GCY11_CAEEL
ID GCY11_CAEEL Reviewed; 1168 AA.
AC Q18331;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 5.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Receptor-type guanylate cyclase gcy-11 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-11 {ECO:0000312|WormBase:C30G4.3};
GN ORFNames=C30G4.3 {ECO:0000312|WormBase:C30G4.3};
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:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal muscle.
CC {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; BX284606; CCD63635.3; -; Genomic_DNA.
DR RefSeq; NP_510755.4; NM_078354.5.
DR AlphaFoldDB; Q18331; -.
DR STRING; 6239.C30G4.3; -.
DR EPD; Q18331; -.
DR PaxDb; Q18331; -.
DR EnsemblMetazoa; C30G4.3.1; C30G4.3.1; WBGene00001537.
DR UCSC; C30G4.3; c. elegans.
DR WormBase; C30G4.3; CE53392; WBGene00001537; gcy-11.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; Q18331; -.
DR OrthoDB; 7731at2759; -.
DR PhylomeDB; Q18331; -.
DR PRO; PR:Q18331; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001537; Expressed in embryo and 2 other tissues.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; cGMP biosynthesis; Coiled coil; Glycoprotein; GTP-binding;
KW Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1168
FT /note="Receptor-type guanylate cyclase gcy-11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433280"
FT TOPO_DOM 19..517
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..1168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 562..888
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 959..1089
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 896..934
FT /evidence="ECO:0000255"
FT BINDING 964
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 964
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 965
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1008
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1008
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1168 AA; 131443 MW; 8F11C246C0B8A4A1 CRC64;
MPCREIFLLW ILVPIASSSD HITFFGRYAC NVDFKTDYCT PDTYVGRAFY YGLEDGGGIT
TNGTFVNSDI TVEFFDPTVQ GNFSIGRQDG NYMSSMLDIM LADTKKNDGL LGVVGVENDC
KEIAALAQAY DASSLLVNCE DQVGESQMPS STALQMSSTQ GGKYRAFAKL AKSVGWNNLA
VINFVEDGPA DISYHDQLLD ALSAESISLD FVKKGGFSST ITSAMFTGLE SVIDVILETY
MKTRIYVIVL DLPVSGTFFM NAMSTMGLLE TGKYFVVMMS SIESDAANYF GFNVNRGNMI
FKTIDYGISD ADIRQYYRSF MYFTDVPHYT KDFSDEWTSF QKRVDGDASK TFCPPMCNTK
AKGIANNDPW SDDAYWYSES PSIVDAYDLG RLLSETVKVH GASLLRDPES LVQTMSGRGV
TSLLGYVTKF NTNGVSQREY ILWAPQQASS SNGPIPLPEW ATLAARMLPD GKGNYSIIWK
NLTQLGIFNG ELPQSKPECG FNNELCPAGI RNLSELEIIV IAVCVVAILI LVGVIAYIAR
WIAYERRLES SYFLVHRKHV QLVDMTKFGS SRGGSMIQSA MSMRSQYEDS GPVGGATMNF
YTNGIRKAAI RRNQMQRSDK GPAANRDEWL EIVDWHLAKY ENTLVTVRKI NKTQLKLTRE
MKQEIDLLMN ETHENLNRFF GLINESDLIF TIHSYGPRKS LMDLLRNDDL RLDRMFKVSF
VEDVVKGLQF LHEGSKIGYH GNLKSSNCIV DAYWRIKLSN YGMEQIRVEE PESKPDDLLW
FAPEIIRRYA VKHDLSKLEL AKADIYSLAI VLYEIYGRQG PFGDDLLDSD EIIEQLKFPD
GGALTRPDIH LITKAPYPLA SVVEKCWVED PASRPSIKKV RELLKPLSKG LKGNIADNIM
NLLDRYRNNL EDVIKERTEQ LEDERKRNES LLLQLLPKSV ANSLKNGQPV DAEFYDSVSI
YFSDIVGFTA LSSKSTPLQV VNMLNNLYTN FDTIIDKFDC YKVETIGDAY MFVSGLPEVN
SYLHAGEVAS ASLELLDSIK TFTVSHCPDE KLRLRIGNHT GPVVTGVVGI RMPRYCLFGD
TVIIANMMES SGEPMRIQIS SDAYELILKC GGYVTEQREK IVLKNKLEVM TYWMNDYSKD
ARLARLVAHQ EKFPHLEHLI HKFNKGVR
