PDE8B_MOUSE
ID PDE8B_MOUSE Reviewed; 865 AA.
AC E9Q4S1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B;
DE Short=PDE8B;
DE EC=3.1.4.53;
DE AltName: Full=Cell proliferation-inducing gene 22 protein;
GN Name=Pde8b;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=18431404; DOI=10.1038/ejhg.2008.85;
RA Horvath A., Giatzakis C., Tsang K., Greene E., Osorio P., Boikos S.,
RA Libe R., Patronas Y., Robinson-White A., Remmers E., Bertherat J.,
RA Nesterova M., Stratakis C.A.;
RT "A cAMP-specific phosphodiesterase (PDE8B) that is mutated in adrenal
RT hyperplasia is expressed widely in human and mouse tissues: a novel PDE8B
RT isoform in human adrenal cortex.";
RL Eur. J. Hum. Genet. 16:1245-1253(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497; SER-731 AND SER-734, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Testis;
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. May be involved in
CC specific signaling in the thyroid gland (By similarity). {ECO:0000250}.
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 -!- 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 -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:18431404}.
CC -!- DEVELOPMENTAL STAGE: Detectable in the adrenal gland of newborn
CC animals. {ECO:0000269|PubMed:18431404}.
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 PDE8 subfamily. {ECO:0000305}.
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DR EMBL; AC123034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC147108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E9Q4S1; -.
DR SMR; E9Q4S1; -.
DR iPTMnet; E9Q4S1; -.
DR PhosphoSitePlus; E9Q4S1; -.
DR SwissPalm; E9Q4S1; -.
DR MaxQB; E9Q4S1; -.
DR PaxDb; E9Q4S1; -.
DR PRIDE; E9Q4S1; -.
DR ProteomicsDB; 287905; -.
DR Ensembl; ENSMUST00000067082; ENSMUSP00000070465; ENSMUSG00000021684.
DR MGI; MGI:2443999; Pde8b.
DR VEuPathDB; HostDB:ENSMUSG00000021684; -.
DR eggNOG; KOG1229; Eukaryota.
DR GeneTree; ENSGT00940000157817; -.
DR InParanoid; E9Q4S1; -.
DR OMA; NIVQFLN; -.
DR PhylomeDB; E9Q4S1; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR UniPathway; UPA00762; UER00747.
DR ChiTaRS; Pde8b; mouse.
DR PRO; PR:E9Q4S1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; E9Q4S1; protein.
DR Bgee; ENSMUSG00000021684; Expressed in olfactory tubercle and 222 other tissues.
DR ExpressionAtlas; E9Q4S1; baseline and differential.
DR Genevisible; E9Q4S1; 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:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0090032; P:negative regulation of steroid hormone biosynthetic process; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0035106; P:operant conditioning; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR000014; PAS.
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 InterPro; IPR013938; PDEase_PDE8.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF08629; PDE8; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50112; PAS; 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..865
FT /note="High affinity cAMP-specific and IBMX-insensitive
FT 3',5'-cyclic phosphodiesterase 8B"
FT /id="PRO_0000414225"
FT DOMAIN 247..318
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 519..855
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 17..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 595
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 599
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60658"
FT BINDING 635
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60658"
FT BINDING 636
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60658"
FT BINDING 636
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O60658"
FT BINDING 761
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O60658"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 865 AA; 96739 MW; D1ED48083F1DE072 CRC64;
MGCAPSIHVS QSGVIYCRDS DESNSPRQTS SVSQGPTAPL HGLFVQTDAA DAMPPSRAAG
PPGAVRVRRS RAELGSGSST GSSGPATTTC RGRRRHCCSS AEAETQTSYT SVKVLLIFAK
EDSQSDGFWW ACDRAGYRCN IARTPESALE CFLDKHHEII VIDHRQSRNF DAEAVCRSIR
ATNPSEHTVI LAVVSQASDD HEEASVLPLL HAGFNRRFME NSSIIACYNE LIQIEHGEVR
SQFKLRACNS VFTALDHCHE AIEITSDDHV IQYVNPAFER MMGYHKGELL GKELADLPKS
DKNRADLLDT INTCIKKGKE WQGVYYARRK SGDSIQQHVK ITPVIGQGGK IRHFVSLKKL
CCTTDSNKQI HRIHRDSGDN SQTEPHSFRH KSRRKESIDV KSISSRGSDA PSLQNRRYPS
MARIHSMTIE APITKVINII NAAQENSPVT VAEALDRVLE ILRTTELYSP QLGTKDEDPH
TSDLVGGLMT DGLRRLSGNE YVFTKNVHHS HSHLSMPITI NDVPPSIAQL LDNEESWDFN
IFELEAVTHK RPLVYLGLKV FSRFGVCEFL NCTETTLRAW LQVIEANYHS SNAYHNSTHA
ADVLHATAFF LGKERVKGSL DQLDEVAALI AATVHDVDHP GRTNSFLCNA GSELAVLYND
TAVLESHHTA LAFQLTVKDT KCNIFKNIDR NHYRTLRQAI IDMVLATEMT KHFEHVNKFV
NSINKPLAAE SEGSDCECNP TGKNFPENQI LIKRMMIKCA DVANPCRPLD LCIEWAGRIS
EEYFAQTDEE KRQGLPVVMP VFDRNTCSIP KSQISFIDYF ITDMFDAWDA FAHLPALMQH
LADNYKHWKT LDDLKCKTLR LPSDS
