (PubMed:25009271). {ECO:0000250|UniProtKB:Q19187,
CC ECO:0000269|PubMed:10571181, ECO:0000269|PubMed:10774726,
CC ECO:0000269|PubMed:20436480, ECO:0000269|PubMed:23874221,
CC ECO:0000269|PubMed:25009271, ECO:0000269|PubMed:8348618}.
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:10774726}. Note=Localizes in cilium of sensory
CC neurons. {ECO:0000269|PubMed:10774726}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:R01E6.1b};
CC IsoId=B1Q257-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:R01E6.1a};
CC IsoId=B1Q257-2; Sequence=VSP_057702, VSP_057703, VSP_057704;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in AWC but also in AWB,
CC ASI, ASJ and ASK sensory neurons and in I1 interneuron.
CC {ECO:0000269|PubMed:10774726, ECO:0000269|PubMed:9096403}.
CC -!- DOMAIN: The extracellular domain may not be directly implicated in the
CC detection of volatile odorants. {ECO:0000303|PubMed:10774726}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in AWB and AWC sensory
CC neurons results in a defective preference between different food odors.
CC {ECO:0000269|PubMed:25009271}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; AF235027; AAF68380.1; -; mRNA.
DR EMBL; BX284606; CAA92186.2; -; Genomic_DNA.
DR EMBL; BX284606; CAQ16150.2; -; Genomic_DNA.
DR PIR; T23845; T23845.
DR RefSeq; NP_001123168.2; NM_001129696.2.
DR RefSeq; NP_510266.3; NM_077865.3.
DR AlphaFoldDB; B1Q257; -.
DR SMR; B1Q257; -.
DR STRING; 6239.R01E6.1b; -.
DR PaxDb; B1Q257; -.
DR PRIDE; B1Q257; -.
DR WormBase; R01E6.1a; CE27430; WBGene00003848; odr-1. [B1Q257-2]
DR WormBase; R01E6.1b; CE44132; WBGene00003848; odr-1. [B1Q257-1]
DR eggNOG; KOG1023; Eukaryota.
DR InParanoid; B1Q257; -.
DR OMA; QMIRMSE; -.
DR OrthoDB; 1029184at2759; -.
DR PhylomeDB; B1Q257; -.
DR PRO; PR:B1Q257; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003848; Expressed in pharyngeal muscle cell (C elegans).
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
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; ISS:WormBase.
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; ISS:WormBase.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0050919; P:negative chemotaxis; IMP:WormBase.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IGI:UniProtKB.
DR GO; GO:0042048; P:olfactory behavior; IMP:UniProtKB.
DR GO; GO:0008355; P:olfactory learning; IMP:WormBase.
DR GO; GO:0007602; P:phototransduction; IMP:UniProtKB.
DR GO; GO:0050918; P:positive chemotaxis; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; 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:0040014; P:regulation of multicellular organism growth; IGI:UniProtKB.
DR GO; GO:1990834; P:response to odorant; IMP:UniProtKB.
DR GO; GO:0050913; P:sensory perception of bitter taste; IMP:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00069; Pkinase; 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; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW cGMP biosynthesis; Chemotaxis; Glycoprotein; GTP-binding; Lyase; Membrane;
KW Nucleotide-binding; Olfaction; Receptor; Reference proteome;
KW Sensory transduction; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1067
FT /note="Receptor-type guanylate cyclase gcy-10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433279"
FT TOPO_DOM 21..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..1067
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 509..791
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 859..989
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 515..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..55
FT /note="MLKSLLIIVIVFLHRELCDGIQLILFDNWPSAQNVCASAVADATANGQCTTK
FT SIQ -> MCVLRLWQMRRPMDSVQQSQYSE (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057702"
FT VAR_SEQ 1028..1046
FT /note="EVNCYWLNEHLHEETEPPL -> NAARLKICCETFETHSIDL (in
FT isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057703"
FT VAR_SEQ 1047..1067
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057704"
FT MUTAGEN 647
FT /note="G->D: In n1930; loss of chemotaxis to volatile
FT odorants."
FT /evidence="ECO:0000269|PubMed:8348618"
FT MUTAGEN 904
FT /note="E->A: Probable loss of cyclase activity. Loss of
FT chemotaxis to some volatile odorants."
FT /evidence="ECO:0000269|PubMed:10774726"
FT CONFLICT 177
FT /note="E -> EE (in Ref. 1; AAF68380)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> EV (in Ref. 1; AAF68380)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="D -> DE (in Ref. 1; AAF68380)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="T -> S (in Ref. 1; AAF68380)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="T -> S (in Ref. 1; AAF68380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1067 AA; 121021 MW; 5C8D23FBD3C65294 CRC64;
MLKSLLIIVI VFLHRELCDG IQLILFDNWP SAQNVCASAV ADATANGQCT TKSIQKHLEL
LTVIILLKLF GVFHRINQQH GCSGDNSVKS ASYAINAVAS RTSGELDFVF VGPTCTTDIR
TIGDFAEIWK SPVIGYEPVF EARGVQELTS VINVAQFSVG GVAETLVFLM KELEQVEITL
VGSVKVLPNG LSLSNDLRSY NEIMNSFKIR EYVEVDENDV DWTKVDQKIK RGARMIVVCA
DFYDIYSAFY NIGIRSLSGF RFIIVVILNK PPDEILNQPN VKNLLYGSNA FIISPLQEQY
SDAFSIMQDV IPNLADDQFT TFLRIYHACY AYCVGSVNGA ETQTDNYHTA MSGKAVTTKY
GTFTFDNSGS VLTNYAVFTI NPAEMTFESI LTLKSVAKSC DTYNCFQLSP NKTSDLLWTL
KDMDPPDDCV AKSSCVNYIP HIIAAVVIVT IIVIAIVIIV KQRRHKLNIY KLTWKVPKES
LKIIVNKNAD AKMQRELENR ASNTDNAAAL TSRRRVFGSY ALVGTQRAEY VQFKQIRKIN
FPETTLDYLY SLKQLQHDNL AKFYGIQVND DIMTMTILHT LVERGTLEEF CLDRDFGMDD
TFKSAFMRDI LKGLQYLHKS SIGYHGHLQA STCLIDINWV LKLTLYGVSN FMSDQLDAEN
IKVPEQAAHM ITYPQYVCFP PEHIREYDDS GKQPPRVVRG SPKGDIYCVG MIFYMMVERE
DPYHLIHSVE RPNATLIKQI LNENHMPRIT DDYRQENMLL EMCKECWDRN PDKRPTIKKL
IESISTVYPL SKGNLVDQMI RMSEKYADEL EQMVAIRTAD LADAQMQTMR LLNEMLPASI
AKDLKNGLIM PPRSYESATV MFVQICDFNA LMKRSSPEQV IAFLNDIYDQ FDTVIKRHDA
YKVETTGETY MVASGVPHEN EGRHIFEVAE ISLEIREISY IYVLQHDKNY KLRIRIGFHA
GPIAAGVIGI RSPRYCLFGD TVNFASRMQS NCPPNQIQTS EITARLLFDS HEYKFVKRGI
VHVKGKGEVN CYWLNEHLHE ETEPPLPPMT PVPNPLRRGS IVPLQKA
