PDE1_CAEEL
ID PDE1_CAEEL Reviewed; 664 AA.
AC O18696;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable 3',5'-cyclic phosphodiesterase pde-1;
DE EC=3.1.4.17;
GN Name=pde-1; ORFNames=T04D3.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP INTERACTION WITH CMD-1.
RX PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
RA Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C., Liu R.;
RT "Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
RL Cell Calcium 43:444-456(2008).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27062922; DOI=10.1016/j.cell.2016.03.026;
RA Singhvi A., Liu B., Friedman C.J., Fong J., Lu Y., Huang X.Y., Shaham S.;
RT "A glial K/Cl transporter controls neuronal receptive ending shape by
RT chloride inhibition of an rGC.";
RL Cell 165:936-948(2016).
CC -!- FUNCTION: Redundantly with pde-5, plays a role in the AFD thermosensory
CC neurons to regulate microvilli receptive ending morphology, possibly by
CC regulating cGMP levels. {ECO:0000269|PubMed:27062922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000250};
CC -!- SUBUNIT: Interacts with cmd-1 in the presence of Ca(2+).
CC {ECO:0000269|PubMed:17854888}.
CC -!- TISSUE SPECIFICITY: Expressed in AFD thermosensory neurons.
CC {ECO:0000269|PubMed:27062922}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; Z81114; CAB03289.1; -; Genomic_DNA.
DR PIR; T24459; T24459.
DR RefSeq; NP_493343.1; NM_060942.3.
DR AlphaFoldDB; O18696; -.
DR SMR; O18696; -.
DR BioGRID; 38595; 1.
DR STRING; 6239.T04D3.3a; -.
DR EPD; O18696; -.
DR PaxDb; O18696; -.
DR EnsemblMetazoa; T04D3.3a.1; T04D3.3a.1; WBGene00011433.
DR GeneID; 173200; -.
DR KEGG; cel:CELE_T04D3.3; -.
DR UCSC; T04D3.3; c. elegans.
DR CTD; 173200; -.
DR WormBase; T04D3.3a; CE16340; WBGene00011433; pde-1.
DR eggNOG; KOG3688; Eukaryota.
DR GeneTree; ENSGT00940000157043; -.
DR InParanoid; O18696; -.
DR OMA; HHRWTMQ; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; O18696; -.
DR Reactome; R-CEL-111957; Cam-PDE 1 activation.
DR Reactome; R-CEL-418457; cGMP effects.
DR Reactome; R-CEL-418555; G alpha (s) signalling events.
DR PRO; PR:O18696; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00011433; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; O18696; baseline and differential.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:WormBase.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:WormBase.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IPI:WormBase.
DR GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007635; P:chemosensory behavior; IGI:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:UniProtKB.
DR GO; GO:0032528; P:microvillus organization; IGI:WormBase.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IDA:WormBase.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IGI:WormBase.
DR GO; GO:0007602; P:phototransduction; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IGI:WormBase.
DR GO; GO:0010446; P:response to alkaline pH; IGI:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IGI:UniProtKB.
DR GO; GO:0070482; P:response to oxygen levels; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR InterPro; IPR013706; PDEase_N.
DR Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; cGMP; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..664
FT /note="Probable 3',5'-cyclic phosphodiesterase pde-1"
FT /id="PRO_0000198844"
FT DOMAIN 256..634
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 24..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 74855 MW; 33436A301328201E CRC64;
MNRARKTSSC GCFRSAFCLL KPSTSSASEE HGDSDKKLLS VQLITPRDEE EQTSSRSIKI
PPLDLNGLDC KKNAVAARRA GRRRTSEGGG VRGKGHFAEV VLDGLQRPVS LLRNQKEKSN
SDDNCQEKEP TSPSSSRKKS YDNAPALESL EKLRYILHQL NSGQLPLEDL KRNIEYAALV
LETAYMDETR RICDEDDDLA EVTPETVPDE VREWLAATFT RQNAGKKRDK PKFKSVANAI
RTGIFFEKLF RKQQVVQCPI PPEIAELMKE VCTWSFSPFQ LNEVSEGHAL KYVGFELFNR
YGFMDRFKVP LTALENYLSA LEVGYSKHNN PYHNVVHAAD VTQSSHFMLS QTGLANSLGD
LELLAVLFGA LIHDYEHTGH TNNFHIQSQS QFAMLYNDRS VLENHHVSSC FRLMKEDDKN
ILTHLTRDEY KELRNMVIEI VLATDMSTHF MQIKTMKSML SLPEGIDKNK ALCLIVHACD
ISHPAKPWNL HERWTEGVLE EFFRQGDLEA SMGLPYSPLC DRHTVHVADS QIGFIDFIVE
PTMVVCGELL VKMVEPLVSL PPTDSLFPPS VDGGDDKSPS NALSPLPDLR NSSTSPSSIR
RIPLNYAGKL DIPTPWMKFL HENKAHWKER AAKEEEERKI KEAAEAEAAA KQVEENKENG
VTTN
