Reviewed, UniProtKB/Swiss-Prot Q8K1R3 (PNPT1_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	783 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	RNA-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro mRNA catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 45

45

Mitochondrion Potential

Chain

46 – 783

738

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

PRO_0000024752

Regions

Domain

605 – 664

60

KH

Domain

679 – 750

72

S1 motif

Amino acid modifications

Modified residue

124

1

Phosphoserine By similarity

Modified residue

758

1

Phosphothreonine By similarity

Modified residue

776

1

Phosphoserine By similarity

Natural variations

Alternative sequence

535 – 540

6

GIEDYN → ASIFPV in isoform 2.

VSP_013639

Alternative sequence

541 – 783

243

Missing in isoform 2.

VSP_013640

Experimental info

Sequence conflict

90

1

A → P in AAO33354. Ref.2

Sequence conflict

298

1

V → G in AAO33354. Ref.2

Sequence conflict

315

1

K → Q in AAO33354. Ref.2

Sequence conflict

415

1

I → V in AAO33354. Ref.2

Sequence conflict

431

1

P → L in BAB23374. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

783

Helix Strand Turn

Details...

Helix

281 – 299

19

Helix

307 – 324

18

Turn

325 – 327

3

Beta strand

329 – 331

3

Helix

333 – 352

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: F35F6BE91AAB5626	FASTA	783	85,683
	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
	Isoform 2. Checksum: E57BFA2B602361C4	FASTA	540	58,923
	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 TDILASIFPV

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

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.

IPI

IPI00321923.
IPI00556889.

RefSeq

NP_082145.1.
XP_001472157.1.

UniGene

Mm.211131

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WHU	NMR	-	A	273-363	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q8K1R3.

Proteomic databases

PRIDE

Q8K1R3.

Genome annotation databases

Ensembl

ENSMUSG00000020464. Mus musculus. [Contig view]

GeneID

100044383.
71701.

KEGG

mmu:100044383.
mmu:71701.

Organism-specific databases

MGI

MGI:1918951. Pnpt1.

Phylogenomic databases

HOGENOM

Q8K1R3.

HOVERGEN

Q8K1R3.

OMA

Q8K1R3. DFPFTIR.

Enzyme and pathway databases

BRENDA

2.7.7.8. 244.

Gene expression databases

ArrayExpress

Q8K1R3.

Bgee

Q8K1R3.

GermOnline

ENSMUSG00000020464. Mus musculus.

Family and domain databases

InterPro

IPR001247. 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]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:1.10.10.400. PNPase_PH_RNA-bd_bac/org-type. 1 hit.

PANTHER

PTHR11252. PNPase. 1 hit.

Pfam

PF00013. 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]

PIRSF

PIRSF005499. PNPase. 1 hit.

SMART

SM00322. KH. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03591. Polynuc_phos. 1 hit.

PROSITE

PS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

457882.

SOURCE

Search...

Entry information

Entry name

PNPT1_MOUSE

Accession

Primary (citable) accession number: Q8K1R3
Secondary accession number(s): Q3UEP9 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)