PDE12_BOVIN
ID PDE12_BOVIN Reviewed; 609 AA.
AC Q08DF7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15231837; DOI=10.1074/jbc.m400089200;
RA Kubota K., Nakahara K., Ohtsuka T., Yoshida S., Kawaguchi J., Fujita Y.,
RA Ozeki Y., Hara A., Yoshimura C., Furukawa H., Haruyama H., Ichikawa K.,
RA Yamashita M., Matsuoka T., Iijima Y.;
RT "Identification of 2'-phosphodiesterase, which plays a role in the 2-5A
RT system regulated by interferon.";
RL J. Biol. Chem. 279:37832-37841(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 -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:15231837}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; BC123772; AAI23773.1; -; mRNA.
DR RefSeq; NP_001069601.1; NM_001076133.1.
DR AlphaFoldDB; Q08DF7; -.
DR SMR; Q08DF7; -.
DR STRING; 9913.ENSBTAP00000020675; -.
DR PaxDb; Q08DF7; -.
DR PRIDE; Q08DF7; -.
DR Ensembl; ENSBTAT00000020675; ENSBTAP00000020675; ENSBTAG00000015563.
DR GeneID; 538860; -.
DR KEGG; bta:538860; -.
DR CTD; 201626; -.
DR VEuPathDB; HostDB:ENSBTAG00000015563; -.
DR VGNC; VGNC:32670; PDE12.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000157205; -.
DR HOGENOM; CLU_016428_7_2_1; -.
DR InParanoid; Q08DF7; -.
DR OMA; LFRWFRE; -.
DR OrthoDB; 724242at2759; -.
DR TreeFam; TF323175; -.
DR Reactome; R-BTA-8983711; OAS antiviral response.
DR Proteomes; UP000009136; Chromosome 22.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IMP:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IEA:Ensembl.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IBA:GO_Central.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IEA:Ensembl.
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 1: Evidence at protein 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..609
FT /note="2',5'-phosphodiesterase 12"
FT /id="PRO_0000324311"
FT REGION 203..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96LI5"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6L8Q7"
SQ SEQUENCE 609 AA; 67264 MW; 705BD47426930984 CRC64;
MWRLPGVRAA LRGVRTAVER RSRTEAASET SVGAMERAVV RCVPSEPKLS LSFALADGSH
KNMQRDQSEP LGRALSRIAT NALKGHAKVA AAKKSRKNRP NAGSGVACAG PGPEPAAACE
PVVKLYYREE AVAEDVLNVD AWQDGAVLQI GDVKYKVERN PPAFTELQLP RYIMAGFPVC
PKLGVEFGDP TGSLFRWYKE TKPRAAEPEG GGPSSSSPSS PSPGWTETGV DERVYTPSNA
DIGLRLKLHC TPGNGQRFGP SRELESVCPV EAGPGTCTFD HRHLYTKKVT DDALIRTVSY
NILADTYAQT EFSRTVLYPY CAPYALELDY RQNLIQKELT GYNADLICLQ EVDRCVFTDS
LMPALEAFGL EGVFRIKQHE GLATFYRKSK FSLLSQHDIA FHEALQSDPL HKELLEKLAL
YPSAQERVLQ RSSVVQVSVL QSTKDSSKKI CVANTHLYWH PKGGYIRLIQ MAVALAHIRH
VSCDLYPGIP VIFCGDFNST PSTGMYHFVI NGSIAEDHED WTSNGEEERC NMSLSHFFKL
KSACGEPAYT NYVGGFHGCL DYIFIDLHAL EVEQVIPLPS HEEVTTHQAL PSVSHPSDHI
ALVCDLKWK
