PDE4_CAEEL
ID PDE4_CAEEL Reviewed; 674 AA.
AC Q22000; Q86NE7; Q86NE8; Q86NE9; Q8IFZ3; Q95ZQ6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable 3',5'-cyclic phosphodiesterase pde-4;
DE EC=3.1.4.17;
GN Name=pde-4; ORFNames=R153.1;
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).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=29033363; DOI=10.1016/j.devcel.2017.09.013;
RA Yu B., Wang X., Wei S., Fu T., Dzakah E.E., Waqas A., Walthall W.W.,
RA Shan G.;
RT "Convergent Transcriptional Programs Regulate cAMP Levels in C. elegans
RT GABAergic Motor Neurons.";
RL Dev. Cell 43:212-226(2017).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes (By similarity).
CC Antagonizes dorsal D (DD) motor neuron respecification by reducing
CC levels of cAMP (PubMed:29033363). {ECO:0000250|UniProtKB:P27815,
CC ECO:0000269|PubMed:29033363}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=d;
CC IsoId=Q22000-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q22000-2; Sequence=VSP_014345, VSP_014352;
CC Name=b;
CC IsoId=Q22000-3; Sequence=VSP_014347, VSP_014350;
CC Name=c;
CC IsoId=Q22000-4; Sequence=VSP_014346, VSP_014351;
CC Name=e;
CC IsoId=Q22000-5; Sequence=VSP_014348, VSP_014349;
CC Name=f;
CC IsoId=Q22000-6; Sequence=VSP_014353, VSP_014354;
CC -!- TISSUE SPECIFICITY: Expressed in dorsal D (DD) motor neurons and
CC several other neurons at the L1 stage. Expression in DD neurons
CC decreases gradually beginning in the late L1 stage. Highly expressed in
CC adult ventral D (VD) motor neurons, but diminished in adult DD motor
CC neurons. {ECO:0000269|PubMed:29033363}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; FO081170; CCD69643.1; -; Genomic_DNA.
DR EMBL; FO081170; CCD69647.1; -; Genomic_DNA.
DR EMBL; FO081170; CCD69649.1; -; Genomic_DNA.
DR EMBL; FO081170; CCD69644.1; -; Genomic_DNA.
DR EMBL; FO081170; CCD69648.1; -; Genomic_DNA.
DR EMBL; FO081170; CCD69645.1; -; Genomic_DNA.
DR PIR; T16769; T16769.
DR RefSeq; NP_495600.1; NM_063199.3. [Q22000-5]
DR RefSeq; NP_495601.1; NM_063200.1. [Q22000-2]
DR RefSeq; NP_871944.1; NM_182144.3. [Q22000-4]
DR RefSeq; NP_871945.1; NM_182145.3. [Q22000-1]
DR RefSeq; NP_871946.1; NM_182146.3.
DR RefSeq; NP_871947.1; NM_182147.3. [Q22000-6]
DR AlphaFoldDB; Q22000; -.
DR SMR; Q22000; -.
DR BioGRID; 39569; 2.
DR STRING; 6239.R153.1d; -.
DR EPD; Q22000; -.
DR PaxDb; Q22000; -.
DR PeptideAtlas; Q22000; -.
DR EnsemblMetazoa; R153.1a.1; R153.1a.1; WBGene00020114. [Q22000-2]
DR EnsemblMetazoa; R153.1b.1; R153.1b.1; WBGene00020114. [Q22000-5]
DR EnsemblMetazoa; R153.1c.1; R153.1c.1; WBGene00020114. [Q22000-4]
DR EnsemblMetazoa; R153.1d.1; R153.1d.1; WBGene00020114. [Q22000-1]
DR EnsemblMetazoa; R153.1e.1; R153.1e.1; WBGene00020114. [Q22000-3]
DR EnsemblMetazoa; R153.1e.2; R153.1e.2; WBGene00020114. [Q22000-3]
DR EnsemblMetazoa; R153.1f.1; R153.1f.1; WBGene00020114. [Q22000-6]
DR GeneID; 174235; -.
DR UCSC; R153.1b; c. elegans. [Q22000-1]
DR CTD; 174235; -.
