GCY19_CAEEL
ID GCY19_CAEEL Reviewed; 1182 AA.
AC O16544;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 4.
DT 03-AUG-2022, entry version 165.
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:C17F4.6};
GN ORFNames=C17F4.6 {ECO:0000312|WormBase:C17F4.6};
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 IL2 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}.
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; BX284602; CCD64916.1; -; Genomic_DNA.
DR RefSeq; NP_494491.4; NM_062090.6.
DR AlphaFoldDB; O16544; -.
DR SMR; O16544; -.
DR STRING; 6239.C17F4.6; -.
DR PaxDb; O16544; -.
DR UCSC; C17F4.6; c. elegans.
DR WormBase; C17F4.6; CE45028; WBGene00001544; gcy-19.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; O16544; -.
DR OMA; SIDPFFM; -.
DR PhylomeDB; O16544; -.
DR PRO; PR:O16544; -.
DR Proteomes; UP000001940; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1182
FT /note="Receptor-type guanylate cyclase gcy-19"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433288"
FT TOPO_DOM 25..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..1182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 562..849
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 907..1037
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1094..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1182 AA; 132247 MW; 35E4D8C0B0060F3F CRC64;
MEYLLFLLLF AGFLTFLPRF LIYAQITSST TTTTPVPAAN RRTIRVGVAA VQTTELDSIG
WPMSGGAINM AIQKLRDDGF IAPFDFEVTV NYTECDRSLG AAVGMEFMRT KRLDVVIGPP
CRDPMEIMAT MATYYSTPML GWGLVTDSKF TDTERYPYLT NIMANSLSLG FSLVKLLEMM
EWDRVALVYE ESAQDYPLSV INDVETAINE YDTFAVNVVV KQALPGGDLN DAQYISVLNR
IKLRCRIIVS VFQTAPTRRR YLKMIDQQGM ANEEYVHILL GLRSIGFGKQ SAGLTKCELN
CLSSGLAPFW DIAPDDGLND RLKQAATRML VMDLSTDVPD INYLNTFTMN CGAVVVNPPV
SCATPACINA STSPPSAFAR SLHDVFYLYG LAITNLYNQD PAYLNDIDKI NGALQLNFAG
LTGEVSINAN NSRVPKLMLY ALNDKYDQAS FMNLTYSLNG GAVSVSLAYT NEASLWYWYG
GKRPLSVPVC GFAGTDCPQS FVDQYGALVF AIGGVLIFAM LFVITCFFYV MRQKRLERDR
IDAEWQIPLV KLQAPPKRDK ERMSKRSLQS GPSNITDTSK MTFDNTFSNY SIFYLDKEPV
LSTAHPASNL IRTDYDTFVR LRKLDHENVN KFVGMSIDGP EYLAVWKLCM RGSLQDIIGQ
GNFSIDPFFM FCVIRDMAEG LKYLHNSFLH VHANLRSGTV LVNESWQAKL TDFGLGTLAE
EKKPMKRRQL WMAPEVIRGT LLPHQIEKSA DIYSLAVIAS EVLTRKEAWN MAERKDTVDE
IVYRIKKGGP NAPRPELDMD GVEINHNLLI LIRDCWSEEP ADRPSADVIC NLLKNMMPKK
GNLMDHVFNI LEDYTTNLEV EVEDRTKELT AEKKKADVLL GRMLPKQVAE RLKQGQTVEP
EGFDSVTVFF SDVVKFTQLA AKCSPFQVVN LLNDLYSNFD AIIEEHGCYK VESIGDGYLC
VSGLPSKNGN AHIKQIVELS LDFMSYCKSF KIPHLPREKV ELRIGVNSGP CVAGVVGLSM
PRYCLFGDTV NTASRMESNG KASHIHLSAA SYTLLMKHYP NQYNTASRGD VIIKGKGVME
TFWVFERNNQ FMGVSSNSGY QSDKKATNNG SSPESTPPST PPMHEVKANS PVRHRKPPSP
SSPTLSKRSV SPIMEAKARD IHNEETEALY RQFRRQETLA LI
