| Tag | Content |
|---|
| CPLM ID | CPLM-001366 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A |
Protein Synonyms/Alias | MmPDE8 |
Gene Name | Pde8a |
Gene Synonyms/Alias | Pde8 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 311 | PVIGQGGKIRHYVSI | 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 | Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development (By similarity). |
Sequence Annotation | DOMAIN 209 280 PAS.
DOMAIN 283 325 PAC.
REGION 526 807 Catalytic (By similarity).
ACT_SITE 551 551 Proton donor (By similarity).
METAL 555 555 Divalent metal cation 1 (By similarity).
METAL 591 591 Divalent metal cation 1 (By similarity).
METAL 592 592 Divalent metal cation 1 (By similarity).
METAL 592 592 Divalent metal cation 2 (By similarity).
METAL 720 720 Divalent metal cation 1 (By similarity).
MOD_RES 355 355 Phosphoserine; by PKA (By similarity).
MOD_RES 452 452 Phosphoserine. |
Keyword | cAMP; Complete proteome; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 823 AA |
Protein Sequence | MGCAPSIHTS ENRTFSHSDG EDEDVDVDVP GPAPRSIQRW STAPGLVEPQ PRDNGASKVS 60
VADVQFGPMR FHQDQLQVLL VFTKEDSQCN GFHRACEKAG FKCTVTKEVQ TVLTCFQDKL 120
HDIIIIDHRY PRQMDAETLC RSIRSSKFSE NTVIVGVVRR VDKEESSLMP FLAAGFTRRF 180
IENPNVMACY NELLQLACGE VRSQLKLRAC NSVFTALEKS QEAIEITSED HIIQYANPAF 240
ESTMGYQSGE LIGKELAQVP INEKKGDLLD AINSCVTVDK EWQGVYHTQK KNGDNIQQNV 300
KIIPVIGQGG KIRHYVSIIR VCNGNNKVET TTECVQTDSQ TDNQAGKHKD RRKHSMDAKA 360
VSSRTSDVSS QRRHSSLARI HSMMIEAPIT KVINIINAAQ ENSPVPVTEA LNRVLDILRT 420
TELYSPQFNA QDDPHATDLV GGLMSDGLRR FSGNEYILAT KNLPPLSNNL ATPVSLHDVP 480
PRIALAIENE EQWDFDIFEL EVATQNRPLI YLGLKTFARF GMCEFLQCSE TTLRSWFQMI 540
ESNYHSSNPY HNSTHAADVL HATAYFLSRD KIKETLDRID EVAALIAATV HDVDHPGRTN 600
SFLCNAGNQL AVLYNDTAVL ESHHVALAFQ LTLENDQCNI FKQMERNDYR TLRQSIIDMV 660
LATEMTKHFE HVNKFINSIN KPLTAQESEE PDRSLEDIKA MLKTPESRAL IKRMMIKCAD 720
VSNPCRPLEH CIEWAARISE EYFSQTDEEK QLDLPVVMPV FDRNTCSIPK SQISFIDYFI 780
TDMFDAWDAF VDLPNLMQHL DDNFRYWKGL DEKKLRSLRP PPE 823 |
Gene Ontology | GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:MGI. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro. GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway. GO:0035556; P:intracellular signal transduction; IEA:GOC. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |