Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00121
Entry Name
UniProt Accession
Theoretical PI
6.15
Molecular Weight
88412.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Protein Synonyms/Alias
3.1.4.17; 3.1.4.35;
Gene Name
PDE10A
Gene Synonyms/Alias
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Isoform 2
GPSNNASCFRRLTEC
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Charych EI, Jiang LX, Lo F, Sullivan K, Brandon NJ. Interplay ofpalmitoylation and phosphorylation in the trafficking and localization ofphosphodiesterase 10A: implications for the treatment of schizophrenia. JNeurosci. 2010 Jul 7;30(27):9027-37. doi: 10.1523/JNEUROSCI.1635-10.2010.[PMID:20610737]
Functional Description
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.
Sequence Annotation
Domain: 91 234 GAF 1.
Domain: 266 412 GAF 2.
Region: 286 287 Allosteric effector binding.
Region: 330 331 Allosteric effector binding.
Active site: 515 515 Proton donor.
Metal binding site: 519 519 Divalent metal cation 1.
Metal binding site: 553 553 Divalent metal cation 1.
Metal binding site: 554 554 Divalent metal cation 1.
Metal binding site: 554 554 Divalent metal cation 2.
Metal binding site: 664 664 Divalent metal cation 1.
Binding site: 364 364 Allosteric effector.
Binding site: 383 383 Allosteric effector.
Binding site: 515 515 Substrate.
Binding site: 716 716 Substrate.
Protein Length
779 AA.
Protein Sequence
(Isoform 2)
MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK  60
NNKSEDESAP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS SIIKIATKAD  120
GFALYFLGEC NNSLCIFTPP GIKEGKPRLI PAGPITQGTT VSAYVAKSRK TLLVEDILGD  180
ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA  240
SVAIHQVQVC RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF  300
QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP  360
RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL  420
ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM QFTLPVRLCK EIELFHFDIG  480
PFENMWPGIF VYMVHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI  540
LQNNHTLFTD LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV  600
SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS  660
HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKKD  720
EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLS QWEKVIRGEE TATWISSPSV  780
AQKAAASED                                                          789
FASTA
(Isoform 2)
>LipidDB-9606-00121|Q9Y233-2
MEDGPSNNASCFRRLTECFLSPSLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRK
NNKSEDESAPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKAD
GFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGD
ERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWA
SVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALF
QVDHKNKELYSDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADP
RFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCAL
ALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIG
PFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAI
LQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTV
SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQS
HRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKD
EVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSV
AQKAAASED
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC
GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc
GO:0030552; F:cAMP binding; IDA:UniProtKB
GO:0030553; F:cGMP binding; NAS:UniProtKB
GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway
GO:0046069; P:cGMP catabolic process; IEA:UniProtKB-UniPathway
GO:0043949; P:regulation of cAMP-mediated signaling; IEA:Ensembl
GO:0010738; P:regulation of protein kinase A signaling; IEA:Ensembl
GO:0007165; P:signal transduction; IEA:InterPro
Interpro
InterPro; IPR003018; GAF
InterPro; IPR029016; GAF_dom_like
InterPro; IPR003607; HD/PDEase_dom
InterPro; IPR023088; PDEase
InterPro; IPR002073; PDEase_catalytic_dom
InterPro; IPR023174; PDEase_CS
Pfam
Pfam; PF01590; GAF;
Pfam; PF00233; PDEase_I;
SMART
SMART; SM00065; GAF;
SMART; SM00471; HDc;
PROSITE
PROSITE; PS00126; PDEASE_I;
PRINTS
PRINTS; PR00387; PDIESTERASE1;