GCY5_CAEEL
ID GCY5_CAEEL Reviewed; 1122 AA.
AC Q23682;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Receptor-type guanylate cyclase gcy-5 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-5 {ECO:0000312|WormBase:ZK970.6};
GN ORFNames=ZK970.6 {ECO:0000312|WormBase:ZK970.6};
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). Unlike other guanylate cyclases
CC expressed in ASE neurons, may not play a role in chemotaxis responses
CC to salt ions mediated by ASE sensory neurons (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: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in both ASEL and ASER neurons during
CC early embryonic stages and becomes specifically expressed in ASER
CC neuron in early larval stage. {ECO:0000269|PubMed:16099833,
CC 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}.
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DR EMBL; BX284602; CAA88890.1; -; Genomic_DNA.
DR PIR; T28130; T28130.
DR RefSeq; NP_496219.1; NM_063818.1.
DR AlphaFoldDB; Q23682; -.
DR SMR; Q23682; -.
DR STRING; 6239.ZK970.6; -.
DR EPD; Q23682; -.
DR PaxDb; Q23682; -.
DR PRIDE; Q23682; -.
DR EnsemblMetazoa; ZK970.6.1; ZK970.6.1; WBGene00001532.
DR GeneID; 191643; -.
DR KEGG; cel:CELE_ZK970.6; -.
DR CTD; 191643; -.
DR WormBase; ZK970.6; CE02406; WBGene00001532; gcy-5.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q23682; -.
DR OMA; NTSECIN; -.
DR OrthoDB; 145275at2759; -.
DR PhylomeDB; Q23682; -.
DR PRO; PR:Q23682; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001532; Expressed in adult organism.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
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:0010035; P:response to inorganic substance; 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; 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; cGMP biosynthesis; Glycoprotein; GTP-binding; Lyase;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1122
FT /note="Receptor-type guanylate cyclase gcy-5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433274"
FT TOPO_DOM 20..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..1122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 542..830
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 888..1018
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 536..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1122 AA; 126422 MW; A757AA74B993EA8F CRC64;
MRLLYFSMVL LWVLGASECQ VIPSSRRTLR VGIAAAQDTQ SGSIGWASCG GTLPIAVQYL
KSKGFLTDFD VEYYMEYTEC DRASVAKAGM KFMKEMNVDV VVGPSCGDAL AIMGTLSAIY
KKLVLGWGFV SDTQLADTNR FPYVASVQPT AQTLGLATSR ILEMFQFDRV ALLYYKDDQD
YCKSVMDDVE ATLSDPDLYP VRIVWKGELQ SDNEALTRST LQAVKSRARI VLLCAISGPE
KRNYLISIAQ QNMTTNEYVH ILLTMRSIGY GVQTSLGKKT FANGLTPLWE SFTVAPDGNE
TNARRAAEKM LVIDVNSDVQ DAEFLQYLTK NIADAVRNPP MKCNTSECIN ASSTSMGSYA
RHLFDVFYLY GMAVSKLNST DPTVYGNLNL LMPQMVTSFD GMTGRVQIGQ NLYRVPTYQL
YGLDEKYEQV ALVNMTFYNS SSQLSRGYSD EGRSVWHFWD GTRPLDTPIC GFSGRYCPVQ
FWDQYGVLIF VASIVLIFLI CIMLMCFGFM IRGRRAEQER LNSEWQIPSI QLIMPQKEKR
KPNSRRSLQS GPSTITGESK MTIDGGFHEN YTVQMFEKDL VLTTKHHSMQ MNKEEKEKFV
KLRKLEHDNL NKFIGLSIDG PQFVAVWKMC SRGSLQDIIA RGNFSMDGFF MFCIITDIAE
GMNFLHKSFL HLHGNLRSAT CLVNDSWQVK LTDFGLGALL EEHTPSKKRL LWAAPEVLRG
SLTIHQMDPS ADVYSFAIIA SEILTKREAW DISNRKEGAD EILYMVKKGG NRTIRPELIL
DAEVSPRLTT LVKDCWSEQP EDRPKAEQIC KLLSEMTPRG NTNLMDHVFN MLEEYTSTLE
VDIEERTKEL TLEKKKADIL LSRMLPKQVA ERLKAGQTVE PEGFDTVTVL FSDVVKFTQL
AAKCSPFQVV NLLNDLYSNF DTIIEEHGVY KVESIGDGYL CVSGLPTKNG YAHIKQIVDM
SLKFMDYCKS FKVPHLPREK VELRIGINSG PCVAGVVGLS MPRYCLFGDT VNTASRMESN
GKPSMIHMSE AAHSLLTDHY PHQYETSSRG EVIIKGKGVM ETFWVLGKTD SDTKSLSTRT
TPPITDENWP PQMKEDLKKR AVTPYPERQR SGKSKMDTLK VV
