ID PDE5_CAEEL Reviewed; 728 AA.
AC P91119;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Probable 3',5'-cyclic phosphodiesterase pde-5;
DE EC=3.1.4.17;
GN Name=pde-5; ORFNames=C32E12.2;
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 FUNCTION.
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-1, 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 -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; FO080144; CCD61583.1; -; Genomic_DNA.
DR PIR; T25590; T25590.
DR RefSeq; NP_491544.3; NM_059143.3.
DR AlphaFoldDB; P91119; -.
DR SMR; P91119; -.
DR BioGRID; 47958; 1.
DR STRING; 6239.C32E12.2.1; -.
DR EPD; P91119; -.
DR PaxDb; 6239-C32E12-2; -.
DR PeptideAtlas; P91119; -.
DR EnsemblMetazoa; C32E12.2.1; C32E12.2.1; WBGene00016328.
DR GeneID; 183125; -.
DR KEGG; cel:CELE_C32E12.2; -.
DR UCSC; C32E12.2; c. elegans.
DR AGR; WB:WBGene00016328; -.
DR WormBase; C32E12.2; CE45692; WBGene00016328; pde-5.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156543; -.
DR HOGENOM; CLU_006980_1_1_1; -.
DR InParanoid; P91119; -.
DR OMA; HNWAHGW; -.
DR OrthoDB; 5479253at2759; -.
DR PhylomeDB; P91119; -.
DR Reactome; R-CEL-418457; cGMP effects.
DR Reactome; R-CEL-418555; G alpha (s) signalling events.
DR PRO; PR:P91119; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00016328; Expressed in pharyngeal muscle cell (C elegans) and 2 other cell types or tissues.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; ISS:WormBase.
DR GO; GO:0004118; F:cGMP-stimulated 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:0032528; P:microvillus organization; IGI:WormBase.
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; 3.30.450.40; -; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 PANTHER; PTHR11347:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cGMP; Coiled coil; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..728
FT /note="Probable 3',5'-cyclic phosphodiesterase pde-5"
FT /id="PRO_0000198848"
FT DOMAIN 214..371
FT /note="GAF"
FT DOMAIN 390..709
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 708..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 691..728
FT /evidence="ECO:0000255"
FT ACT_SITE 465
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 614
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 728 AA; 83227 MW; 7C28EC4EEEC16D85 CRC64;
MDDASVLKYL QENPKLVEDF VVSNEISPET FKRWAVRRTM KYKNVKNGTS GGTGAWTEPD
LSMKRRVILE TSDNRTRILY EITQCCGQLI GTNSIELIVQ NDEGAFSCRK TENGELKLKK
VKTSKSADYI QTIVNAGNQT IAEIHFYTQL DSTEKSIVNA VCTWAAATNY YSELYTHKQE
GSDGQDIHEN IAKQRKLSNF LLDVARSIFH DIVSMDAVII KVMNFAQKLV DADRASLFLV
DSKNAQIYAR IFDVGTGDEE HVRVNSEGQK EIRFDMSKGI AGYVASTGEG LNIENAYEDE
RFNADVDSKT GYTTKTILCM PILIRGIVIG VVQMVNKHDG VFTRQDEDAF EIFAVYCGLA
LHHAKLYDKI RRSEQKYRVA LEVLAYHSVC NADEVNKLKK IEINNRIVEL ETIDFNGMRL
SELEKPLYAV YMFKTLFADT LRFDTEDLIR FVLTVRKNYR RVAYHNWAHG WSVAHAMFAT
LMNSPDAFTK LEALALYVSC LCHDLDHRGK NNAYMKTMST PLASIYSTSV MERHHFNQTV
TILQQDGHNI LKSLSSEDYK KTLSLIKHCI LATDLALFFS NKAKLNVILD NNTFDINRQE
HRLLTQAVMM TGCDLVASAK PWNIQTETVK VIFEEFYDQG DAERLSGKEP IPMMDRQQAH
MLPQMQVGFM RGICMPCYDL IARIFPKNDK MRERCEYNAK KWEELAEEQR KKQEALAQQN
GEANETQE
//
