GCY3_CAEEL
ID GCY3_CAEEL Reviewed; 1140 AA.
AC Q10028;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Receptor-type guanylate cyclase gcy-3 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-3 {ECO:0000312|WormBase:R134.1a};
GN ORFNames=R134.1 {ECO:0000312|WormBase:R134.1a};
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=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).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). {ECO:0000250|UniProtKB:Q19187}.
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 asymmetrically in ASE right (ASER)
CC sensory neuron and bilaterally in ASI sensory neurons. Expressed in PVT
CC interneuron. {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; BX284602; CAA88052.1; -; Genomic_DNA.
DR PIR; T24213; T24213.
DR RefSeq; NP_496037.1; NM_063636.1.
DR AlphaFoldDB; Q10028; -.
DR SMR; Q10028; -.
DR STRING; 6239.R134.1; -.
DR PaxDb; Q10028; -.
DR PRIDE; Q10028; -.
DR EnsemblMetazoa; R134.1a.1; R134.1a.1; WBGene00001530.
DR GeneID; 191641; -.
DR CTD; 191641; -.
DR WormBase; R134.1a; CE01636; WBGene00001530; gcy-3.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196185; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q10028; -.
DR OMA; DLMPKTK; -.
DR OrthoDB; 127698at2759; -.
DR PhylomeDB; Q10028; -.
DR PRO; PR:Q10028; -.
DR Proteomes; UP000001940; Chromosome II.
DR ExpressionAtlas; Q10028; baseline and differential.
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: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: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: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 ATP-binding; Cell membrane; cGMP biosynthesis; Glycoprotein; GTP-binding;
KW Lyase; Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1140
FT /note="Receptor-type guanylate cyclase gcy-3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433271"
FT TOPO_DOM 22..495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..1140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 538..826
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 897..1027
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1083..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 544..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1140 AA; 128075 MW; 66E061D247D8E33B CRC64;
MKNVFQLLIP LFFHLFSLVS LQNIPVSTGT TRPKLKVGIA AAQKTQSASI GWNVCGGAVP
LAIERLKQAG YVTNFDFEYY VEYTECDLAS TVRTGINFLK NLEVDVIIGP PCSEAIRTMA
TLATLYKKPV LGWGFVSQAD LSDMTRFPYL ITVLPTSQTL GYAASKLLEL YKWDKVALLY
YKSEVNHCGG VMNDVETTFN DPSTYSIQIV LKAEIDASDN VTTNAVISSV KTRARIILWC
AQLGSEKRDY MIKISQLGLD TDEYVHVLIS MRSIGFGVQT FVGKTTFKLS GLTPVWESFS
NVTDGLENVA KRGATNVLVI DLNSEVSDKA YLDYMQRNIL NVVKLPPLNC STVDCVSSTA
TGMGAYARHL FDVVYLYGIA LTRVNSTDSA VYDDMSKLIP QFVTSFNGMT GLVAINQNLS
RMPLYQLYGL DEQYEQTSLM NLSFADGTTV ATISLAYSNE SSAVWHFWGG IRPLATPICG
FLGNSCPLPF WEQYGILIFV GAGVFLIMIT TNLICFLFMI KNRREEQARI NSEWQIPFVK
LRELERKSKG TSKRSLQSAP STITGESKVS TGSEFCENYE VKMFEKDMVL TMKFQYMNLN
KADMDKFVKL RKLDHENLNK FIGLSIDSSQ FISVTKLCSR GSLLDILYKG NFSMDFFFMY
CIIKDVAEGM SYLHKSFLRL HGNLRSATCL VNDSWQVKLA EFGFDQLLEE ITPTKRRLLW
AAPEVLRGSL TVSQMDPSAD VFSFAIIASE ILTRKEAWDL KERKEGYDEI IYRVKKGGSF
PIRPDIITDV PDVNPTLIAL VKDCWAEAPE DRPTAENICE QLRDLMPKTK SNLMDHVFNM
LEEYTSTLEV EVEERTKELT LEKKKADLLL SRMLPKQVAE RLKAGQTVEP EGFDSVTVFF
SDVVKFTILA SKCTPFQVVN LLNDLYSNFD TIIEEHGVYK VESIGDGYLC VSGLPTRNGF
NHIKQIVDMS LKFMDYCKNF KIPHLPRERV ELRIGVNSGP CVAGVVGLSM PRYCLFGDTV
NTASRMESNG KPSLIHLTSD AHLLLMKHFP HQYETNSRGE VIIKGKGVME TFWVLGRSGD
IEPSISNRST PPVTQERFTV RAPDTPEARS VSSHGSRPSS NHNNNNDPLY RQYKMDTLKI
