PDE3_CAEEL
ID PDE3_CAEEL Reviewed; 678 AA.
AC Q8I0P7; B7FAS9; B7FAT0; G5EG24; Q9BH44;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 4.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable 3',5'-cyclic phosphodiesterase pde-3;
DE EC=3.1.4.17;
GN Name=pde-3; ORFNames=E01F3.1;
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], AND ALTERNATIVE SPLICING.
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).
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 Evidence={ECO:0000250|UniProtKB:P54750};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=e;
CC IsoId=Q8I0P7-1; Sequence=Displayed;
CC Name=a {ECO:0000303|PubMed:9851916};
CC IsoId=Q8I0P7-2; Sequence=VSP_053658, VSP_053664, VSP_053665;
CC Name=b;
CC IsoId=Q8I0P7-3; Sequence=VSP_053661;
CC Name=c;
CC IsoId=Q8I0P7-4; Sequence=VSP_053660, VSP_053662, VSP_053665;
CC Name=d;
CC IsoId=Q8I0P7-5; Sequence=VSP_053659, VSP_053663, VSP_053665;
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000250|UniProtKB:P54750}.
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DR EMBL; Z93376; CAB07570.3; -; Genomic_DNA.
DR EMBL; AL132949; CAB07570.3; JOINED; Genomic_DNA.
DR EMBL; Z93376; CAD59146.3; -; Genomic_DNA.
DR EMBL; Z82279; CAD59146.3; JOINED; Genomic_DNA.
DR EMBL; AL132949; CAD59146.3; JOINED; Genomic_DNA.
DR EMBL; Z93376; CAT01013.1; -; Genomic_DNA.
DR EMBL; AL132949; CAT01013.1; JOINED; Genomic_DNA.
DR EMBL; Z93376; CAT01014.1; -; Genomic_DNA.
DR EMBL; AL132949; CAT01014.1; JOINED; Genomic_DNA.
DR EMBL; Z93376; CBL43431.1; -; Genomic_DNA.
DR EMBL; AL132949; CBL43431.1; JOINED; Genomic_DNA.
DR EMBL; Z82279; CBL43431.1; JOINED; Genomic_DNA.
DR PIR; T20399; T20399.
DR RefSeq; NP_001254452.1; NM_001267523.1. [Q8I0P7-4]
DR RefSeq; NP_001254453.1; NM_001267524.1.
DR RefSeq; NP_001254454.1; NM_001267525.1. [Q8I0P7-5]
DR RefSeq; NP_497084.2; NM_064683.5. [Q8I0P7-2]
DR RefSeq; NP_871943.3; NM_182143.3.
DR AlphaFoldDB; Q8I0P7; -.
DR SMR; Q8I0P7; -.
DR BioGRID; 48784; 1.
DR IntAct; Q8I0P7; 1.
DR STRING; 6239.E01F3.1i; -.
DR EPD; Q8I0P7; -.
DR PaxDb; Q8I0P7; -.
DR PeptideAtlas; Q8I0P7; -.
DR EnsemblMetazoa; E01F3.1a.1; E01F3.1a.1; WBGene00008443. [Q8I0P7-2]
DR EnsemblMetazoa; E01F3.1b.1; E01F3.1b.1; WBGene00008443. [Q8I0P7-3]
DR EnsemblMetazoa; E01F3.1c.1; E01F3.1c.1; WBGene00008443. [Q8I0P7-4]
DR EnsemblMetazoa; E01F3.1d.1; E01F3.1d.1; WBGene00008443. [Q8I0P7-5]
DR EnsemblMetazoa; E01F3.1e.1; E01F3.1e.1; WBGene00008443. [Q8I0P7-1]
DR GeneID; 183981; -.
DR UCSC; E01F3.1b; c. elegans. [Q8I0P7-1]
DR CTD; 183981; -.
