GCY29_CAEEL
ID GCY29_CAEEL Reviewed; 1069 AA.
AC O62026;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Receptor-type guanylate cyclase gcy-29 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000250|UniProtKB:Q19187};
DE Flags: Precursor;
GN Name=gcy-29 {ECO:0000312|WormBase:C04H5.3};
GN ORFNames=C04H5.3 {ECO:0000312|WormBase:C04H5.3};
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 ASE and AFD 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; BX284602; CAB03842.3; -; Genomic_DNA.
DR PIR; T18931; T18931.
DR PIR; T18933; T18933.
DR RefSeq; NP_497026.2; NM_064625.4.
DR AlphaFoldDB; O62026; -.
DR STRING; 6239.C04H5.3; -.
DR PaxDb; O62026; -.
DR PRIDE; O62026; -.
DR EnsemblMetazoa; C04H5.3.1; C04H5.3.1; WBGene00007314.
DR UCSC; C04H5.3; c. elegans.
DR WormBase; C04H5.3; CE53989; WBGene00007314; gcy-29.
DR eggNOG; KOG1023; Eukaryota.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; O62026; -.
DR OMA; PIFAYTA; -.
DR OrthoDB; 172467at2759; -.
DR PhylomeDB; O62026; -.
DR PRO; PR:O62026; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007314; 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:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; 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; Glycoprotein; GTP-binding;
KW Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1069
FT /note="Receptor-type guanylate cyclase gcy-29"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433296"
FT TOPO_DOM 24..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 497..806
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 876..1006
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 503..511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 881
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 881
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 882
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 925
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 925
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 240
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 1069 AA; 121502 MW; D2598823C243F67B CRC64;
MLPNFWNFQF IFVIFCWIPI VVSDEKIVLK IGSISSRDNA KMLESILEMA KKKMTEQGVL
GEKLDIQIIT VEGCGASFEG VAAAAELYHV QKVDAYFGPY CSKELSPVAT MASYWNIPIF
AYTATSAEFA NTKVYKTLLR TSFQSLNSIS EATAAFMAHH NITKAAIVAN IGTDSFEKIQ
SLEKALRSRG ITVARRVMFE EAASAQDLVD NGYMNELRDN ARVILPIFSS TRDLSTVFRN
ATWLANMASP EFIYINPLIV ARNSEEPPVF YGKMAQKSIK AENPNTIQIY NSYGFSDDLL
NEFLAIFDQN QRIYIDEKDL FNYVALYESF CVFAKLTEKY LHSLKEKPED GKIRIDGKAL
WNMAVGMTFQ GVLDNVIFDN GAERMTSFSA FYVDEKRDQI RTVSLINSTV TSKNCMDPVC
IELVVSDVVT KFWSSPSGKL PDSEPECGFR EENCDYTQTI VIATAVVCII LTVFLGIWLR
RACETSALDK MPWRVFRDDV QILDEEQVKS VVSLNSASTK MSQVETKLIK NHAIVGVNTH
AVYDLYEQRQ NIRFTREDLI LLTKMKQAVH DNINPFIGVS FNEKSELLLL WKFCSRGTLQ
DVIYCEKFAM DEKFQGAFVR DITMGLEYLH SSPIGYHGGL ACWSVLIDKN WMLKLTDYAV
CDPLKRWEKH GRINCKVDNE AEKQWQKMAS LYVPPEIRTA NEKNRLKRMD QKWQGQTILK
RQQSDIYAFG VIIYEILFRS LPYDEKVDLT ELAQKAAEGD KIQKPSIQRN KKLNPDLIAL
LQDCWSDQPD MRPTIRRVRL ATEIALKTKG NLVDSMMRMM EEYANNLEKL VGERTKLAEE
ANLRAERLLF QLLPKHVAIE LKAGRTVAPK MYDSATVMFS DIVGFTKLCS ASTPIEVVNL
LNKLYSEFDT VISKHDCYKV ETIGDAYMVV SGIPIENGQR HVANISAVTL GIMDLLKVFE
VPHRRDYRLT IRLGFASGQV SAAVVGLSSP RYCLFGETVN IAAVMESSGE GGRVQITETS
KILLENEYPE FIIEIRGINK DVKQDDFVTY WLTGKDEDYF KKKNNTFDF
