Overview
| Uniprot ID | Q6L8Q7 |
|---|
| Protein Name | 2',5'-phosphodiesterase 12 |
|---|
| Gene Name | PDE12 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 88 |
NALKGHAKAAAAKKS |
| 97 |
AAAKKSRKSRPNASG |
Function
Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP (PubMed:26055709). Also cleaves 3',5'-phosphodiester bond of oligoadenylates (PubMed:21666256, PubMed:26055709, PubMed:30389976). Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells and Hela cells (PubMed:26055709)
Protein Sequence
10
MWRLPGARAA
20
LRVIRTAVEK
30
LSRAEAGSQT
40
AAGAMERAVV
50
RCVPSEPKLS
60
LSFALADGSH
70
KNMQRDQSEP
80
LGRVLSRIAT
90
NALKGHAKAA
100
AAKKSRKSRP
110
NASGGAACSG
120
PGPEPAVFCE
130
PVVKLYYREE
140
AVAEDVLNVD
150
AWQDGAVLQI
160
GDVKYKVERN
170
PPAFTELQLP
180
RYIMAGFPVC
190
PKLSLEFGDP
200
ASSLFRWYKE
210
AKPGAAEPEV
220
GVPSSLSPSS
230
PSSSWTETDV
240
EERVYTPSNA
250
DIGLRLKLHC
260
TPGDGQRFGH
270
SRELESVCVV
280
EAGPGTCTFD
290
HRHLYTKKVT
300
EDALIRTVSY
310
NILADTYAQT
320
EFSRTVLYPY
330
CAPYALELDY
340
RQNLIQKELT
350
GYNADVICLQ
360
EVDRAVFSDS
370
LVPALEAFGL
380
EGVFRIKQHE
390
GLATFYRKSK
400
FSLLSQHDIS
410
FYEALESDPL
420
HKELLEKLVL
430
YPSAQEKVLQ
440
RSSVLQVSVL
450
QSTKDSSKRI
460
CVANTHLYWH
470
PKGGYIRLIQ
480
MAVALAHIRH
490
VSCDLYPGIP
500
VIFCGDFNST
510
PSTGMYHFVI
520
NGSIPEDHED
530
WASNGEEERC
540
NMSLTHFFKL
550
KSACGEPAYT
560
NYVGGFHGCL
570
DYIFIDLNAL
580
EVEQVIPLPS
590
HEEVTTHQAL
600
PSVSHPSDHI
ALVCDLKWK
Gene Ontology
| Classification |
GO ID |
Description |
| Biological Process |
GO:0035457 |
cellular response to interferon-alpha |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005759 |
mitochondrial matrix |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Molecular Function |
GO:0000175 |
3'-5'-RNA exonuclease activity |
| Molecular Function |
GO:0004527 |
exonuclease activity |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Molecular Function |
GO:0004535 |
poly(A)-specific ribonuclease activity |
| Biological Process |
GO:0140374 |
antiviral innate immune response |
| Biological Process |
GO:0071359 |
cellular response to dsRNA |
| Biological Process |
GO:0071346 |
cellular response to type II interferon |
| Biological Process |
GO:0051607 |
defense response to virus |
| Biological Process |
GO:0000958 |
mitochondrial mRNA catabolic process |
| Biological Process |
GO:0006397 |
mRNA processing |
| Biological Process |
GO:0000288 |
nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay |
| Biological Process |
GO:0090304 |
nucleic acid metabolic process |
| Biological Process |
GO:0045070 |
positive regulation of viral genome replication |
| Biological Process |
GO:0044528 |
regulation of mitochondrial mRNA stability |
Reference
[1] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.