DR WormBase; E01F3.1a; CE32847; WBGene00008443; pde-3. [Q8I0P7-2]
DR WormBase; E01F3.1b; CE43375; WBGene00008443; pde-3. [Q8I0P7-3]
DR WormBase; E01F3.1c; CE43353; WBGene00008443; pde-3. [Q8I0P7-4]
DR WormBase; E01F3.1d; CE43321; WBGene00008443; pde-3. [Q8I0P7-5]
DR WormBase; E01F3.1e; CE44810; WBGene00008443; pde-3. [Q8I0P7-1]
DR eggNOG; KOG3688; Eukaryota.
DR InParanoid; Q8I0P7; -.
DR OMA; CYYLTCH; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q8I0P7; -.
DR Reactome; R-CEL-165160; PDE3B signalling.
DR Reactome; R-CEL-418555; G alpha (s) signalling events.
DR PRO; PR:Q8I0P7; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008443; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q8I0P7; baseline and differential.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide 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:0043951; P:negative regulation of cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IGI:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
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: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 Pfam; PF00233; PDEase_I; 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 3: Inferred from homology;
KW Alternative splicing; cGMP; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..678
FT /note="Probable 3',5'-cyclic phosphodiesterase pde-3"
FT /id="PRO_0000198846"
FT DOMAIN 281..632
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 356
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 360
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 421
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 422
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 422
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT BINDING 531
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT VAR_SEQ 1..221
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_053658"
FT VAR_SEQ 1..186
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_053659"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053660"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053661"
FT VAR_SEQ 105..201
FT /note="HMQRTFHEAMRQRRTSLPANSLSLNGAKVTGSSLSEAKGLIADMLMNKELPG
FT NVASCLRAVTMLLEQRPLPLNGLLNDFGLPSVVENPYGGESMVVG -> MFPFRRSESH
FT SPASRCKSAGLPIATTNGFHSIPSSASSSTQSINRQGSVDNLIFKLLTKKYMAKCLGFT
FT PSRSSVAIQTTPVVEVAPVIGQQNEGDK (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053662"
FT VAR_SEQ 187..234
FT /note="SVVENPYGGESMVVGASKPRISNITFSTVTSATGLPTVPAEPNKARSS ->
FT MMSSPSTSRCGHGGVAPADANGKEIQPFGVLVVNKLQKRVNSPLTAFA (in
FT isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_053663"
FT VAR_SEQ 222..234
FT /note="PTVPAEPNKARSS -> MNSKVFKSKKNFC (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_053664"
FT VAR_SEQ 678
FT /note="Q -> QVPFTICCSIAEEEYV (in isoform a, isoform c and
FT isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_053665"
SQ SEQUENCE 678 AA; 75578 MW; D9548D666A154FF6 CRC64;
MSPGPPAVGG VSPPVMVPGS APPFQPTHQY FQHHYHQTPP GKLRDRSPRL SAEMRKNRDT
ATSSPASSGV SIQQRRGSTT QNSGVGSIGL PVLGGRGRGV MSDGHMQRTF HEAMRQRRTS
LPANSLSLNG AKVTGSSLSE AKGLIADMLM NKELPGNVAS CLRAVTMLLE QRPLPLNGLL
NDFGLPSVVE NPYGGESMVV GASKPRISNI TFSTVTSATG LPTVPAEPNK ARSSSYWKTE
ASPSNNNEHE TPVDLLRKIS VSRKESGTHV DTVVTTIDGQ RYDTRELDTD PDLAETAVWS
FPIFQMSRKH PQTILSRLTY NIFQQAELFR IFKVSPIKFF NFFHALEKGY WEIPYHNRIH
AADVLHGCYY LSAHPVRSTF LTPKTPDSVL TPPHPHHQHS SIMSQLSTLE LMALFTAAAM
HDYDHPGRTN AFLVQVEDKK AILYNDRSVL ENHHAAESWK LLNKPENHFI ENLDPAEMKR
FRYLVLEYIL ATDLKQHFEI IMTFTERLTE IDVQVETDRL LIGKLLIKMA DINSPTKPYG
LHRQWTDRIC EEFYEQGDDE RRRGLPITPY MDRGDAQVAK LQDSFIAHVV SPLATAMNEC
GLLPILPGLD TSELIINMEH NHRKWKEQIE LENGGSYEAQ ITCNGGTAVN GVIEEESAST
SDSPDPRRDS PLDSDLSQ
