GCY21_CAEEL
ID GCY21_CAEEL Reviewed; 1119 AA.
AC O16715;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Receptor-type guanylate cyclase gcy-21 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-21 {ECO:0000312|WormBase:F22E5.3};
GN ORFNames=F22E5.3 {ECO:0000312|WormBase:F22E5.3};
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:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in ASG sensory neurons.
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; BX284602; CCD68450.1; -; Genomic_DNA.
DR PIR; T32074; T32074.
DR RefSeq; NP_494324.1; NM_061923.1.
DR AlphaFoldDB; O16715; -.
DR SMR; O16715; -.
DR STRING; 6239.F22E5.3; -.
DR PaxDb; O16715; -.
DR EnsemblMetazoa; F22E5.3.1; F22E5.3.1; WBGene00001546.
DR UCSC; F22E5.3; c. elegans.
DR WormBase; F22E5.3; CE09555; WBGene00001546; gcy-21.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196266; -.
DR HOGENOM; CLU_001072_1_2_1; -.
DR InParanoid; O16715; -.
DR OrthoDB; 7731at2759; -.
DR PhylomeDB; O16715; -.
DR PRO; PR:O16715; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001546; 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: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; 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; 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; Coiled coil; Glycoprotein;
KW GTP-binding; Lyase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1119
FT /note="Receptor-type guanylate cyclase gcy-21"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433290"
FT TOPO_DOM 18..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..1119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 474..769
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 840..970
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 788..817
FT /evidence="ECO:0000255"
FT BINDING 480..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1119 AA; 125836 MW; 826B37C2791572A4 CRC64;
MLSAVLLLLF FIQNVQNFDK IELEDITVYF PLKVDYLAPF GCATGTKCDD EAALNNGTIA
ALGLMRDCYI QSTILNINSK IAVSDVCEMD LSSVKGFDQT SVLMNSQTNS LAKSVMYFLD
KYQWKKVALV SPSTVLTAFA TRVRSDLLDA LTANKIDILV DSRLDPMSDI TDKVKEDAEK
ARIFIICDWS SNANLLRNYL FKLGEMNKMQ SGEYFVLGYI SYDTNYQWLE ASSGDQRLKI
TPRWDRIKLL FDSIQYLADA TNDALNIGAN IYQSDIFYEY LISRKIDSVT GVTEFIDGYG
AIVGSIQIYY HFSSSSHNSY SLFPCARLAQ SSLLNTVWSL TDYSEGLSID FVNKSAPKDT
PVCGFYGENC GPPANNTFII VISVGVAVLI GLAIAAAFLY KRYRYERRLH SLFFMIDRNQ
IILKKHTNLM SQQSLRSMAS IHGSVVAASQ TLRDSHFFIE DYNNASSINA SSIFNTGSTA
RAGPFGPIPG FGGVTGASED EKWHQIPDFG VGLYEGRTVA LKRIYRSDVE FTRSIRLEIA
KLQESVNSNV IEFVGMVVQS PDVFVVYELA QRGSLKDILD NDDMPLDDVF RSQMTKDIIA
GLEYLHSSPI GCHGRLKSTN CLIDARWMVR LSSFGLRELR GEETWQQEDD VQEGKDQLWT
SPELLRWSTG LSQCGVLLVQ KSDVYSLAIV LYELFGRLGP WGDEPMEPRE IVSLVKREAL
AGKKPFRPDM AVLKESPRIV QETVVAAWTE DPLNRPSLHQ IKRKLKPLTI GLKRTIMDNM
VSMIEKYTDK LEKDIAERNE ELEGEKAKSE ALLKMMLPEV VADSLKLGSN VSAESFENCT
VFFSDCPGFV EMSATSKPID IVQFLNDLYT VFDRIIDQFD VYKVETIADA YMVASGLPVP
NGNHHAGEIA SLGLALLKAV ESFKIRHLPN EKVRLRIGMN SGPCVAGVVG LKMPRYCLFG
DTVNTASRME SNGIPLRINC SGTAKEILDQ LGGYEIEERG IVEMKGKGKQ MTYFVRGENS
DMRRERIIRE RVKFASLKKA QIQEKTYEFS LNKLFIVKSF LKLLIRYLQM RRHPISNHNV
VTVKTCMRTI PPQEVYISST LPYEDSEEEA STVYDTVTY
