Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00514
Entry Name
UniProt Accession
Theoretical PI
6.11
Molecular Weight
90161.35
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
16-DEC-2008
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Canonical
GPSNNASCFRRLTEC
[1]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Predicted from GPS-Lipid
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
Region: 296 297 Allosteric effector binding.
Region: 340 341 Allosteric effector binding.
Active site: 525 525 Proton donor.
Metal binding site: 529 529 Divalent metal cation 1.
Metal binding site: 563 563 Divalent metal cation 1.
Metal binding site: 564 564 Divalent metal cation 1.
Metal binding site: 564 564 Divalent metal cation 2.
Metal binding site: 674 674 Divalent metal cation 1.
Binding site: 374 374 Allosteric effector.
Binding site: 393 393 Allosteric effector.
Binding site: 525 525 Substrate.
Binding site: 726 726 Substrate.
Protein Length
794 AA.
Protein Sequence
(Canonical)
MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK  60
NNKAEDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNHLLLYELS SIIRIATKAD  120
GFALYFLGEC NNSLCVFTPP GMKEGQPRLI PAGPITQGTT ISAYVAKSRK 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 HFNLPARICR DIELFHFDIG  480
PFENMWPGIF VYMIHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI  540
LQNNNGLFTD LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV  600
SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLHNQS  660
HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKRD  720
EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLN QWEKVIRGEE TAMWISGPAT  780
SKSTSEKPTR KVDD                                                    794
FASTA
(Canonical)
>LipidDB-10116-00514|Q9QYJ6
MEDGPSNNASCFRRLTECFLSPSLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRK
NNKAEDEPSPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNHLLLYELSSIIRIATKAD
GFALYFLGECNNSLCVFTPPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGD
ERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWA
SVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALF
QVDHKNKELYSDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADP
RFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCAL
ALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMHFNLPARICRDIELFHFDIG
PFENMWPGIFVYMIHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAI
LQNNNGLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTV
SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLHNQS
HRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRD
EVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLNQWEKVIRGEETAMWISGPAT
SKSTSEKPTRKVDD
Gene Ontology
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:RGD
GO:0043025; C:neuronal cell body; IDA:RGD
GO:0043204; C:perikaryon; IDA:RGD
GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC
GO:0030552; F:cAMP binding; IDA:RGD
GO:0030553; F:cGMP binding; IDA:RGD
GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB
GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:RGD
GO:0008144; F:drug binding; IDA:RGD
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0006198; P:cAMP catabolic process; IDA:RGD
GO:0046069; P:cGMP catabolic process; IDA:RGD
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;