Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8K1R3 (PNPT1_MOUSE)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Polyribonucleotide nucleotidyltransferase 1, mitochondrial
    EC=2.7.7.8
Alternative name(s):
    PNPase 1
    Polynucleotide phosphorylase-like protein
    PNPase old-35
    3'-5' RNA exonuclease OLD35
Gene names
Name: Pnpt1
Synonyms: Pnpase
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction By similarity.

Catalytic activity

RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate.

Subunit structure

Homotrimer Potential. Interacts with TCL1A; the interaction has no effect on PNPT1 exonuclease activity By similarity.

Subcellular location

Mitochondrion By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Contains 1 KH domain.

Contains 1 S1 motif domain.

Sequence caution

The sequence AAO33354.1 differs from that shown. Reason: Frameshift at positions 3, 6, 20, 23, 273, 286, 300, 312, 314, 320 and 325.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandRNA-binding
   Molecular functionNucleotidyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processRNA processing

Inferred from electronic annotation. Source: InterPro

mRNA catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3'-5'-exoribonuclease activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

polyribonucleotide nucleotidyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K1R3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8K1R3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     535-540: GIEDYN → ASIFPV
     541-783: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4545Mitochondrion Potential
Chain46 – 783738Polyribonucleotide nucleotidyltransferase 1, mitochondrial
PRO_0000024752

Regions

Domain605 – 66460KH
Domain679 – 75072S1 motif

Amino acid modifications

Modified residue1241Phosphoserine By similarity
Modified residue7581Phosphothreonine By similarity
Modified residue7761Phosphoserine By similarity

Natural variations

Alternative sequence535 – 5406GIEDYN → ASIFPV in isoform 2.
VSP_013639
Alternative sequence541 – 783243Missing in isoform 2.
VSP_013640

Experimental info

Sequence conflict901A → P in AAO33354. Ref.2
Sequence conflict2981V → G in AAO33354. Ref.2
Sequence conflict3151K → Q in AAO33354. Ref.2
Sequence conflict4151I → V in AAO33354. Ref.2
Sequence conflict4311P → L in BAB23374. Ref.3

Secondary structure

.......... 783
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: F35F6BE91AAB5626

FASTA78385,683
        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 

« Hide

Isoform 2.

Checksum: E57BFA2B602361C4
Show »

FASTA54058,923

References

« Hide 'large scale' references
[1]"Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring."
Raijmakers R., Vree Egberts W., van Venrooij W.J., Pruijn G.J.M.
J. Mol. Biol. 323:653-663(2002) [PubMed: 12419256] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of mouse homolog of old-35."
Leszczyniecka M., Fisher P.B.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Liver and Lung.
[4]The mouse genome sequencing consortium
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary gland and Mammary tumor.
[6]"Solution structure of the alpha-helical domain from mouse hypothetical PNPase."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 273-363.

Cross-references

Sequence databases

AJ507387 mRNA. Translation: CAD45436.1.
AF465249 mRNA. Translation: AAO33354.1. Frameshift.
AK004563 mRNA. Translation: BAB23374.1.
AK149419 mRNA. Translation: BAE28862.1.
BX000351 Genomic DNA. Translation: CAI25081.1.
BC027228 mRNA. Translation: AAH27228.2.
BC049283 mRNA. Translation: AAH49283.1.
BC055826 mRNA. Translation: AAH55826.1.
IPIIPI00321923.
IPI00556889.
RefSeqNP_082145.1.
XP_001472157.1.
UniGeneMm.211131

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WHUNMR-A273-363[»]
ModBaseSearch...

PTM databases

PhosphoSiteQ8K1R3.

Proteomic databases

PRIDEQ8K1R3.

Genome annotation databases

EnsemblENSMUSG00000020464. Mus musculus. [Contig view]
GeneID100044383.
71701.
KEGGmmu:100044383.
mmu:71701.

Organism-specific databases

MGIMGI:1918951. Pnpt1.

Phylogenomic databases

HOGENOMQ8K1R3.
HOVERGENQ8K1R3.
OMAQ8K1R3. DFPFTIR.

Enzyme and pathway databases

BRENDA2.7.7.8. 244.

Gene expression databases

ArrayExpressQ8K1R3.
BgeeQ8K1R3.
GermOnlineENSMUSG00000020464. Mus musculus.

Family and domain databases

InterProIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH.
IPR004088. KH_type_1.
IPR018111. KH_type_1_subgr.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR015848. PNPase_PH_RNA-bd_bac/org-type.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit.
PANTHERPTHR11252. PNPase. 1 hit.
PfamPF00013. KH_1. 1 hit.
PF03726. PNPase. 1 hit.
PF01138. RNase_PH. 2 hits.
PF03725. RNase_PH_C. 2 hits.
PF00575. S1. 1 hit.
[Graphical view]
PIRSFPIRSF005499. PNPase. 1 hit.
SMARTSM00322. KH. 1 hit.
[Graphical view]
TIGRFAMsTIGR03591. Polynuc_phos. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio457882.
SOURCESearch...

Entry information

Entry namePNPT1_MOUSE
AccessionPrimary (citable) accession number: Q8K1R3
Secondary accession number(s): Q3UEP9 expand/collapse secondary AC list , Q810U7, Q812B3, Q8R2U3, Q9DC52
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents