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   24-JAN-2024, entry version 181.
DE   RecName: Full=3',5'-cyclic-AMP phosphodiesterase 7B {ECO:0000305};
DE            EC=3.1.4.53 {ECO:0000269|PubMed:10814504, ECO:0000269|PubMed:10872825};
DE   AltName: Full=cAMP-specific phosphodiesterase 7B {ECO:0000303|PubMed:10814504};
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; 20.
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; 9606-ENSP00000310661; -.
DR   PeptideAtlas; Q9NP56; -.
DR   ProteomicsDB; 81887; -.
DR   Antibodypedia; 19754; 334 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   AGR; HGNC:8792; -.
DR   CTD; 27115; -.
DR   DisGeNET; 27115; -.
DR   GeneCards; PDE7B; -.
DR   HGNC; HGNC:8792; PDE7B.
DR   HPA; ENSG00000171408; Low tissue specificity.
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   InParanoid; Q9NP56; -.
DR   OMA; MVKLLWK; -.
DR   OrthoDB; 240889at2759; -.
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 1164 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 cell types or tissues.
DR   ExpressionAtlas; Q9NP56; baseline and differential.
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: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; TAS:ProtInc.
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:SF72; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 7B; 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.
DR   Genevisible; Q9NP56; HS.
PE   1: Evidence at protein level;
KW   cAMP; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..450
FT                   /note="3',5'-cyclic-AMP 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
//