ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8K1R3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PNPT1_MOUSE
Primary accession number Q8K1R3
Secondary accession numbers Q3UEP9 Q810U7 Q812B3 Q8R2U3 Q9DC52
Integrated into Swiss-Prot on May 10, 2005
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Polyribonucleotide nucleotidyltransferase 1, mitochondrial [Precursor]
Synonyms EC 2.7.7.8
PNPase 1
Polynucleotide phosphorylase-like protein
PNPase old-35
3'-5' RNA exonuclease OLD35
Gene name
Name: Pnpt1
Synonyms: Pnpase
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1016/S0022-2836(02)00947-6; PubMed=12419256 [NCBI, ExPASy, EBI, Israel, Japan]
Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.;
"Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring.";
J. Mol. Biol. 323:653-663(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Leszczyniecka M., Fisher P.B.;
"Cloning of mouse homolog of old-35.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
TISSUE=Liver, and Lung;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N;
TISSUE=Mammary gland, and Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
STRUCTURE BY NMR OF 273-363.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the alpha-helical domain from mouse hypothetical PNPase.";
Submitted (NOV-2004) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ507387; CAD45436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF465249; AAO33354.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004563; BAB23374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK149419; BAE28862.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX000351; CAI25081.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027228; AAH27228.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC049283; AAH49283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC055826; AAH55826.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_082145.1; -.
XP_001472157.1; -.
UniGene Mm.211131
3D structure databases
PDB
1WHU; NMR; -; A=273-363.[ExPASy / RCSB / EBI]
PDBsum 1WHU; -.
ModBase Q8K1R3.
PTM databases
PhosphoSite Q8K1R3; -.
Organism-specific databases
MGI MGI:1918951; Pnpt1.
Gene expression databases
ArrayExpress Q8K1R3; -.
GermOnline ENSMUSG00000020464; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0000175; Molecular function: 3'-5'-exoribonuclease activity (inferred from electronic annotation from InterPro).
GO:0004654; Molecular function: polyribonucleotide nucleotidyltransferase activity (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0006402; Biological process: mRNA catabolic process (inferred from electronic annotation from InterPro).
GO:0006396; Biological process: RNA processing (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001247; ExoRNase_PH_dom1.
IPR015847; ExoRNase_PH_dom2.
IPR004087; KH.
IPR004088; KH_type_1.
IPR012340; NA-bd_OB-fold.
IPR012162; PNPase.
IPR015848; PNPase_PH_RNA-bd_bac/org-type.
IPR003029; S1_RNA-bd.
Graphical view of domain structure.
Gene3D G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
G3DSA:1.10.10.400; PNPase_PH_RNA-bd_bac/org-type; 1.
PANTHER PTHR11252; PNPase; 1.
Pfam PF00013; KH_1; 1.
PF03726; PNPase; 1.
PF01138; RNase_PH; 2.
PF03725; RNase_PH_C; 2.
PF00575; S1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005499; PNPase; 1.
SMART SM00322; KH; 1.
SM00316; S1; 1.
SMART graphical view of domain structure.
PROSITE PS50084; KH_TYPE_1; 1.
PS50126; S1; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8K1R3.
Genome annotation databases
Ensembl ENSMUSG00000020464; Mus musculus. [Contig view]
GeneID 100044383; -.
71701; -.
KEGG mmu:100044383; -.
mmu:71701; -.
Phylogenomic databases
HOGENOM Q8K1R3; -.
HOVERGEN Q8K1R3; -.
Other
NextBio 457882; -.
SOURCE Pnpt1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Mitochondrion; Nucleotidyltransferase; Phosphoprotein; RNA-binding; Transferase; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    45  45     Mitochondrion (Potential). 
CHAIN   46   783  738     Polyribonucleotide nucleotidyltransferase 1, mitochondrial. PRO_0000024752
DOMAIN   605   664  60     KH. 
DOMAIN   679   750  72     S1 motif. 
MOD_RES   124   124        Phosphoserine (By similarity). 
MOD_RES   758   758        Phosphothreonine (By similarity). 
MOD_RES   776   776        Phosphoserine (By similarity). 
VAR_SEQ   535   540        GIEDYN -> ASIFPV (in isoform 2). VSP_013639
VAR_SEQ   541   783        Missing (in isoform 2). VSP_013640
CONFLICT   90    90        A -> P (in Ref. 2; AAO33354). 
CONFLICT   298   298        V -> G (in Ref. 2; AAO33354). 
CONFLICT   315   315        K -> Q (in Ref. 2; AAO33354). 
CONFLICT   415   415        I -> V (in Ref. 2; AAO33354). 
CONFLICT   431   431        P -> L (in Ref. 3; BAB23374). 
HELIX   281   299  19      
HELIX   307   324  18      
TURN   325   327  3      
STRAND   329   331  3      
HELIX   333   352  20      
Sequence information
Length: 783 AA [This is the length of the unprocessed precursor] Molecular weight: 85683 Da [This is the MW of the unprocessed precursor] CRC64: F35F6BE91AAB5626 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAACRLCCLC PCLRPLGCGP LGRPGRNRAL SYLQMRALWS STGSRAVTVD LGHRKLEISS 

        70         80         90        100        110        120 
GKLARFADGC AVIQSGDTAV MVTAVSKTKA SPSQFMPLVV DYRQKAAAAG RIPTNYLRRE 

       130        140        150        160        170        180 
IGSSDREVLT SRVIDRSIRP LFPAGYFYDT QVLCNLLAVD GINEPDILAV NGASVALSLS 

       190        200        210        220        230        240 
DIPWNGPVGA VRIGMIDGEC VVNPTRREMS SSTLNLVVAG APKSQIVMLE ASAENILQQD 

       250        260        270        280        290        300 
FCHAIKVGVK YTQQIIQGIQ QLVKEIGVAK RTPQKIFTPS AEIVKYTKII AMEKLYAVFT 

       310        320        330        340        350        360 
DYEHDKVSRD EAVNKIRLDT EEHLKEKFPE VDQFEIIESF NIVAKEVFRS IILNEYKRCD 

       370        380        390        400        410        420 
GRDLTSLRNI SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD SLESSIKSDQ IITAINGVKD 

       430        440        450        460        470        480 
KNFMLHYEFP PYATNETGKV TGVNRRELGH GALAEKALCP VIPKDFPFTI RVTSEVLESN 

       490        500        510        520        530        540 
GSSSMASACG GSLALMDAGV PISSAVAGVA VGLVTKTNPE KGEIEDYRLL TDILGIEDYN 

       550        560        570        580        590        600 
GDMDFKIAGT NKGITALQAD IKLPGVPIKI IMEAIQQASV AKKEILQIMN KTISKPRASR 

       610        620        630        640        650        660 
KENGPVVETV KVPLSKRAKF VGPGGYHLKK LQAETGVTIS QVDEETFSIF APTPTAMHEA 

       670        680        690        700        710        720 
RDFITEICRD DQEQQLEFGA VYTATITEIR DTGVMVKLYP NMTAVLLHNS QLDQRKIKHP 

       730        740        750        760        770        780 
TALGLEVGQE IQVKYFGRDP ADGRMRLSRK VLQSPATTAL KTLNDRSSIV MGEPVSQSSN 


SNP 

Q8K1R3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!