GCY27_CAEEL
ID GCY27_CAEEL Reviewed; 735 AA.
AC Q9XU42; C1P657;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Receptor-type guanylate cyclase gcy-27 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-27 {ECO:0000312|WormBase:C06A12.4a};
GN ORFNames=C06A12.4 {ECO:0000312|WormBase:C06A12.4a};
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).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=23874221; DOI=10.1371/journal.pgen.1003619;
RA Krzyzanowski M.C., Brueggemann C., Ezak M.J., Wood J.F., Michaels K.L.,
RA Jackson C.A., Juang B.T., Collins K.D., Yu M.C., L'etoile N.D.,
RA Ferkey D.M.;
RT "The C. elegans cGMP-dependent protein kinase EGL-4 regulates nociceptive
RT behavioral sensitivity.";
RL PLoS Genet. 9:E1003619-E1003619(2013).
RN [4]
RP FUNCTION.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (By similarity). May be involved in sensitivity to
CC quinine by regulating egl-4 activity through the production of cGMP
CC (PubMed:23874221). Promotes the calcium flux to the cytoplasm in ASJ
CC sensory neurons upon removal of a nitric oxide (NO) stimulus and is
CC thereby involved in the behavioral avoidance response to NO-producing
CC organisms like P.aeruginosa (PubMed:30014846).
CC {ECO:0000250|UniProtKB:Q19187, ECO:0000269|PubMed:23874221,
CC ECO:0000269|PubMed:30014846}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C06A12.4a};
CC IsoId=Q9XU42-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C06A12.4b};
CC IsoId=Q9XU42-2; Sequence=VSP_057709;
CC -!- TISSUE SPECIFICITY: Expressed bilaterally in ASK, ASI and ASJ sensory
CC neurons. {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; BX284604; CAB06040.4; -; Genomic_DNA.
DR EMBL; BX284604; CAX65048.1; -; Genomic_DNA.
DR RefSeq; NP_001255956.2; NM_001269027.2.
DR RefSeq; NP_001255957.2; NM_001269028.2.
DR AlphaFoldDB; Q9XU42; -.
DR SMR; Q9XU42; -.
DR STRING; 6239.C06A12.4a; -.
DR PaxDb; Q9XU42; -.
DR EnsemblMetazoa; C06A12.4a.1; C06A12.4a.1; WBGene00001550.
DR EnsemblMetazoa; C06A12.4b.1; C06A12.4b.1; WBGene00001550.
DR GeneID; 191654; -.
DR KEGG; cel:CELE_C06A12.4; -.
DR UCSC; C06A12.4; c. elegans. [Q9XU42-1]
DR CTD; 191654; -.
DR WormBase; C06A12.4a; CE50575; WBGene00001550; gcy-27.
DR WormBase; C06A12.4b; CE50588; WBGene00001550; gcy-27.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00970000196639; -.
DR HOGENOM; CLU_001072_11_1_1; -.
DR InParanoid; Q9XU42; -.
DR OrthoDB; 434403at2759; -.
DR PhylomeDB; Q9XU42; -.
DR PRO; PR:Q9XU42; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001550; Expressed in larva.
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:0007635; P:chemosensory behavior; IMP:UniProtKB.
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:0050913; P:sensory perception of bitter taste; IMP:UniProtKB.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
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 SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; cGMP biosynthesis; Glycoprotein;
KW GTP-binding; Lyase; Membrane; Nucleotide-binding; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT CHAIN ?..735
FT /note="Receptor-type guanylate cyclase gcy-27"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433294"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 188..465
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 538..668
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 194..211
FT /note="RVFGSYALIGTQRAEFIQ -> R (in isoform b)"
FT /id="VSP_057709"
SQ SEQUENCE 735 AA; 84858 MW; E5849756976AE577 CRC64;
MIDGEAYFEK NSTGKLGSWG WRDVNLQFII CTLPVPIYFV VVAIWTINGA SNSYRFPFLQ
TYMILTDRFW LFFRCFTIVA WCGWCSNYIF FPCLMNAILY IISLSLSRDT TFILFIFYQM
NKLITVIRDF SYSVYNWCYE TVIGENTRKY KMTWKVPKES LKIIVNKNAD ARMQRELENR
TAKDEANALT SRRRVFGSYA LIGTQRAEFI QFRQIKHIDI TNASLDFLYN LKQLKHDNLA
NFYGIQLNDD LNTMTILHAL VERGTLEEFC LDRDFGMDET FKSAFMRDIL KGLQYLHLSP
VAYHGHLHAA TCLIDINWVL KIALYGVTNF VCDNFDAENI TMPDRSDYTI SYAQYVCFPP
EHIREYDATG KLPTRFVRGS KQGDIYCVGM IFYMMIERED PYRLIHSVER PGSGLMMEIL
DHNLMPFISN NETQEDTLLD KCKECWNRDP EKRPTIENLR NAIAICYADS KGNLIDQMIR
MNEKYADELE TLVAARSADL ALAQMQTMRL LNEMLPASIA KDLKNGVIAP ARSYASATVM
FVQICDFIVI LKRRPPKEVI GFLNDIFDQF DTVIKRHDAY KVETTGETYM VASGVPNENE
GRHVFEVAEM SLEIRAISLS YTLENDKNYK LRVRIGFHAG PIAAGVIGIK NPRYCLFGDT
VNFASRMQSN CPPLQIQTSE ITARMLLATH EYKLVKRGIV HVKGKGEVNC YWLNEHIHKD
EEIEESGTIS HPLES
