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   11-NOV-2015, entry version 136.
DE   RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 7B;
DE            EC=3.1.4.53;
GN   Name=PDE7B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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].
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
RT   cAMP-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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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. May be
CC       involved in the control of cAMP-mediated neural activity and cAMP
CC       metabolism in the brain.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate.
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   -!- ENZYME REGULATION: Inhibited by dipyridamole, IBMX and SCH 51866.
CC       Insensitive to zaprinast, rolipram, and milrinone.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Also expressed in
CC       heart, liver, skeletal muscle and pancreas.
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
CC       family. PDE7 subfamily. {ECO:0000305}.
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DR   EMBL; AB038040; BAA96537.1; -; mRNA.
DR   EMBL; AJ251860; CAB92441.1; -; mRNA.
DR   EMBL; AL360178; CAH73075.1; -; Genomic_DNA.
DR   EMBL; AL133319; CAH73075.1; JOINED; Genomic_DNA.
DR   EMBL; AL138828; CAH73075.1; JOINED; Genomic_DNA.
DR   EMBL; AL133319; CAH73332.1; -; Genomic_DNA.
DR   EMBL; AL138828; CAH73332.1; JOINED; Genomic_DNA.
DR   EMBL; AL360178; CAH73332.1; JOINED; Genomic_DNA.
DR   EMBL; AL138828; CAI95287.1; -; Genomic_DNA.
DR   EMBL; AL133319; CAI95287.1; JOINED; Genomic_DNA.
DR   EMBL; AL360178; CAI95287.1; JOINED; 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   UniGene; Hs.744230; -.
DR   PDB; 1LXW; Model; -; A=104-433.
DR   PDBsum; 1LXW; -.
DR   ProteinModelPortal; Q9NP56; -.
DR   SMR; Q9NP56; 100-416.
DR   BioGrid; 118010; 2.
DR   IntAct; Q9NP56; 1.
DR   STRING; 9606.ENSP00000310661; -.
DR   BindingDB; Q9NP56; -.
DR   ChEMBL; CHEMBL2111411; -.
DR   DrugBank; DB00201; Caffeine.
DR   DrugBank; DB00651; Dyphylline.
DR   DrugBank; DB00920; Ketotifen.
DR   GuidetoPHARMACOLOGY; 1306; -.
DR   PhosphoSite; Q9NP56; -.
DR   BioMuta; PDE7B; -.
DR   DMDM; 13626185; -.
DR   MaxQB; Q9NP56; -.
DR   PaxDb; Q9NP56; -.
DR   PRIDE; Q9NP56; -.
DR   DNASU; 27115; -.
DR   Ensembl; ENST00000308191; ENSP00000310661; ENSG00000171408.
DR   GeneID; 27115; -.
DR   KEGG; hsa:27115; -.
DR   UCSC; uc003qgp.3; human.
DR   CTD; 27115; -.
DR   GeneCards; PDE7B; -.
DR   HGNC; HGNC:8792; PDE7B.
DR   HPA; HPA023967; -.
DR   MIM; 604645; gene.
DR   neXtProt; NX_Q9NP56; -.
DR   PharmGKB; PA33140; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   eggNOG; ENOG410XRI7; LUCA.
DR   GeneTree; ENSGT00760000118889; -.
DR   HOGENOM; HOG000220881; -.
DR   HOVERGEN; HBG053543; -.
DR   KO; K18436; -.
DR   OrthoDB; EOG7M98G3; -.
DR   PhylomeDB; Q9NP56; -.
DR   TreeFam; TF314638; -.
DR   BRENDA; 3.1.4.53; 2681.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   UniPathway; UPA00762; UER00747.
DR   GenomeRNAi; 27115; -.
DR   NextBio; 49800; -.
DR   PRO; PR:Q9NP56; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; Q9NP56; -.
DR   CleanEx; HS_PDE7B; -.
DR   ExpressionAtlas; Q9NP56; baseline and differential.
DR   Genevisible; Q9NP56; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:ProtInc.
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:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0007268; P:synaptic transmission; TAS:ProtInc.
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; IPR023174; PDEase_CS.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; cAMP; Complete proteome; Hydrolase; Metal-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1    450       cAMP-specific 3',5'-cyclic
FT                                phosphodiesterase 7B.
FT                                /FTId=PRO_0000198836.
FT   REGION      172    410       Catalytic. {ECO:0000250}.
FT   ACT_SITE    173    173       Proton donor. {ECO:0000250}.
FT   METAL       177    177       Divalent metal cation 1. {ECO:0000250}.
FT   METAL       213    213       Divalent metal cation 1. {ECO:0000250}.
FT   METAL       214    214       Divalent metal cation 1. {ECO:0000250}.
FT   METAL       214    214       Divalent metal cation 2. {ECO:0000250}.
FT   METAL       323    323       Divalent metal cation 1. {ECO:0000250}.
FT   MOD_RES     426    426       Phosphoserine.
FT                                {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
//