Full text data of PDE12
PDE12
[Confidence: low (only semi-automatic identification from reviews)]
2',5'-phosphodiesterase 12; 2'-PDE; 2-PDE; 3.1.4.- (Mitochondrial deadenylase; 3.1.13.4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
2',5'-phosphodiesterase 12; 2'-PDE; 2-PDE; 3.1.4.- (Mitochondrial deadenylase; 3.1.13.4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6L8Q7
ID PDE12_HUMAN Reviewed; 609 AA.
AC Q6L8Q7; B4DTU8; Q8IYU3; Q8NDU2; Q8TE78;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 75.
DE RecName: Full=2',5'-phosphodiesterase 12;
DE Short=2'-PDE;
DE Short=2-PDE;
DE EC=3.1.4.-;
DE AltName: Full=Mitochondrial deadenylase;
DE EC=3.1.13.4;
DE Flags: Precursor;
GN Name=PDE12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15231837; DOI=10.1074/jbc.M400089200;
RA Kubota K., Nakahara K., Ohtsuka T., Yoshida S., Kawaguchi J.,
RA Fujita Y., Ozeki Y., Hara A., Yoshimura C., Furukawa H., Haruyama H.,
RA Ichikawa K., Yamashita M., Matsuoka T., Iijima Y.;
RT "Identification of 2'-phosphodiesterase, which plays a role in the 2-
RT 5A system regulated by interferon.";
RL J. Biol. Chem. 279:37832-37841(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TRP-23.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-23.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-609 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21245038; DOI=10.1093/nar/gkq1282;
RA Poulsen J.B., Andersen K.R., Kjaer K.H., Durand F., Faou P.,
RA Vestergaard A.L., Talbo G.H., Hoogenraad N., Brodersen D.E.,
RA Justesen J., Martensen P.M.;
RT "Human 2'-phosphodiesterase localizes to the mitochondrial matrix with
RT a putative function in mitochondrial RNA turnover.";
RL Nucleic Acids Res. 39:3754-3770(2011).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21666256; DOI=10.1093/nar/gkr470;
RA Rorbach J., Nicholls T.J., Minczuk M.;
RT "PDE12 removes mitochondrial RNA poly(A) tails and controls
RT translation in human mitochondria.";
RL Nucleic Acids Res. 39:7750-7763(2011).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, CATALYTIC ACTIVITY,
RP TRANSIT PEPTIDE, AND SUBCELLULAR LOCATION.
RX PubMed=22285541; DOI=10.1016/j.biochi.2012.01.012;
RA Poulsen J.B., Andersen K.R., Kjaer K.H., Vestergaard A.L.,
RA Justesen J., Martensen P.M.;
RT "Characterization of human phosphodiesterase 12 and identification of
RT a novel 2'-5' oligoadenylate nuclease - The ectonucleotide
RT pyrophosphatase/phosphodiesterase 1.";
RL Biochimie 94:1098-1107(2012).
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
CC 2-5A system. This enzyme degraded triphosphorylated 2-5A to
CC produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of
CC oligoadenylates. Plays a role as a negative regulator of the The
CC 2-5A system that is one of the major pathways for antiviral and
CC antitumor functions induced by interferons (IFNs). Suppression of
CC this enzyme induces reduction of viral replication in Hela cells,
CC thus counteracting the antiviral pathway probably by inhibiting
CC the 2-5A system.
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage of poly(A) to 5'-AMP.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for 2'-5' oligoadenylate exonuclease activity;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6L8Q7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6L8Q7-2; Sequence=VSP_032202, VSP_032203;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family.
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DR EMBL; AB115695; BAD20938.1; -; mRNA.
DR EMBL; AK074423; BAB85079.1; -; mRNA.
DR EMBL; AK300374; BAG62110.1; -; mRNA.
DR EMBL; CH471055; EAW65342.1; -; Genomic_DNA.
DR EMBL; AL831824; CAD38538.1; -; mRNA.
DR RefSeq; NP_808881.3; NM_177966.5.
DR UniGene; Hs.572993; -.
DR ProteinModelPortal; Q6L8Q7; -.
DR SMR; Q6L8Q7; 300-607.
DR IntAct; Q6L8Q7; 1.
