ID U4PM84_CAEEL Unreviewed; 593 AA.
AC U4PM84;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=pde-3 {ECO:0000313|EMBL:CDH93184.1,
GN ECO:0000313|WormBase:E01F3.1g};
GN ORFNames=CELE_E01F3.1 {ECO:0000313|EMBL:CDH93184.1}, E01F3.1
GN {ECO:0000313|WormBase:E01F3.1g};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CDH93184.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CDH93184.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CDH93184.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
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:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|ARBA:ARBA00007648, ECO:0000256|RuleBase:RU363067}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284602; CDH93184.1; -; Genomic_DNA.
DR RefSeq; NP_001293569.1; NM_001306640.1.
DR AlphaFoldDB; U4PM84; -.
DR SMR; U4PM84; -.
DR EnsemblMetazoa; E01F3.1g.1; E01F3.1g.1; WBGene00008443.
DR GeneID; 183981; -.
DR AGR; WB:WBGene00008443; -.
DR WormBase; E01F3.1g; CE48904; WBGene00008443; pde-3.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008443; Expressed in larva and 3 other cell types or tissues.
DR ExpressionAtlas; U4PM84; baseline and differential.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 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 PANTHER; PTHR11347:SF179; 3',5'-CYCLIC PHOSPHODIESTERASE PDE-3-RELATED; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Proteomics identification {ECO:0007829|PeptideAtlas:U4PM84};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 181..532
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 123..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 256..260
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 322
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 431
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 482
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 593 AA; 66830 MW; 2337DA1989F5BE07 CRC64;
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 PLDSDLSQVP FTICCSIAEE EYV
//
