PDE12_RAT
ID PDE12_RAT Reviewed; 608 AA.
AC Q6AXQ5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=2',5'-phosphodiesterase 12;
DE Short=2'-PDE;
DE Short=2-PDE;
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q6L8Q7};
DE AltName: Full=Mitochondrial deadenylase;
DE EC=3.1.13.4 {ECO:0000250|UniProtKB:Q6L8Q7};
DE Flags: Precursor;
GN Name=Pde12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Enzyme that cleaves 2',5'-phosphodiester bond linking
CC adenosines of the 5'-triphosphorylated oligoadenylates,
CC triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A
CC system. Degrades triphosphorylated 2-5A to produce AMP and ATP. Also
CC cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a
CC negative regulator of the 2-5A system that is one of the major pathways
CC for antiviral and antitumor functions induced by interferons (IFNs).
CC Suppression of this enzyme increases cellular 2-5A levels and decreases
CC viral replication in cultured small-airway epithelial cells.
CC {ECO:0000250|UniProtKB:Q6L8Q7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000250|UniProtKB:Q6L8Q7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q6L8Q7};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q6L8Q7}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; BC079396; AAH79396.1; -; mRNA.
DR AlphaFoldDB; Q6AXQ5; -.
DR SMR; Q6AXQ5; -.
DR STRING; 10116.ENSRNOP00000043554; -.
DR iPTMnet; Q6AXQ5; -.
DR PhosphoSitePlus; Q6AXQ5; -.
DR jPOST; Q6AXQ5; -.
DR PaxDb; Q6AXQ5; -.
DR PRIDE; Q6AXQ5; -.
DR UCSC; RGD:1310975; rat.
DR RGD; 1310975; Pde12.
DR VEuPathDB; HostDB:ENSRNOG00000059442; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_7_2_1; -.
DR InParanoid; Q6AXQ5; -.
DR OMA; LFRWFRE; -.
DR Reactome; R-RNO-8983711; OAS antiviral response.
DR PRO; PR:Q6AXQ5; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000059442; Expressed in duodenum and 18 other tissues.
DR ExpressionAtlas; Q6AXQ5; baseline and differential.
DR Genevisible; Q6AXQ5; RN.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:RGD.
DR GO; GO:0004527; F:exonuclease activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0071359; P:cellular response to dsRNA; ISO:RGD.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:RGD.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:RGD.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; ISO:RGD.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; ISO:RGD.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 2: Evidence at transcript level;
KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Mitochondrion;
KW mRNA processing; Nuclease; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 17..608
FT /note="2',5'-phosphodiesterase 12"
FT /id="PRO_0000324314"
FT REGION 91..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 350
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
SQ SEQUENCE 608 AA; 67176 MW; 2AC300EAE15C09F7 CRC64;
MWRLPGRAAL RGVRSVVEQR SPAEATTHEA VRAMERAVVR CVPSEPKLSL SFALADGSHK
NMQRDQSEPL GRALSRIATN ALKGHAKVAA AKKSRKNRAH SSGGAACAAT GSEPAATCEP
VVKLYYREEA VAEDVLNVDA WQDGAVLQIG DVKYKVERNP PAFTELQLPR YIMAGFPVCP
KLGLEFGDPA SSVFRWYKEV KPGAAEPGDS GLASSSHSLQ SSAWIETGVD ERVYTPCNAD
IGLRLKLHCT PGNGQRFGPS RELESVCPVE AGPGTCTFDH RHLYTKKVTE DSFIRTVSYN
ILADTYAQTE FSRTVLYPYC APYALELDYR QNLIQKELTG YNADLICLQE VDRAVFSDSL
VPALEAFGLE GVFRIKQHEG LATFYRKSKF RLLSQHDISF QEALKSDPLH KELLEKLALN
PLAQEKVLQR SSVLQISVLQ STTDSSKKIC VANTHLYWHP KGGYIRLIQM AAALVHIRHV
SCDLYPGIPV IFCGDFNSTP STGMYHFVIN GSVPEDHEDW ASNGEEERCG MSLTHCFKLK
SACGEPAYTN YVGGFHGCLD YIFIDLNALE VEQVIPLPSH EEVTTHQALP SVSHPSDHIA
LVCDLKWK