DR STRING; 9606.ENSP00000309142; -.
DR PhosphoSite; Q6L8Q7; -.
DR DMDM; 172046137; -.
DR PaxDb; Q6L8Q7; -.
DR PRIDE; Q6L8Q7; -.
DR DNASU; 201626; -.
DR Ensembl; ENST00000311180; ENSP00000309142; ENSG00000174840.
DR GeneID; 201626; -.
DR KEGG; hsa:201626; -.
DR UCSC; uc003diw.4; human.
DR CTD; 201626; -.
DR GeneCards; GC03P057541; -.
DR H-InvDB; HIX0003393; -.
DR HGNC; HGNC:25386; PDE12.
DR HPA; HPA043171; -.
DR neXtProt; NX_Q6L8Q7; -.
DR PharmGKB; PA162399016; -.
DR eggNOG; COG5239; -.
DR HOGENOM; HOG000006935; -.
DR HOVERGEN; HBG061027; -.
DR InParanoid; Q6L8Q7; -.
DR OMA; RWYKEAK; -.
DR OrthoDB; EOG7T4MJP; -.
DR PhylomeDB; Q6L8Q7; -.
DR GenomeRNAi; 201626; -.
DR NextBio; 90179; -.
DR PRO; PR:Q6L8Q7; -.
DR ArrayExpress; Q6L8Q7; -.
DR Bgee; Q6L8Q7; -.
DR CleanEx; HS_PDE12; -.
DR Genevestigator; Q6L8Q7; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.10.10; -; 1.
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 Alternative splicing; Complete proteome; Exonuclease; Hydrolase;
KW Magnesium; Metal-binding; Mitochondrion; mRNA processing; Nuclease;
KW Phosphoprotein; Polymorphism; Reference proteome; Transit peptide.
FT TRANSIT 1 16 Mitochondrion (Probable).
FT CHAIN 17 609 2',5'-phosphodiesterase 12.
FT /FTId=PRO_0000324312.
FT ACT_SITE 351 351 By similarity.
FT ACT_SITE 561 561 By similarity.
FT ACT_SITE 599 599 By similarity.
FT METAL 351 351 Magnesium 1 (By similarity).
FT METAL 496 496 Magnesium 2 (By similarity).
FT METAL 498 498 Magnesium 2 (By similarity).
FT METAL 599 599 Magnesium 2 (By similarity).
FT MOD_RES 217 217 Phosphoserine.
FT VAR_SEQ 527 535 EERCNMSLT -> GGFGGNFLL (in isoform 2).
FT /FTId=VSP_032202.
FT VAR_SEQ 536 609 Missing (in isoform 2).
FT /FTId=VSP_032203.
FT VARIANT 23 23 R -> W (in dbSNP:rs2241988).
FT /FTId=VAR_039698.
SQ SEQUENCE 609 AA; 67352 MW; 1D1F3AB4795B52A4 CRC64;
MWRLPGARAA LRVIRTAVEK LSRAEAGSQT AAGAMERAVV RCVPSEPKLS LSFALADGSH
KNMQRDQSEP LGRVLSRIAT NALKGHAKAA AAKKSRKSRP NASGGAACSG PGPEPAVFCE
PVVKLYYREE AVAEDVLNVD AWQDGAVLQI GDVKYKVERN PPAFTELQLP RYIMAGFPVC
PKLSLEFGDP ASSLFRWYKE AKPGAAEPEV GVPSSLSPSS PSSSWTETDV EERVYTPSNA
DIGLRLKLHC TPGDGQRFGH SRELESVCVV EAGPGTCTFD HRHLYTKKVT EDALIRTVSY
NILADTYAQT EFSRTVLYPY CAPYALELDY RQNLIQKELT GYNADVICLQ EVDRAVFSDS
LVPALEAFGL EGVFRIKQHE GLATFYRKSK FSLLSQHDIS FYEALESDPL HKELLEKLVL
YPSAQEKVLQ RSSVLQVSVL QSTKDSSKRI CVANTHLYWH PKGGYIRLIQ MAVALAHIRH
VSCDLYPGIP VIFCGDFNST PSTGMYHFVI NGSIPEDHED WASNGEEERC NMSLTHFFKL
KSACGEPAYT NYVGGFHGCL DYIFIDLNAL EVEQVIPLPS HEEVTTHQAL PSVSHPSDHI
ALVCDLKWK
//
ID PDE12_HUMAN Reviewed; 609 AA.
