PDE7B_HUMAN
ID PDE7B_HUMAN Reviewed; 450 AA.
AC Q9NP56; Q5W154;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 7B {ECO:0000303|PubMed:10814504};
DE EC=3.1.4.53 {ECO:0000269|PubMed:10814504, ECO:0000269|PubMed:10872825};
GN Name=PDE7B {ECO:0000303|PubMed:10814504};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10814504; DOI=10.1006/bbrc.2000.2661;
RA Sasaki T., Kotera J., Yuasa K., Omori K.;
RT "Identification of human PDE7B, a cAMP-specific phosphodiesterase.";
RL Biochem. Biophys. Res. Commun. 271:575-583(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND ACTIVITY REGULATION.
RC TISSUE=Fetal brain;
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 GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes (PubMed:10814504,
CC PubMed:10872825). May be involved in the control of cAMP-mediated
CC neural activity and cAMP metabolism in the brain (PubMed:10814504).
CC {ECO:0000269|PubMed:10814504, 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:10814504, 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 (PubMed:10814504, PubMed:10872825). Insensitive to zaprinast, rolipram,
CC and milrinone (PubMed:10814504, PubMed:10872825).
CC {ECO:0000269|PubMed:10814504, ECO:0000269|PubMed:10872825}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:10814504};
CC KM=0.2 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:0000269|PubMed:10814504,
CC ECO:0000269|PubMed:10872825}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (PubMed:10814504). Also
CC expressed in heart, liver, skeletal muscle and pancreas
CC (PubMed:10814504). {ECO:0000269|PubMed:10814504}.
CC -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC putative divalent metal sites and an N-terminal regulatory domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE7 subfamily. {ECO:0000305}.
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DR EMBL; AB038040; BAA96537.1; -; mRNA.
DR EMBL; AJ251860; CAB92441.1; -; mRNA.
DR EMBL; AL360178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47957.1; -; Genomic_DNA.
DR EMBL; BC075082; AAH75082.1; -; mRNA.
DR EMBL; BC075083; AAH75083.1; -; mRNA.
DR CCDS; CCDS5175.1; -.
DR PIR; JC7266; JC7266.
DR RefSeq; NP_061818.1; NM_018945.3.
DR AlphaFoldDB; Q9NP56; -.
DR SMR; Q9NP56; -.
DR BioGRID; 118010; 19.
DR IntAct; Q9NP56; 1.
DR STRING; 9606.ENSP00000310661; -.
DR BindingDB; Q9NP56; -.
DR ChEMBL; CHEMBL4716; -.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB09283; Trapidil.
DR DrugCentral; Q9NP56; -.
DR GuidetoPHARMACOLOGY; 1306; -.
DR iPTMnet; Q9NP56; -.
DR PhosphoSitePlus; Q9NP56; -.
DR BioMuta; PDE7B; -.
DR DMDM; 13626185; -.
DR jPOST; Q9NP56; -.
DR MassIVE; Q9NP56; -.
DR MaxQB; Q9NP56; -.
DR PaxDb; Q9NP56; -.
DR PeptideAtlas; Q9NP56; -.
DR PRIDE; Q9NP56; -.
DR ProteomicsDB; 81887; -.
DR Antibodypedia; 19754; 289 antibodies from 30 providers.
DR DNASU; 27115; -.
DR Ensembl; ENST00000308191.11; ENSP00000310661.6; ENSG00000171408.14.
DR GeneID; 27115; -.
DR KEGG; hsa:27115; -.
DR MANE-Select; ENST00000308191.11; ENSP00000310661.6; NM_018945.4; NP_061818.1.
DR UCSC; uc003qgp.4; human.
DR CTD; 27115; -.
DR DisGeNET; 27115; -.
DR GeneCards; PDE7B; -.
DR HGNC; HGNC:8792; PDE7B.
DR HPA; ENSG00000171408; Tissue enhanced (brain).
DR MIM; 604645; gene.
DR neXtProt; NX_Q9NP56; -.
DR OpenTargets; ENSG00000171408; -.
DR PharmGKB; PA33140; -.
DR VEuPathDB; HostDB:ENSG00000171408; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000159413; -.
DR HOGENOM; CLU_005940_6_5_1; -.
DR OMA; YPPIDLR; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q9NP56; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.53; 2681.
DR PathwayCommons; Q9NP56; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR SignaLink; Q9NP56; -.
DR UniPathway; UPA00762; UER00747.
DR BioGRID-ORCS; 27115; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; PDE7B; human.
DR GenomeRNAi; 27115; -.
DR Pharos; Q9NP56; Tclin.
DR PRO; PR:Q9NP56; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NP56; protein.
DR Bgee; ENSG00000171408; Expressed in germinal epithelium of ovary and 169 other tissues.
DR ExpressionAtlas; Q9NP56; baseline and differential.
DR Genevisible; Q9NP56; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
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..450
FT /note="cAMP-specific 3',5'-cyclic phosphodiesterase 7B"
FT /id="PRO_0000198836"
FT DOMAIN 97..420
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 418..450
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:0000250|UniProtKB:Q9QXQ1"
SQ SEQUENCE 450 AA; 51835 MW; EC142BF3E28D0028 CRC64;
MSCLMVERCG EILFENPDQN AKCVCMLGDI RLRGQTGVRA ERRGSYPFID FRLLNSTTYS
GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED YLGQARHMLS KVGMWDFDIF
LFDRLTNGNS LVTLLCHLFN THGLIHHFKL DMVTLHRFLV MVQEDYHSQN PYHNAVHAAD
VTQAMHCYLK EPKLASFLTP LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS
VLENHHWRST IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN
KDLRLEDAQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGE LEQKFELEIS
PLCNQQKDSI PSIQIGFMSY IVEPLFREWA HFTGNSTLSE NMLGHLAHNK AQWKSLLPRQ
HRSRGSSGSG PDHDHAGQGT ESEEQEGDSP
