GCY1_CAEEL
ID GCY1_CAEEL Reviewed; 1137 AA.
AC Q09435;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Receptor-type guanylate cyclase gcy-1 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-1; ORFNames=AH6.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP TISSUE SPECIFICITY.
RX PubMed=16547101; DOI=10.1534/genetics.106.055749;
RA Ortiz C.O., Etchberger J.F., Posy S.L., Frokjaer-Jensen C., Lockery S.,
RA Honig B., Hobert O.;
RT "Searching for neuronal left/right asymmetry: genomewide analysis of
RT nematode receptor-type guanylyl cyclases.";
RL Genetics 173:131-149(2006).
RN [3]
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). Involved in the sensing of K+ gradient
CC by the ASE right (ASER) sensory neuron (PubMed:19523832).
CC {ECO:0000250|UniProtKB:Q19187, 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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in sensory neurons.
CC Expressed asymmetrically in the right ASE (ASER) neuron and bilaterally
CC in ASI and URX neurons. Expressed in PVT and bilaterally in AIY non-
CC sensory neurons. Expressed in intestine. {ECO:0000269|PubMed:16547101}.
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; Z48009; CAA88089.1; -; Genomic_DNA.
DR PIR; T18625; T18625.
DR RefSeq; NP_496039.1; NM_063638.1.
DR AlphaFoldDB; Q09435; -.
DR SMR; Q09435; -.
DR STRING; 6239.AH6.1; -.
DR PaxDb; Q09435; -.
DR PRIDE; Q09435; -.
DR EnsemblMetazoa; AH6.1.1; AH6.1.1; WBGene00001528.
DR GeneID; 191639; -.
DR KEGG; cel:CELE_AH6.1; -.
DR UCSC; AH6.1; c. elegans.
DR CTD; 191639; -.
DR WormBase; AH6.1; CE01450; WBGene00001528; gcy-1.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196185; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q09435; -.
DR OMA; IVEYTEC; -.
DR OrthoDB; 154751at2759; -.
DR PhylomeDB; Q09435; -.
DR PRO; PR:Q09435; -.
DR Proteomes; UP000001940; Chromosome II.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0010226; P:response to lithium ion; IMP:UniProtKB.
DR GO; GO:0035864; P:response to potassium ion; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IMP:UniProtKB.
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; 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 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; 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 cGMP biosynthesis; Chemotaxis; Coiled coil; Glycoprotein; GTP-binding;
KW Lyase; Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1137
FT /note="Receptor-type guanylate cyclase gcy-1"
FT /id="PRO_0000012388"
FT TOPO_DOM 19..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..1137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 557..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 REGION 1086..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 840..871
FT /evidence="ECO:0000255"
FT COMPBIAS 1087..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1137 AA; 128104 MW; 93EC01501F0228F9 CRC64;
MQIFTILLLF NIFPSIFVQN LPDTTVAPRT KRTIKIGIAA AQRIQTSSIG WSVCGGAVPL
AIERLKEMGF VKDFDFEYIV DYTECDLGSV VRAGMEFIKT HKVDVIIGPP CAQALRLMSF
LAENYKKPVL GWGFVSDTDL SDVIRFPHLT TVIPNSLMLG YAASKMLTTF HWNRVALLYY
FSDVKYCSGV MNDIEATFND PSTPNVNIVI KAEIYLNDNE TTDNVFQTVK SRARIILWCT
QTSVEKRDYL IKIATHDMIG DEYVHIMLSM RNVAFGTQTS LGKPTFSQSG LTPIWESFTE
GTDGFEKMAK QAATRMFVLD VNSEVADKKY LEYMQKNIIK AVQSPPMNCS TVECMTANTT
IMGGYARHLF DVVYLYGIAL THTNSTDPAV YGDVDVLVHQ FVTSFQGMTG HVVISPNLTR
MPIFQLYGLN SDYDQVALVD FTYTNSVMVP NVTLFYKDEG GAVWSYYGHS RPLDIPICGF
LGKSCPVSFW EQYKILIFVA IAVIVLMVLI MIIGCLCVIS GKRAERARIN AEWQVPFAKL
IESEKQVRGK GASRRSLQSA PSISTGHSGV TTVSDFCENY TMMMYEKEMV LTAKYQYTHL
TKADKERFVK MRKLDHENIN RFIGLSIDSA HFISVTKLCS RGSLQDILSR GNFSMDYFFM
FCIIRDVAKG LEYLHKTFLR LHGNLRSATC LVNDSWQVKL AEYGMDNLVE EQTPPKKRLL
WVAPEVLRGS LSVSQMEPSA DIYSFAIIAS EILTKKEAWD ILDRKEDCEE IVYNVKKGGL
FPIRPEIITD IHDVNPALIA LVKDCWAEVP EDRPTAENIC SQMKGLVSKQ KTNLMDHVFN
MLEEYTSTLE EEIEERTKEL TLEKKKADIL LSRMLPKQVA ERLKAGQTVE PEGFDSVTVF
FSDVVKFTIL ASKCSPFQTV NLLNDLYSNF DTIIEQHGVY KVESIGDGYL CVSGLPTRNG
YAHIKQIVDM SLKFMEYCKS FNIPHLPREN VELRIGVNSG PCVAGVVGLS MPRYCLFGDT
VNTASRMESN GKPSLIHLTN DAHSLLTTHY PNQYETSSRG EVIIKGKGVM ETFWVHGRFG
EMEPTELRSI SNRSTPPVTN DRWIPNPSSS HGSRPSSVYD PLQGHQKFKM DTLKVAN
