GCY15_CAEEL
ID GCY15_CAEEL Reviewed; 1115 AA.
AC P91550;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Receptor-type guanylate cyclase gcy-15 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-15 {ECO:0000312|WormBase:ZC239.7};
GN ORFNames=ZC239.7 {ECO:0000312|WormBase:ZC239.7};
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 bilaterally 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; CCD64945.1; -; Genomic_DNA.
DR RefSeq; NP_494468.2; NM_062067.2.
DR AlphaFoldDB; P91550; -.
DR SMR; P91550; -.
DR STRING; 6239.ZC239.7; -.
DR PaxDb; P91550; -.
DR PRIDE; P91550; -.
DR EnsemblMetazoa; ZC239.7.1; ZC239.7.1; WBGene00001541.
DR UCSC; ZC239.7; c. elegans.
DR WormBase; ZC239.7; CE42950; WBGene00001541; gcy-15.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196266; -.
DR HOGENOM; CLU_001072_1_2_1; -.
DR InParanoid; P91550; -.
DR OMA; YERKLHS; -.
DR OrthoDB; 7731at2759; -.
DR PhylomeDB; P91550; -.
DR PRO; PR:P91550; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001541; Expressed in larva and 1 other tissue.
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: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 InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
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 Lyase; Membrane; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..1115
FT /note="Receptor-type guanylate cyclase gcy-15"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433284"
FT TOPO_DOM ?..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 528..823
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 894..1024
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT COILED 838..871
FT /evidence="ECO:0000255"
FT BINDING 534..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1115 AA; 124987 MW; 50846B068ED0BDCB CRC64;
MEIAINRLNA DKDLEVFHDL DVNYVDTSKT AGPRAARTAA LNNATVAAMG LMRDCYIQST
ILNINLKIAV SDVCEMDLSS VKGFDQTSVL MNSQTNSLAK SVMYFLDKYQ WKKVALVSPS
AVLTAFAARV RSDLLDALTA NKIDILVDSR LDPMSDITEK VKEDAEKARI FIICDWSSNA
NLLRNYIFKL GEMNKMQSGE YFVLGYISYD TNYQWLEASS GDQRLVHLGA SDINDYNLTE
NDLHEVYKNV VILSDGPPPA EPNSTWEDIK TQVLKKKPAK MCPPYCNTTI SEKITPRWDR
IKLLFDSIQY LADATNDALN IGANIYQSDI FYEHLISRKV DSVTGVTEYI DGYGAIVGSM
QIYYHFSSSS HNSYSLFPCA RLAQSSLLNT VWSLTDYSEG LSIDFVNKSA PKDTPVCGFY
GENCGPPANN TFIIVISVGV AVLIGLAIAA AFLYKRYRYE RRLHSLFFMI DRNQIILKKH
TNLMSQQSLR SMASIHGSVV AASQTLRDSH FFIEDYNNAS SINASSIFNT GSTARAGPFG
PIPGFGGVTG ASEDEKWHQI PDFGVGLYEG RTVALKRIYR SDVEFTRSNR LEIAKLQESV
NSNVIEFVGM VVQSPDVFVV YELAQRGSLK DILDNDDMPL DDVFRSQMTK DIIAGLEYLH
SSPVGCHGRL KSTNCLIDAR WMVRLSSFGL RELRGEETWQ QEDDVQEGKD QLWTSPELLR
WSTGLSQCGV LLVQKSDVYS LAIVLYELFG RLGPWGDEPM EPREIVSLVK REALAGKKPF
RPDMAVLKES PRIVQETVVA AWTEDPLNRP SLHQIKRKLK PLTIGLKRTI MDNMVSMIEK
YTDKLEKDIA ERNEELEAEK AKSEALLKMM LPEVVADSLK LGSNVSAESF ENCTVFFSDC
PGFVEMSATS KPIDIVQFLN DLYTVFDRII DQFDVYKVET IADAYMVASG LPVPNGNHHA
GEIASLGLAL LKAVESFKIR HLPNEKVRLR IGMNSGPCVA GVVGLKMPRY CLFGDTVNTA
SRMESNGIRK FFWVAEPVSS LRINCSGTAK EILDQLGGYE IEERGIVEMK GKGKQMTYFV
RGENSDMRRE RIIRERVKFA SLKKAQIQEK TYEFS
