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cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) (EC 3.1.4.35)

 PDE10_RAT               Reviewed;         794 AA.
Q9QYJ6; Q6S9E6; Q6S9E7; Q6S9E8; Q6S9E9; Q9QYJ5;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 102.
RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
EC=3.1.4.17;
EC=3.1.4.35;
Name=Pde10a;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=10583409; DOI=10.1046/j.1432-1327.1999.00963.x;
Fujishige K., Kotera J., Omori K.;
"Striatum- and testis-specific phosphodiesterase PDE10A isolation and
characterization of a rat PDE10A.";
Eur. J. Biochem. 266:1118-1127(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), TISSUE
SPECIFICITY, CATALYTIC ACTIVITY, AND INDUCTION.
STRAIN=Wistar;
PubMed=14752115; DOI=10.1074/jbc.M312500200;
O'Connor V., Genin A., Davis S., Karishma K.K., Doyere V.,
De Zeeuw C.I., Sanger G., Hunt S.P., Richter-Levin G., Mallet J.,
Laroche S., Bliss T.V.P., French P.J.;
"Differential amplification of intron-containing transcripts reveals
long term potentiation-associated up-regulation of specific Pde10A
phosphodiesterase splice variants.";
J. Biol. Chem. 279:15841-15849(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 452-794 IN COMPLEXES WITH
ZINC; MAGNESIUM AND A SYNTHETIC INHIBITOR.
PubMed=17228859; DOI=10.1021/jm060653b;
Chappie T.A., Humphrey J.M., Allen M.P., Estep K.G., Fox C.B.,
Lebel L.A., Liras S., Marr E.S., Menniti F.S., Pandit J.,
Schmidt C.J., Tu M., Williams R.D., Yang F.V.;
"Discovery of a series of 6,7-dimethoxy-4-pyrrolidylquinazoline PDE10A
inhibitors.";
J. Med. Chem. 50:182-185(2007).
-!- FUNCTION: Plays a role in signal transduction by regulating the
intracellular concentration of cyclic nucleotides. Can hydrolyze
both cAMP and cGMP, but has higher affinity for cAMP and is more
efficient with cAMP as substrate. {ECO:0000269|PubMed:10583409}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate. {ECO:0000269|PubMed:14752115}.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate. {ECO:0000269|PubMed:14752115}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions.;
-!- ENZYME REGULATION: Inhibited by dipyridamole and moderately by
IBMX, zaprinast and rolipram. {ECO:0000269|PubMed:10583409}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.26 uM for cAMP {ECO:0000269|PubMed:10583409};
KM=9.3 uM for cGMP {ECO:0000269|PubMed:10583409};
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
3',5'-cyclic GMP: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10583409}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=PDE10A2;
IsoId=Q9QYJ6-1; Sequence=Displayed;
Name=2; Synonyms=PDE10A3;
IsoId=Q9QYJ6-2; Sequence=VSP_035921;
Name=3; Synonyms=PDE10A11;
IsoId=Q9QYJ6-3; Sequence=VSP_035922;
Name=4; Synonyms=PDE10A12;
IsoId=Q9QYJ6-4; Sequence=VSP_035923;
Name=5; Synonyms=PDE10A13;
IsoId=Q9QYJ6-5; Sequence=VSP_035920;
Name=6; Synonyms=PDE10A14;
IsoId=Q9QYJ6-6; Sequence=VSP_035919;
-!- TISSUE SPECIFICITY: Detected in striatum and testis (at protein
level). Detected in whole brain, hippocampus, olfactory bulb,
striatum neurons and testis. {ECO:0000269|PubMed:10583409,
ECO:0000269|PubMed:14752115}.
-!- INDUCTION: Up-regulated in brain after seizures. Up-regulated in
the hippocampus one hour after induction of long-term
potentiation. {ECO:0000269|PubMed:14752115}.
-!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme
activity. The binding of cAMP stimulates enzyme activity.
-!- DOMAIN: Composed of a C-terminal catalytic domain containing two
divalent metal sites and an N-terminal regulatory domain which
contains one cyclic nucleotide-binding region.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB027155; BAA88996.1; -; mRNA.
EMBL; AB027156; BAA88997.1; -; mRNA.
EMBL; AY462091; AAS21243.1; -; mRNA.
