GCY17_CAEEL
ID GCY17_CAEEL Reviewed; 1088 AA.
AC X5M8U1; X5LV47;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Receptor-type guanylate cyclase gcy-17 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-17 {ECO:0000312|WormBase:W03F11.2a};
GN ORFNames=W03F11.2 {ECO:0000312|WormBase:W03F11.2a};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:W03F11.2a};
CC IsoId=X5M8U1-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:W03F11.2b};
CC IsoId=X5M8U1-2; Sequence=VSP_057705;
CC -!- TISSUE SPECIFICITY: Expressed in PHA 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; BX284601; CDO41084.1; -; Genomic_DNA.
DR EMBL; BX284601; CDO41085.1; -; Genomic_DNA.
DR RefSeq; NP_001293327.1; NM_001306398.1. [X5M8U1-1]
DR RefSeq; NP_001293328.1; NM_001306399.1. [X5M8U1-2]
DR AlphaFoldDB; X5M8U1; -.
DR SMR; X5M8U1; -.
DR STRING; 6239.W03F11.2; -.
DR PaxDb; X5M8U1; -.
DR EnsemblMetazoa; W03F11.2a.1; W03F11.2a.1; WBGene00001542. [X5M8U1-1]
DR EnsemblMetazoa; W03F11.2b.1; W03F11.2b.1; WBGene00001542. [X5M8U1-2]
DR GeneID; 191649; -.
DR KEGG; cel:CELE_W03F11.2; -.
DR CTD; 191649; -.
DR WormBase; W03F11.2a; CE49683; WBGene00001542; gcy-17. [X5M8U1-1]
DR WormBase; W03F11.2b; CE49714; WBGene00001542; gcy-17. [X5M8U1-2]
DR eggNOG; KOG1023; Eukaryota.
DR OMA; FRISHMP; -.
DR OrthoDB; 229634at2759; -.
DR PRO; PR:X5M8U1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001542; 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; 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 Alternative splicing; Cell membrane; cGMP biosynthesis; Coiled coil;
KW Glycoprotein; GTP-binding; Lyase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1088
FT /note="Receptor-type guanylate cyclase gcy-17"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433285"
FT TOPO_DOM 21..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 535..824
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 882..1012
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 529..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 826..854
FT /evidence="ECO:0000255"
FT COMPBIAS 534..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 569..571
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057705"
SQ SEQUENCE 1088 AA; 122824 MW; CC000D9290BCB398 CRC64;
MLFLRLFIFT PFLILANCQA RRTIKVGLLF VQNVSSLQVG IGYRTSAAAV LVTKNKIRED
HVLDGFDFEF LWDFDECNEI LGAGKTVDLL EVKKVDVIFG PTCSRPALIS SALATYYNIP
IFEWGLTSTR QLTDVKRFPT TLPFSVNSYS LAMAILGTLK QFQWTEFVFL YCNDGDDEKC
ESLKDDVQTV ASAHEELSLA YTFRIQSKKL EDMRAAIVEI KKRGRIIVAC VASGNGSKRT
LMQAVALENA NNSEYVYIMA ETNSRGFVVE EVGGKWHYLW EGKFDDSDTF STEDSRTSMA
NLLFLVDNMG MNNVVTPQYL NFSKNVIEMM KDEPFNCVED CVGEEYSSVA KYAGQLADAF
YAYAVAVNRL LTANPQAEIR NGTMILRNIG MTFEGVGGGD LTVDPDSART SEIIMIGLNS
SRLPETYGKL IINNQSVHFE QLYSDEVMDV WNGRQRPKAK PTCGFTGTQC PPDFVRDYLV
IVIIIVMFLI FAVSAAVGAV FYAIRQKRKE IERQDELWHV EASHLKPISK KSKSEASQRS
FASGPSTSTK LTVESRTETT RFIFYIYQVR NNEVVAANKH DFRPQLTDVE RSELRQMRSL
DHDNLNKFIG LCLNSQQLLS IWRYCSRGSL ADVISRSSMQ MDSFFMLSLI RDIANGLGFI
HTSMLHFHGY LSSRSCLIDD RWQVKISDFG LNEVRGMDKL STENMLWWAP EVLRGLEQRS
KEADIYSFGI ICSEVITRSS AFDLENRKEK PEEIIYQLKK GGFNAIRPSL LTDEALEINP
ALVHLIRDCW TEKPSERPPI DQVRSLLRGM NDGKKGNLMD HVFNMLETYA STLEEEVNER
TKELVEEQKK SDVLLYRMLP KTVAEKLKAG ISIEPETFEL VTIFFSDVVQ FTTLASKCTP
LQVVQLLNDL YTIFDSIIEQ NDVYKVETIG DGYLCVSGLP HRNGHDHIKH IARMSLAFLS
SLAEFRVAHM PSERINLRIG INCGSVVAGV VGLTMPRYCL FGDAVNTASR MESNGKPGRI
HVSSEANHLL THVVGGFRTE ERGEVIIKGK GVMNTYWLLG ENDSVPVKSN MRKRENTPSM
ARSITPEI