DR WormBase; R153.1a; CE02038; WBGene00020114; pde-4. [Q22000-2]
DR WormBase; R153.1b; CE28641; WBGene00020114; pde-4. [Q22000-5]
DR WormBase; R153.1c; CE32060; WBGene00020114; pde-4. [Q22000-4]
DR WormBase; R153.1d; CE33438; WBGene00020114; pde-4. [Q22000-1]
DR WormBase; R153.1e; CE33439; WBGene00020114; pde-4. [Q22000-3]
DR WormBase; R153.1f; CE33440; WBGene00020114; pde-4. [Q22000-6]
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_005940_8_0_1; -.
DR InParanoid; Q22000; -.
DR OMA; LQAENCN; -.
DR OrthoDB; 1783517at2759; -.
DR PhylomeDB; Q22000; -.
DR Reactome; R-CEL-180024; DARPP-32 events.
DR Reactome; R-CEL-418555; G alpha (s) signalling events.
DR PRO; PR:Q22000; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00020114; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q22000; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
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:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006198; P:cAMP catabolic process; ISS:WormBase.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:WormBase.
DR GO; GO:0040013; P:negative regulation of locomotion; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0030431; P:sleep; IMP:WormBase.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR040844; PDE4_UCR.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF18100; PDE4_UCR; 1.
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 2: Evidence at transcript level;
KW Alternative splicing; cAMP; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..674
FT /note="Probable 3',5'-cyclic phosphodiesterase pde-4"
FT /id="PRO_0000198847"
FT DOMAIN 328..660
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_014345"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_014346"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014347"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_014348"
FT VAR_SEQ 49..91
FT /note="SRTPPAALPPRTSAVTIPGSNHKLTSSASSYHPPRELTVSTFS -> MCGSR
FT RHLRRNEDGMNGVARRKQFKLRPWQSTALPSRHDHYSC (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_014349"
FT VAR_SEQ 63..91
FT /note="VTIPGSNHKLTSSASSYHPPRELTVSTFS -> MNGVARRKQFKLRPWQSTA
FT LPSRHDHYSC (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014350"
FT VAR_SEQ 76..90
FT /note="ASSYHPPRELTVSTF -> MTSRRHTVWFVPGSR (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_014351"
FT VAR_SEQ 126..150
FT /note="SDDLREASSLRPVSRASSIASNEHG -> MSISLINNNNRSVRRKFGESGFT
FT LR (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_014352"
FT VAR_SEQ 151..158
FT /note="HGDDLIVT -> YVILYIFL (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_014353"
FT VAR_SEQ 159..674
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_014354"
SQ SEQUENCE 674 AA; 75389 MW; 87BA310BE45DBD30 CRC64;
MPRRRGSSSS SSAAGGSGGG GGFGFSSLRR ELHLHNFFRT SSPSASSTSR TPPAALPPRT
SAVTIPGSNH KLTSSASSYH PPRELTVSTF SAGSATAADG LGGAHLTPSL SSSVHARRES
FLYRASDDLR EASSLRPVSR ASSIASNEHG HGDDLIVTPF AQLLASLRNV RSNLISITNI
QNSDDSRHAN RSAKRPPLHN IELPDDVVHC AHDTLEELDW CLDQLETIQT HRSVSEMASS
KFRKMLNKEL SHFAESSKSG TQVSKFLITT YMDKEEDEPS IEIEVPTEVQ GPSTSGPMTL
SILKKAQTAA MNKISGVRKL RAPSHDGHVP EYGVNCAREI AVHMQRLDDW GPDVFKIDEL
SKNHSLTVVT FSLLRQRNLF KTFEIHQSTL VTYLLNLEHH YRNNHYHNFI HAADVAQSMH
VLLMSPVLTE VFTDLEVLAA IFAGAVHDVD HPGFTNQYLI NSNNELAIMY NDESVLEQHH
LAVAFKLLQD SNCDFLANLS RKQRLQFRKI VIDMVLATDM SKHMSLLADL KTMVEAKKVA
GNNVIVLDKY NDKIQVLQSM IHLADLSNPT KPIELYQQWN QRIMEEYWRQ GDKEKELGLE
ISPMCDRGNV TIEKSQVGFI DYIVHPLYET WADLVYPDAQ NILDQLEENR EWYQSRIPEE
PDTARTVTED DEHK
