PDE12_MOUSE
ID PDE12_MOUSE Reviewed; 608 AA.
AC Q3TIU4; Q3TTY4; Q6P2L5; Q8BKH8; Q8BTS8; Q8BUQ5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Eye, Placenta, Skin, Spinal cord, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK051991; BAC34827.1; ALT_INIT; mRNA.
DR EMBL; AK082947; BAC38703.1; -; mRNA.
DR EMBL; AK088843; BAC40606.1; -; mRNA.
DR EMBL; AK155088; BAE33039.1; -; mRNA.
DR EMBL; AK161083; BAE36189.1; -; mRNA.
DR EMBL; AK167708; BAE39752.1; -; mRNA.
DR EMBL; BC064450; AAH64450.1; -; mRNA.
DR CCDS; CCDS26882.1; -.
DR RefSeq; NP_848783.3; NM_178668.3.
DR AlphaFoldDB; Q3TIU4; -.
DR SMR; Q3TIU4; -.
DR BioGRID; 229276; 32.
DR STRING; 10090.ENSMUSP00000059666; -.
DR iPTMnet; Q3TIU4; -.
DR PhosphoSitePlus; Q3TIU4; -.
DR EPD; Q3TIU4; -.
DR jPOST; Q3TIU4; -.
DR MaxQB; Q3TIU4; -.
DR PaxDb; Q3TIU4; -.
DR PeptideAtlas; Q3TIU4; -.
DR PRIDE; Q3TIU4; -.
DR ProteomicsDB; 287903; -.
DR Antibodypedia; 46309; 125 antibodies from 22 providers.
DR DNASU; 211948; -.
DR Ensembl; ENSMUST00000052932; ENSMUSP00000059666; ENSMUSG00000043702.
DR GeneID; 211948; -.
DR KEGG; mmu:211948; -.
DR UCSC; uc007stb.1; mouse.
DR CTD; 201626; -.
DR MGI; MGI:2443226; Pde12.
DR VEuPathDB; HostDB:ENSMUSG00000043702; -.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000157205; -.
DR HOGENOM; CLU_016428_7_2_1; -.
DR InParanoid; Q3TIU4; -.
DR OMA; LFRWFRE; -.
DR OrthoDB; 724242at2759; -.
DR PhylomeDB; Q3TIU4; -.
DR TreeFam; TF323175; -.
DR Reactome; R-MMU-8983711; OAS antiviral response.
DR BioGRID-ORCS; 211948; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Pde12; mouse.
DR PRO; PR:Q3TIU4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3TIU4; protein.
DR Bgee; ENSMUSG00000043702; Expressed in ectoplacental cone and 63 other tissues.
DR Genevisible; Q3TIU4; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; ISO:MGI.
DR GO; GO:0004527; F:exonuclease activity; ISO:MGI.
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:MGI.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; ISO:MGI.
DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:MGI.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; ISO:MGI.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; ISO:MGI.
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..608
FT /note="2',5'-phosphodiesterase 12"
FT /id="PRO_0000324313"
FT REGION 90..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"
FT CONFLICT 21..22
FT /note="SR -> TG (in Ref. 1; BAC38703)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="G -> S (in Ref. 1; BAC40606/BAE33039)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="K -> E (in Ref. 1; BAE39752)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="E -> A (in Ref. 1; BAC40606/BAE33039)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="C -> G (in Ref. 1; BAE36189)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="N -> H (in Ref. 1; BAE36189)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="K -> Q (in Ref. 1; BAE36189)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="P -> L (in Ref. 1; BAE39752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 67514 MW; DC67C45DE3FF556C CRC64;
MWRLPGRSAL RGVRSVVERR SRAEAGTHEA VRAMERAVVR CVPSEPKLSL SFALADGSHK
NMQRDQSEPL GRALSRIATN ALKGHAKVAA AKKSRKNRAH SSGGAACEAT GPEPVATCEP
VVKLYYREEA VAEDVLNVDA WQDGAVLQIG DVKYKVERNP PTFTELQLPR YIMAGFPVCP
KLGVEFGDPA SSVFRWYKEV KPGAAEPGDS GPASSSHSSQ PSAWIETGVD ERVYTPCNAD
IGLRLRLHCT PGNGQRFGPS RELESLCPVE AGPGTCTFDH RHLYTKKVTE DSFIRTVSYN
ILADTYAQTE FSRTVLYPYC APYALELDYR QNLIQKELTG YNADLICLQE VDRAVFSDSL
VPALEAFGLE GVFRIKQHEG LATFYRKSKF RLLSQHDISF QEALKSDPLH KELLEKLALN
PLAQEKVLQR SSVLQISVLQ STTDSSKKIC VANTHLYWHP KGGYIRLIQM EVALVHIRHV
SRDLYPGIPV IFCGDFNSTP STGMYHFVIS GSIAEDHEDW ASNGEEERCS MPLSHCFKLK
SACGEPAYTN YVGGFHGCLD YIFIDLNTLE VEQVIPLPSH EEVTTHQALP SVSHPSDHIA
LVCDLKWK