EMBL; AY462092; AAS21244.1; -; mRNA.
EMBL; AY462093; AAS21245.1; -; mRNA.
EMBL; AY462094; AAS21246.1; -; mRNA.
EMBL; AY462095; AAS21247.1; -; mRNA.
EMBL; CH474059; EDL83106.1; -; Genomic_DNA.
RefSeq; NP_071572.1; NM_022236.1. [Q9QYJ6-1]
UniGene; Rn.44869; -.
PDB; 2O8H; X-ray; 1.80 A; A=452-794.
PDB; 2OVV; X-ray; 2.00 A; A=452-794.
PDB; 2OVY; X-ray; 1.80 A; A=452-794.
PDB; 3HQW; X-ray; 1.70 A; A=452-794.
PDB; 3HQY; X-ray; 2.00 A; A=452-794.
PDB; 3HQZ; X-ray; 1.70 A; A=452-794.
PDB; 3HR1; X-ray; 1.53 A; A=452-794.
PDB; 3LXG; X-ray; 2.30 A; A=463-770.
PDB; 3QPN; X-ray; 2.00 A; A=452-794.
PDB; 3QPO; X-ray; 1.80 A; A=452-794.
PDB; 3QPP; X-ray; 1.80 A; A=452-794.
PDBsum; 2O8H; -.
PDBsum; 2OVV; -.
PDBsum; 2OVY; -.
PDBsum; 3HQW; -.
PDBsum; 3HQY; -.
PDBsum; 3HQZ; -.
PDBsum; 3HR1; -.
PDBsum; 3LXG; -.
PDBsum; 3QPN; -.
PDBsum; 3QPO; -.
PDBsum; 3QPP; -.
ProteinModelPortal; Q9QYJ6; -.
SMR; Q9QYJ6; -.
STRING; 10116.ENSRNOP00000060834; -.
BindingDB; Q9QYJ6; -.
ChEMBL; CHEMBL6140; -.
iPTMnet; Q9QYJ6; -.
SwissPalm; Q9QYJ6; -.
PaxDb; Q9QYJ6; -.
PRIDE; Q9QYJ6; -.
Ensembl; ENSRNOT00000043474; ENSRNOP00000042134; ENSRNOG00000011310. [Q9QYJ6-1]
GeneID; 63885; -.
KEGG; rno:63885; -.
CTD; 10846; -.
RGD; 68434; Pde10a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG082113; -.
InParanoid; Q9QYJ6; -.
KO; K18438; -.
OMA; CRFTMSV; -.
OrthoDB; EOG091G037C; -.
TreeFam; TF316499; -.
Reactome; R-RNO-418457; cGMP effects.
Reactome; R-RNO-418555; G alpha (s) signalling events.
UniPathway; UPA00762; UER00747.
UniPathway; UPA00763; UER00748.
EvolutionaryTrace; Q9QYJ6; -.
PMAP-CutDB; Q9QYJ6; -.
PRO; PR:Q9QYJ6; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000011310; -.
ExpressionAtlas; Q9QYJ6; baseline and differential.
Genevisible; Q9QYJ6; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; ISO:RGD.
GO; GO:0030552; F:cAMP binding; IDA:RGD.
GO; GO:0030553; F:cGMP binding; IDA:RGD.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:RGD.
GO; GO:0046069; P:cGMP catabolic process; IDA:RGD.
GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISO:RGD.
GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 2.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
SUPFAM; SSF55781; SSF55781; 2.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing; cAMP;
cAMP-binding; cGMP; cGMP-binding; Complete proteome; Cytoplasm;
Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome;
Repeat.
CHAIN 1 794 cAMP and cAMP-inhibited cGMP 3',5'-cyclic
phosphodiesterase 10A.
/FTId=PRO_0000355559.
REGION 296 297 Allosteric effector binding.
{ECO:0000250}.
REGION 340 341 Allosteric effector binding.
{ECO:0000250}.
ACT_SITE 525 525 Proton donor. {ECO:0000250}.
METAL 529 529 Divalent metal cation 1.
METAL 563 563 Divalent metal cation 1.
METAL 564 564 Divalent metal cation 1.
METAL 564 564 Divalent metal cation 2.
METAL 674 674 Divalent metal cation 1.
