GCY20_CAEEL
ID GCY20_CAEEL Reviewed; 1108 AA.
AC O62179;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Receptor-type guanylate cyclase gcy-20 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-20 {ECO:0000312|WormBase:F21H7.9};
GN Synonyms=gcy-16 {ECO:0000312|WormBase:F21H7.9};
GN ORFNames=F21H7.9 {ECO:0000312|EMBL:CAB07591.2};
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=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). {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 left (ASEL) sensory
CC neuron. Expressed in excretory gland and canal cell.
CC {ECO:0000269|PubMed:19523832}.
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; BX284605; CAB07591.2; -; Genomic_DNA.
DR PIR; T21223; T21223.
DR RefSeq; NP_507101.1; NM_074700.1.
DR AlphaFoldDB; O62179; -.
DR SMR; O62179; -.
DR STRING; 6239.F21H7.9; -.
DR PaxDb; O62179; -.
DR EnsemblMetazoa; F21H7.9.1; F21H7.9.1; WBGene00001545.
DR GeneID; 184797; -.
DR KEGG; cel:CELE_F21H7.9; -.
DR UCSC; F21H7.9; c. elegans.
DR CTD; 184797; -.
DR WormBase; F21H7.9; CE28919; WBGene00001545; gcy-20.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196659; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; O62179; -.
DR OMA; TGHIHIS; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; O62179; -.
DR PRO; PR:O62179; -.
DR Proteomes; UP000001940; Chromosome V.
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:0007635; P:chemosensory behavior; IEA:UniProt.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
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:0010038; P:response to metal ion; IEA:UniProt.
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 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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1108
FT /note="Receptor-type guanylate cyclase gcy-20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433289"
FT TOPO_DOM 16..474
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..1108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 483..803
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 876..1006
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1083..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1108 AA; 124349 MW; 7E3999A3A144E71B CRC64;
MRILLLLLQN ILVFCQFLQT IKVGLMFSKD TASVIRSVGY RTSAAAVLVA KDRIRAEHLL
DQYDFNFTIK FDECSESLAA GKVVELLTHD NVDVIIGPTC NRAGVAVASL ADFYNVPVFQ
WGLTTTADIG NFSRYQTTVT LSLDTHSISL AVREILRQYG WSEFVFIYSN DGDEEKCAAM
KDDMEKMGIE NSDVTMAYMI QIQTVTMESL QRTLLEVSKR GRIIIACFAS GRGFKKAFIA
STVLAGMSTE EYLYVFAEPQ SRGFYVDEAD GKVHYSWDDT DGQLVTGLTN EQIRDAYGKV
LYICDNMGEP TTITTQYTNF TSQVISRMAE QPFNCVQDCS NQSYKHAATY AGQLADSFYA
YAFALNKSLT QDPTRSNLKN GSFVLSNIGM TFQGVGGEAV TLDESGSRIV QVYMFAMNSS
LLPYMAASLL VNVSEVVFTP FYKSESELWS VRPLSRPKCG FTGLECPADF VKEYLVYTII
AAFIVILALL AGCAGLLYTM HMKRKEMERQ DLLWQVAFVE LQQVQSKSRA EASMHSFASG
PSTSTKMTVE SRTETTNFIF YHYHQEVVAA KKHDLLVLFD ANQKSEFRQM RNFDNDNLNK
FIGLCLDGPQ LLSLWRFCSR GSLSDVISKS SMQMDSFFMF SLIRDISNGL YFIHSSFLKC
HGQLTSRCCL IDDRWQIKIS GFGLKSVRTF ENPKKEDLLW ASPEYLRNED QERLPEGDIY
SFGIICAEIL TRSSAFDLEN RKEKPDVIIY QVKKGGHNPT RPSLDTGETV VINPALLHLV
RDCWTERPSE RPSIEQVRSH LNGMKDGRKT NLMDHVFNML ETYASTLEEE VSDRTKELTE
EKKKSDVLLY RMLPRMVADK LKLGQTVEPE TFEQVTIFFS DVVQFTTLAG KCTPLQVVTL
LNDLYTIFDG IIEQNDVYKV ETIGDGYLCV SGLPHRNGND HIRHIARMSL GFLSSLEFFR
VQHLPAERIN LRIGINCGSV VAGVVGLTMP RYCLFGDAVN TASRMESNGK PGQIHVTAEA
NRMLTQVVGG FRTESRGEVI IKGKGVMETF WLLGEESGYT APSKAAPKVI QHRQSIRSIS
PILEKNAEGS ETSSLSVDQA GDNNSETV