AC Q6L8Q7; B4DTU8; Q8IYU3; Q8NDU2; Q8TE78;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 75.
DE RecName: Full=2',5'-phosphodiesterase 12;
DE Short=2'-PDE;
DE Short=2-PDE;
DE EC=3.1.4.-;
DE AltName: Full=Mitochondrial deadenylase;
DE EC=3.1.13.4;
DE Flags: Precursor;
GN Name=PDE12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15231837; DOI=10.1074/jbc.M400089200;
RA Kubota K., Nakahara K., Ohtsuka T., Yoshida S., Kawaguchi J.,
RA Fujita Y., Ozeki Y., Hara A., Yoshimura C., Furukawa H., Haruyama H.,
RA Ichikawa K., Yamashita M., Matsuoka T., Iijima Y.;
RT "Identification of 2'-phosphodiesterase, which plays a role in the 2-
RT 5A system regulated by interferon.";
RL J. Biol. Chem. 279:37832-37841(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TRP-23.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-23.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-609 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21245038; DOI=10.1093/nar/gkq1282;
RA Poulsen J.B., Andersen K.R., Kjaer K.H., Durand F., Faou P.,
RA Vestergaard A.L., Talbo G.H., Hoogenraad N., Brodersen D.E.,
RA Justesen J., Martensen P.M.;
RT "Human 2'-phosphodiesterase localizes to the mitochondrial matrix with
RT a putative function in mitochondrial RNA turnover.";
RL Nucleic Acids Res. 39:3754-3770(2011).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=21666256; DOI=10.1093/nar/gkr470;
RA Rorbach J., Nicholls T.J., Minczuk M.;
RT "PDE12 removes mitochondrial RNA poly(A) tails and controls
RT translation in human mitochondria.";
RL Nucleic Acids Res. 39:7750-7763(2011).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, CATALYTIC ACTIVITY,
RP TRANSIT PEPTIDE, AND SUBCELLULAR LOCATION.
RX PubMed=22285541; DOI=10.1016/j.biochi.2012.01.012;
RA Poulsen J.B., Andersen K.R., Kjaer K.H., Vestergaard A.L.,
RA Justesen J., Martensen P.M.;
RT "Characterization of human phosphodiesterase 12 and identification of
RT a novel 2'-5' oligoadenylate nuclease - The ectonucleotide
RT pyrophosphatase/phosphodiesterase 1.";
RL Biochimie 94:1098-1107(2012).
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
CC 2-5A system. This enzyme degraded triphosphorylated 2-5A to
CC produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of
CC oligoadenylates. Plays a role as a negative regulator of the The
CC 2-5A system that is one of the major pathways for antiviral and
CC antitumor functions induced by interferons (IFNs). Suppression of
CC this enzyme induces reduction of viral replication in Hela cells,
CC thus counteracting the antiviral pathway probably by inhibiting
CC the 2-5A system.
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage of poly(A) to 5'-AMP.
CC -!- COFACTOR: Magnesium.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for 2'-5' oligoadenylate exonuclease activity;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6L8Q7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6L8Q7-2; Sequence=VSP_032202, VSP_032203;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family.
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DR EMBL; AB115695; BAD20938.1; -; mRNA.
DR EMBL; AK074423; BAB85079.1; -; mRNA.
DR EMBL; AK300374; BAG62110.1; -; mRNA.
DR EMBL; CH471055; EAW65342.1; -; Genomic_DNA.
DR EMBL; AL831824; CAD38538.1; -; mRNA.
DR RefSeq; NP_808881.3; NM_177966.5.
DR UniGene; Hs.572993; -.
DR ProteinModelPortal; Q6L8Q7; -.
DR SMR; Q6L8Q7; 300-607.
DR IntAct; Q6L8Q7; 1.
DR STRING; 9606.ENSP00000309142; -.
DR PhosphoSite; Q6L8Q7; -.
DR DMDM; 172046137; -.
DR PaxDb; Q6L8Q7; -.
DR PRIDE; Q6L8Q7; -.
DR DNASU; 201626; -.
DR Ensembl; ENST00000311180; ENSP00000309142; ENSG00000174840.
DR GeneID; 201626; -.
DR KEGG; hsa:201626; -.
DR UCSC; uc003diw.4; human.
DR CTD; 201626; -.
DR GeneCards; GC03P057541; -.
DR H-InvDB; HIX0003393; -.
DR HGNC; HGNC:25386; PDE12.
DR HPA; HPA043171; -.
DR neXtProt; NX_Q6L8Q7; -.
DR PharmGKB; PA162399016; -.
DR eggNOG; COG5239; -.
DR HOGENOM; HOG000006935; -.
DR HOVERGEN; HBG061027; -.
DR InParanoid; Q6L8Q7; -.
DR OMA; RWYKEAK; -.
DR OrthoDB; EOG7T4MJP; -.
DR PhylomeDB; Q6L8Q7; -.
DR GenomeRNAi; 201626; -.
DR NextBio; 90179; -.
DR PRO; PR:Q6L8Q7; -.
DR ArrayExpress; Q6L8Q7; -.
DR Bgee; Q6L8Q7; -.
DR CleanEx; HS_PDE12; -.
DR Genevestigator; Q6L8Q7; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.10.10; -; 1.
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 Alternative splicing; Complete proteome; Exonuclease; Hydrolase;
KW Magnesium; Metal-binding; Mitochondrion; mRNA processing; Nuclease;
KW Phosphoprotein; Polymorphism; Reference proteome; Transit peptide.
FT TRANSIT 1 16 Mitochondrion (Probable).
FT CHAIN 17 609 2',5'-phosphodiesterase 12.
FT /FTId=PRO_0000324312.
FT ACT_SITE 351 351 By similarity.
FT ACT_SITE 561 561 By similarity.
FT ACT_SITE 599 599 By similarity.
FT METAL 351 351 Magnesium 1 (By similarity).
FT METAL 496 496 Magnesium 2 (By similarity).
FT METAL 498 498 Magnesium 2 (By similarity).
FT METAL 599 599 Magnesium 2 (By similarity).
FT MOD_RES 217 217 Phosphoserine.
FT VAR_SEQ 527 535 EERCNMSLT -> GGFGGNFLL (in isoform 2).
FT /FTId=VSP_032202.
FT VAR_SEQ 536 609 Missing (in isoform 2).
FT /FTId=VSP_032203.
FT VARIANT 23 23 R -> W (in dbSNP:rs2241988).
FT /FTId=VAR_039698.
SQ SEQUENCE 609 AA; 67352 MW; 1D1F3AB4795B52A4 CRC64;
MWRLPGARAA LRVIRTAVEK LSRAEAGSQT AAGAMERAVV RCVPSEPKLS LSFALADGSH
KNMQRDQSEP LGRVLSRIAT NALKGHAKAA AAKKSRKSRP NASGGAACSG PGPEPAVFCE
PVVKLYYREE AVAEDVLNVD AWQDGAVLQI GDVKYKVERN PPAFTELQLP RYIMAGFPVC
PKLSLEFGDP ASSLFRWYKE AKPGAAEPEV GVPSSLSPSS PSSSWTETDV EERVYTPSNA
DIGLRLKLHC TPGDGQRFGH SRELESVCVV EAGPGTCTFD HRHLYTKKVT EDALIRTVSY
NILADTYAQT EFSRTVLYPY CAPYALELDY RQNLIQKELT GYNADVICLQ EVDRAVFSDS
LVPALEAFGL EGVFRIKQHE GLATFYRKSK FSLLSQHDIS FYEALESDPL HKELLEKLVL
YPSAQEKVLQ RSSVLQVSVL QSTKDSSKRI CVANTHLYWH PKGGYIRLIQ MAVALAHIRH
VSCDLYPGIP VIFCGDFNST PSTGMYHFVI NGSIPEDHED WASNGEEERC NMSLTHFFKL
KSACGEPAYT NYVGGFHGCL DYIFIDLNAL EVEQVIPLPS HEEVTTHQAL PSVSHPSDHI
ALVCDLKWK
//