GCY19_CAEBR
ID GCY19_CAEBR Reviewed; 1214 AA.
AC A8XQC7;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Receptor-type guanylate cyclase gcy-19 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-19 {ECO:0000312|WormBase:CBG17049a};
GN ORFNames=CBG17049 {ECO:0000312|WormBase:CBG17049a};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000312|Proteomes:UP000008549};
RN [1] {ECO:0000312|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP34845.2,
RC ECO:0000312|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE601138; CAP34845.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XQC7; -.
DR STRING; 6238.CBG17049; -.
DR WormBase; CBG17049a; CBP39728; WBGene00036817; Cbr-gcy-19.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; A8XQC7; -.
DR OMA; SIDPFFM; -.
DR OrthoDB; 97535at2759; -.
DR Proteomes; UP000008549; Chromosome II.
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: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 Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00069; Pkinase; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1214
FT /note="Receptor-type guanylate cyclase gcy-19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433287"
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..1214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 572..859
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 917..1047
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1116..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 363
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 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1214 AA; 136134 MW; 959F378A9C15C53B CRC64;
MEHLIFLLIF GGYSPSIAQI TSSTTTTTPV PAANRRTIRV GVAAVQSTEL DSIGWPMSGG
AINLAIQKLR DDGFIAAFDF EINVNYTECD RSLGAAVGME FMRSKKYDVV IGAPCQDPME
IMATMATYYT TPLLAWGLVT DSKFTDAERY PYLTNIMANS LSLGFSLVKL FEMMDWDRVA
LLYETSPQDY PLSIINDVET AINEYEDYSV NVVVKQAVPS GDLNDAQYIS VLNRIKSRCR
IVVAVIQTAT PRRKYLRMIT EQNMVSDEYV HIWLGLRSIG FGKQSAGLTK CELNCLSSGL
TPVWEVLPDD GWNERAKLAA TRLLVMDLST DVPDVNYLNT FTSQCGAQVV NPPVSCETEQ
CKNASTSPPS AFARSLHDVF YLYGLAITNI YNTNPVNLAN GQAINDAMQL TFAGDCSAQF
FSKKNILTFL GLTGEVSINA NNTRVPKLML YALNENYDQA SFMNLTYSLD GGASVSLGYT
NEASLWFWYN GKRPLTIPIC GFLGTECPQT FVDQYGALVF SIGGVLALAM LFLITCFFYV
LRQRKLERDR IDAEWQIPLV KLQVPPKREK ERMSKRSIQS GPSNITDTSK MTFDNTFSNY
SIFYLDKEPV LSTAHPASNL DRTDYDTFVK LRKLDHDNIN KFVGLSIDGA EYLAVWKMCM
RGSLQDIIGQ GNFSIDPFFM FCVIRDMAEG LKYLHNSFLH VHANLRSGTV LINESWQAKL
TDFGLGNLAE EKKPMKRRQL WMAPEVIRGT LLPHQVEKPA DIYSLAIIAS EVLTRKEAWN
MSERKDTVDE IVYRIKKGGP NSIRPDLDMD GVEINHSLLV LIRDCWSEDP TDRPGADIIC
NLLKNMMPKK GNLMDHVFNI LEDYTTNLEV EVEDRTKELT AEKKKADVLL GRMLPKQVAE
RLKQGQTVEP EGFDSVTVFF SDVVKFTQLS QKCSPFQVVN LLNDLYSNFD AIIEEHGVYK
VESIGDGYLC VSGLPQRNGN AHIKCIVELS LDFMAYCKAF KIPHLPREKV ELRVGVNSGP
CVAGVVGLSM PRYCLFGDTV NTASRMESNG KPSHIHLSAA AYTLLMKHYP NQYNTASRGD
VIIKVGPLLG LFRPFQGKGV METFWVFERN NQFMGNSSNM AYNPENKKKQ KNDDEDVDDE
SSDGSSRAPN TPPMHDVNAN SPPRQRKPGP PSSSPTFSKR SVSPILEEKA REIHNEETEA
LYRQFRRQET LALM
