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Protein

2',5'-phosphodiesterase 12

Gene

Pde12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. 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 interferon (IFNs) (By similarity).By similarity

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei350 – 3501By similarity
Metal bindingi350 – 3501Magnesium 1By similarity
Metal bindingi495 – 4951Magnesium 2By similarity
Metal bindingi497 – 4971Magnesium 2By similarity
Active sitei560 – 5601By similarity
Active sitei598 – 5981By similarity
Metal bindingi598 – 5981Magnesium 2By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
2',5'-phosphodiesterase 12 (EC:3.1.4.-)
Short name:
2'-PDE
Short name:
2-PDE
Alternative name(s):
Mitochondrial deadenylase (EC:3.1.13.4)
Gene namesi
Name:Pde12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:2443226. Pde12.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616MitochondrionBy similarityAdd
BLAST
Chaini17 – 6085922',5'-phosphodiesterase 12PRO_0000324313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3TIU4.
MaxQBiQ3TIU4.
PaxDbiQ3TIU4.
PeptideAtlasiQ3TIU4.
PRIDEiQ3TIU4.

PTM databases

iPTMnetiQ3TIU4.
PhosphoSiteiQ3TIU4.

Expressioni

Gene expression databases

BgeeiQ3TIU4.
GenevisibleiQ3TIU4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059666.

Structurei

3D structure databases

ProteinModelPortaliQ3TIU4.
SMRiQ3TIU4. Positions 160-608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CCR4/nocturin family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0620. Eukaryota.
COG5239. LUCA.
GeneTreeiENSGT00550000074364.
HOGENOMiHOG000006935.
HOVERGENiHBG061027.
InParanoidiQ3TIU4.
KOiK19612.
OMAiDSSKRIC.
OrthoDBiEOG7T4MJP.
PhylomeDBiQ3TIU4.
TreeFamiTF323175.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3TIU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRLPGRSAL RGVRSVVERR SRAEAGTHEA VRAMERAVVR CVPSEPKLSL
60 70 80 90 100
SFALADGSHK NMQRDQSEPL GRALSRIATN ALKGHAKVAA AKKSRKNRAH
110 120 130 140 150
SSGGAACEAT GPEPVATCEP VVKLYYREEA VAEDVLNVDA WQDGAVLQIG
160 170 180 190 200
DVKYKVERNP PTFTELQLPR YIMAGFPVCP KLGVEFGDPA SSVFRWYKEV
210 220 230 240 250
KPGAAEPGDS GPASSSHSSQ PSAWIETGVD ERVYTPCNAD IGLRLRLHCT
260 270 280 290 300
PGNGQRFGPS RELESLCPVE AGPGTCTFDH RHLYTKKVTE DSFIRTVSYN
310 320 330 340 350
ILADTYAQTE FSRTVLYPYC APYALELDYR QNLIQKELTG YNADLICLQE
360 370 380 390 400
VDRAVFSDSL VPALEAFGLE GVFRIKQHEG LATFYRKSKF RLLSQHDISF
410 420 430 440 450
QEALKSDPLH KELLEKLALN PLAQEKVLQR SSVLQISVLQ STTDSSKKIC
460 470 480 490 500
VANTHLYWHP KGGYIRLIQM EVALVHIRHV SRDLYPGIPV IFCGDFNSTP
510 520 530 540 550
STGMYHFVIS GSIAEDHEDW ASNGEEERCS MPLSHCFKLK SACGEPAYTN
560 570 580 590 600
YVGGFHGCLD YIFIDLNTLE VEQVIPLPSH EEVTTHQALP SVSHPSDHIA

LVCDLKWK
Length:608
Mass (Da):67,514
Last modified:March 18, 2008 - v2
Checksum:iDC67C45DE3FF556C
GO

Sequence cautioni

The sequence BAC34827.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 222SR → TG in BAC38703 (PubMed:16141072).Curated
Sequence conflicti104 – 1041G → S in BAC40606 (PubMed:16141072).Curated
Sequence conflicti104 – 1041G → S in BAE33039 (PubMed:16141072).Curated
Sequence conflicti123 – 1231K → E in BAE39752 (PubMed:16141072).Curated
Sequence conflicti471 – 4711E → A in BAC40606 (PubMed:16141072).Curated
Sequence conflicti471 – 4711E → A in BAE33039 (PubMed:16141072).Curated
Sequence conflicti493 – 4931C → G in BAE36189 (PubMed:16141072).Curated
Sequence conflicti523 – 5231N → H in BAE36189 (PubMed:16141072).Curated
Sequence conflicti538 – 5381K → Q in BAE36189 (PubMed:16141072).Curated
Sequence conflicti578 – 5781P → L in BAE39752 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK051991 mRNA. Translation: BAC34827.1. Different initiation.
AK082947 mRNA. Translation: BAC38703.1.
AK088843 mRNA. Translation: BAC40606.1.
AK155088 mRNA. Translation: BAE33039.1.
AK161083 mRNA. Translation: BAE36189.1.
AK167708 mRNA. Translation: BAE39752.1.
BC064450 mRNA. Translation: AAH64450.1.
CCDSiCCDS26882.1.
RefSeqiNP_848783.3. NM_178668.3.
UniGeneiMm.290758.
Mm.491244.

Genome annotation databases

EnsembliENSMUST00000052932; ENSMUSP00000059666; ENSMUSG00000043702.
GeneIDi211948.
KEGGimmu:211948.
UCSCiuc007stb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK051991 mRNA. Translation: BAC34827.1. Different initiation.
AK082947 mRNA. Translation: BAC38703.1.
AK088843 mRNA. Translation: BAC40606.1.
AK155088 mRNA. Translation: BAE33039.1.
AK161083 mRNA. Translation: BAE36189.1.
AK167708 mRNA. Translation: BAE39752.1.
BC064450 mRNA. Translation: AAH64450.1.
CCDSiCCDS26882.1.
RefSeqiNP_848783.3. NM_178668.3.
UniGeneiMm.290758.
Mm.491244.

3D structure databases

ProteinModelPortaliQ3TIU4.
SMRiQ3TIU4. Positions 160-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000059666.

PTM databases

iPTMnetiQ3TIU4.
PhosphoSiteiQ3TIU4.

Proteomic databases

EPDiQ3TIU4.
MaxQBiQ3TIU4.
PaxDbiQ3TIU4.
PeptideAtlasiQ3TIU4.
PRIDEiQ3TIU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052932; ENSMUSP00000059666; ENSMUSG00000043702.
GeneIDi211948.
KEGGimmu:211948.
UCSCiuc007stb.1. mouse.

Organism-specific databases

CTDi201626.
MGIiMGI:2443226. Pde12.

Phylogenomic databases

eggNOGiKOG0620. Eukaryota.
COG5239. LUCA.
GeneTreeiENSGT00550000074364.
HOGENOMiHOG000006935.
HOVERGENiHBG061027.
InParanoidiQ3TIU4.
KOiK19612.
OMAiDSSKRIC.
OrthoDBiEOG7T4MJP.
PhylomeDBiQ3TIU4.
TreeFamiTF323175.

Miscellaneous databases

ChiTaRSiPde12. mouse.
PROiQ3TIU4.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TIU4.
GenevisibleiQ3TIU4. MM.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Eye, Placenta, Skin, Spinal cord and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPDE12_MOUSE
AccessioniPrimary (citable) accession number: Q3TIU4
Secondary accession number(s): Q3TTY4
, Q6P2L5, Q8BKH8, Q8BTS8, Q8BUQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: July 6, 2016
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.