| Tag | Content |
|---|
| CPLM ID | CPLM-016764 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A |
Protein Synonyms/Alias | |
Gene Name | Pde10a |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 28 | SPSLTDEKVKAYLSL | ubiquitination | [1] | | 307 | FQVDHKNKELYSDLF | ubiquitination | [1] | | 338 | EIRFSIEKGIAGQVA | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition. |
Sequence Annotation | REGION 290 291 Allosteric effector binding (By
REGION 334 335 Allosteric effector binding (By
ACT_SITE 519 519 Proton donor (By similarity).
METAL 523 523 Divalent metal cation 1 (By similarity).
METAL 557 557 Divalent metal cation 1 (By similarity).
METAL 558 558 Divalent metal cation 1 (By similarity).
METAL 558 558 Divalent metal cation 2 (By similarity).
METAL 668 668 Divalent metal cation 1 (By similarity).
BINDING 368 368 Allosteric effector (By similarity).
BINDING 387 387 Allosteric effector (By similarity).
BINDING 519 519 Substrate (By similarity).
BINDING 720 720 Substrate (By similarity). |
Keyword | Allosteric enzyme; Alternative splicing; cAMP; cAMP-binding; cGMP; cGMP-binding; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 790 AA |
Protein Sequence | MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK 60
TNKAKDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNHLLLYELS SIIRIATKAD 120
GFALYFLGEC NNSLCVFIPP GMKEGQPRLI PAGPITQGTT ISAYVAKSRK TLLVEDILGD 180
ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA 240
SVAIHQVQVC RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF 300
QVDHKNKELY SDLFDIGEEK EGKPIFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP 360
RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL 420
ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM RFNLPARICR 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 TAMWISGPGP 780
APSKSTPEKL NVKVED 796 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:EC. GO:0030552; F:cAMP binding; ISS:UniProtKB. GO:0030553; F:cGMP binding; IEA:UniProtKB-KW. GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IMP:MGI. GO:0010738; P:regulation of protein kinase A signaling cascade; IMP:MGI. GO:0007165; P:signal transduction; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |