PDE6_CAEEL
ID PDE6_CAEEL Reviewed; 760 AA.
AC Q9N2V9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable 3',5'-cyclic phosphodiesterase pde-6;
DE EC=3.1.4.17;
GN Name=pde-6; ORFNames=Y95B8A.10;
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).
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 -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000250|UniProtKB:P54750}.
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DR EMBL; FO081787; CCD73546.1; -; Genomic_DNA.
DR RefSeq; NP_490787.1; NM_058386.1.
DR AlphaFoldDB; Q9N2V9; -.
DR SMR; Q9N2V9; -.
DR BioGRID; 55379; 2.
DR IntAct; Q9N2V9; 1.
DR STRING; 6239.Y95B8A.10a; -.
DR iPTMnet; Q9N2V9; -.
DR EPD; Q9N2V9; -.
DR PaxDb; Q9N2V9; -.
DR PeptideAtlas; Q9N2V9; -.
DR EnsemblMetazoa; Y95B8A.10a.1; Y95B8A.10a.1; WBGene00022389.
DR UCSC; Y95B8A.10a; c. elegans.
DR WormBase; Y95B8A.10a; CE23151; WBGene00022389; pde-6.
DR eggNOG; KOG1229; Eukaryota.
DR HOGENOM; CLU_005940_4_2_1; -.
DR InParanoid; Q9N2V9; -.
DR OMA; CGGSYSE; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q9N2V9; -.
DR Reactome; R-CEL-418555; G alpha (s) signalling events.
DR PRO; PR:Q9N2V9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022389; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q9N2V9; baseline and differential.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; ISS:WormBase.
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:1900194; P:negative regulation of oocyte maturation; IMP:WormBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
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; IPR035965; PAS-like_dom_sf.
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 SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cGMP; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..760
FT /note="Probable 3',5'-cyclic phosphodiesterase pde-6"
FT /id="PRO_0000198849"
FT DOMAIN 426..750
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 760 AA; 84881 MW; 2BDD7274D30B34B5 CRC64;
MGDRSGVGGE EGEKSVLGAS AHSQAGRRQQ HTPAARRGAQ RAPAATAAAA SRPVFAMRWC
CGGSYSENGG GGGGSRGAPP TPLLTVAATS SSTAHDTFGP MQVKMLKTAV IVTEGTGESV
LLDSLRASGW ICTVSFPTQA TSDVESICPL AVFIDLRVPH PSQIAKDVSS VSTEEVLIVS
IAEKHISEKR RRALAQSNII HHVTWNTRDV VLFDYVGRLA NRIRALPALF AVLDETDQAV
EICDEQRVVQ YVNRAYENVT GCIRSEVIGQ PESEMRRKSL PRARGEEERR RSCDWKFIRV
PFANNSQFVY MKRSNTTGDT AAIFRDVSLK SLKSQTGGIE APISEVLTML RDVSARVDGE
PAQTIKDAMK VLSSHELYAP SINRFRDADR IATQYYDGLI RLHHPARQRK RSVVDAHREK
RGSHGERRRV SADVKNALEN DNCWKFDILH LEKVSDHHAL SQVGMKVFER WKVCDVLGCS
DDLLHRWILS IEAHYHAGNT YHNATHAADV LQATSFFLDS PSVAVHVNES HAVAALLAAA
VHDLDHPGRG NAYLINTRQS LAILYNDNSI LENHHIALAF QLTLQHNANV NIFSSLSREE
FIQMRHAMVE MVLATDISRH FEYLAKFNKM HVTDVPEEQR DTNSLTICDM LVKCADISNP
AREWGLCQRW AHRIVEEYFE QTREEKEKGL PVTMEVFDRN TCNVPITQCG FIDMFAREAF
ATFTEFAKLG ELSDQLESNY EKWKVMTSQW TPTHNTNLVL
