PDE7B_MOUSE
ID PDE7B_MOUSE Reviewed; 446 AA.
AC Q9QXQ1; A1L3T2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 7B;
DE EC=3.1.4.53 {ECO:0000269|PubMed:10872825};
GN Name=Pde7b {ECO:0000303|PubMed:10618442, ECO:0000312|MGI:MGI:1352752};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10618442; DOI=10.1073/pnas.97.1.472;
RA Hetman J.M., Soderling S.H., Glavas N.A., Beavo J.A.;
RT "Cloning and characterization of PDE7B, a cAMP-specific
RT phosphodiesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:472-476(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=C57BL/6J;
RX PubMed=10872825; DOI=10.1006/bbrc.2000.2743;
RA Gardner C.E., Robas N.M., Cawkill D., Fidock M.D.;
RT "Cloning and characterisation of the human and mouse PDE7B, a novel cAMP-
RT specific nucleotide phosphodiesterase.";
RL Biochem. Biophys. Res. Commun. 272:186-192(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426 AND THR-445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes (PubMed:10872825).
CC May be involved in the control of cAMP-mediated neural activity and
CC cAMP metabolism in the brain (By similarity).
CC {ECO:0000250|UniProtKB:Q9NP56, ECO:0000269|PubMed:10872825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:10872825};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q13946};
CC Note=Binds 2 divalent metal cations per subunit (By similarity). Site 1
CC may preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions (By similarity).
CC {ECO:0000250|UniProtKB:Q13946};
CC -!- ACTIVITY REGULATION: Inhibited by dipyridamole, IBMX and SCH 51866.
CC Insensitive to zaprinast, rolipram, and milrinone.
CC {ECO:0000269|PubMed:10872825}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:10872825};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000305|PubMed:10872825}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {ECO:0000269|PubMed:10872825}.
CC -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC putative divalent metal sites and an N-terminal regulatory domain.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE7 subfamily. {ECO:0000305}.
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DR EMBL; AF190639; AAF25195.1; -; mRNA.
DR EMBL; AJ251859; CAB92530.1; -; mRNA.
DR EMBL; BC130267; AAI30268.1; -; mRNA.
DR CCDS; CCDS35859.1; -.
DR RefSeq; NP_001334295.1; NM_001347366.1.
DR RefSeq; NP_038903.3; NM_013875.6.
DR AlphaFoldDB; Q9QXQ1; -.
DR SMR; Q9QXQ1; -.
DR STRING; 10090.ENSMUSP00000020165; -.
DR iPTMnet; Q9QXQ1; -.
DR PhosphoSitePlus; Q9QXQ1; -.
DR MaxQB; Q9QXQ1; -.
DR PaxDb; Q9QXQ1; -.
DR PRIDE; Q9QXQ1; -.
DR ProteomicsDB; 287904; -.
DR Antibodypedia; 19754; 289 antibodies from 30 providers.
DR DNASU; 29863; -.
DR Ensembl; ENSMUST00000020165; ENSMUSP00000020165; ENSMUSG00000019990.
DR GeneID; 29863; -.
DR KEGG; mmu:29863; -.
DR UCSC; uc007eoa.2; mouse.
DR CTD; 27115; -.
DR MGI; MGI:1352752; Pde7b.
DR VEuPathDB; HostDB:ENSMUSG00000019990; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000159413; -.
DR InParanoid; Q9QXQ1; -.
DR OMA; YPPIDLR; -.
DR PhylomeDB; Q9QXQ1; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.53; 3474.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR UniPathway; UPA00762; UER00747.
DR BioGRID-ORCS; 29863; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Pde7b; mouse.
DR PRO; PR:Q9QXQ1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9QXQ1; protein.
DR Bgee; ENSMUSG00000019990; Expressed in caudate-putamen and 203 other tissues.
DR ExpressionAtlas; Q9QXQ1; baseline and differential.
DR Genevisible; Q9QXQ1; MM.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:MGI.
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:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
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 1: Evidence at protein level;
KW cAMP; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..446
FT /note="cAMP-specific 3',5'-cyclic phosphodiesterase 7B"
FT /id="PRO_0000198837"
FT DOMAIN 97..420
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 422..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 323
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 446 AA; 51337 MW; 7C052664B693A5A8 CRC64;
MSCLMVERCG EVLFESPEQS VKCVCMLGDV RLRGQTGVPA ERRGSYPFID FRLLNNTTHS
GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED YLGQARHMLS KVGTWDFDIF
LFDRLTNGNS LVTLLCHLFN SHGLIHHFKL DMVTLHRFLV MVQEDYHGHN PYHNAVHAAD
VTQAMHCYLK EPKLASFLTP LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS
VLENHHWRST IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN
KDLRLENVQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGD LEQKFELEIS
PLCNQQKDSI PSIQIGFMTY IVEPLFREWA RFTGNSTLSE NMLSHLAHNK AQWKSLLSNQ
HRRRGSGQDL AGPAPETLEQ TEGATP