BINDING 374 374 Allosteric effector. {ECO:0000250}.
BINDING 393 393 Allosteric effector. {ECO:0000250}.
BINDING 525 525 Substrate. {ECO:0000250}.
BINDING 726 726 Substrate. {ECO:0000250}.
VAR_SEQ 1 141 Missing (in isoform 6).
{ECO:0000303|PubMed:14752115}.
/FTId=VSP_035919.
VAR_SEQ 1 80 Missing (in isoform 5).
{ECO:0000303|PubMed:14752115}.
/FTId=VSP_035920.
VAR_SEQ 1 23 MEDGPSNNASCFRRLTECFLSPS -> MSNDSPEGAVGSCN
ATG (in isoform 2).
{ECO:0000303|PubMed:10583409,
ECO:0000303|PubMed:14752115}.
/FTId=VSP_035921.
VAR_SEQ 1 23 MEDGPSNNASCFRRLTECFLSPS -> MSKKRKALEGGGGG
GEPQLPEEEPTAWFGGSSEEPAGCLPITFKGGSKGPALLAL
RNRTDSRGQMSNDSPEGAVGSCNATG (in isoform
3). {ECO:0000303|PubMed:14752115}.
/FTId=VSP_035922.
VAR_SEQ 1 23 MEDGPSNNASCFRRLTECFLSPS -> MSKKRKALEGGGGG
GEPQLPEEEPTAWFGGSSEEPAGCLPITFKGGSKGPALLAL
RNRTDSRGQMSNDSPEGAVGSCNATGSTGSTGELGKEFHTP
PRRKSASDSRLALCMG (in isoform 4).
{ECO:0000303|PubMed:14752115}.
/FTId=VSP_035923.
HELIX 466 471 {ECO:0000244|PDB:3HR1}.
HELIX 483 485 {ECO:0000244|PDB:3HR1}.
HELIX 486 498 {ECO:0000244|PDB:3HR1}.
HELIX 500 502 {ECO:0000244|PDB:3HQW}.
HELIX 505 517 {ECO:0000244|PDB:3HR1}.
STRAND 523 526 {ECO:0000244|PDB:3HR1}.
HELIX 527 542 {ECO:0000244|PDB:3HR1}.
TURN 545 547 {ECO:0000244|PDB:3HR1}.
HELIX 550 562 {ECO:0000244|PDB:3HR1}.
TURN 563 566 {ECO:0000244|PDB:3HR1}.
HELIX 572 578 {ECO:0000244|PDB:3HR1}.
HELIX 581 585 {ECO:0000244|PDB:3HR1}.
STRAND 587 589 {ECO:0000244|PDB:3HR1}.
HELIX 590 603 {ECO:0000244|PDB:3HR1}.
TURN 610 613 {ECO:0000244|PDB:3HR1}.
HELIX 616 632 {ECO:0000244|PDB:3HR1}.
HELIX 635 650 {ECO:0000244|PDB:3HR1}.
HELIX 659 674 {ECO:0000244|PDB:3HR1}.
HELIX 676 679 {ECO:0000244|PDB:3HR1}.
HELIX 682 705 {ECO:0000244|PDB:3HR1}.
HELIX 712 714 {ECO:0000244|PDB:3HR1}.
HELIX 716 721 {ECO:0000244|PDB:3HR1}.
HELIX 722 732 {ECO:0000244|PDB:3HR1}.
HELIX 734 744 {ECO:0000244|PDB:3HR1}.
HELIX 746 748 {ECO:0000244|PDB:3HR1}.
HELIX 749 766 {ECO:0000244|PDB:3HR1}.
SEQUENCE 794 AA; 90161 MW; A36C4678B385846E CRC64;
MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK
NNKAEDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNHLLLYELS SIIRIATKAD
GFALYFLGEC NNSLCVFTPP GMKEGQPRLI PAGPITQGTT ISAYVAKSRK TLLVEDILGD
ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA
SVAIHQVQVC RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF
QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP
RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL
ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM HFNLPARICR DIELFHFDIG
PFENMWPGIF VYMIHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI
LQNNNGLFTD LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV
SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLHNQS
HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKRD
EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLN QWEKVIRGEE TAMWISGPAT
SKSTSEKPTR KVDD


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