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Q5RCW2

- PNPT1_PONAB

UniProt

Q5RCW2 - PNPT1_PONAB

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Protein

Polyribonucleotide nucleotidyltransferase 1, mitochondrial

Gene

PNPT1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: UniProtKB
  2. miRNA binding Source: UniProtKB
  3. poly(G) binding Source: UniProtKB
  4. poly(U) RNA binding Source: UniProtKB
  5. polyribonucleotide nucleotidyltransferase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to oxidative stress Source: UniProtKB
  2. mitochondrial mRNA catabolic process Source: UniProtKB
  3. mitochondrial mRNA polyadenylation Source: UniProtKB
  4. mitochondrial RNA 3'-end processing Source: UniProtKB
  5. mitochondrial RNA 5'-end processing Source: UniProtKB
  6. mitochondrial RNA catabolic process Source: UniProtKB
  7. mitochondrion morphogenesis Source: UniProtKB
  8. mitotic cell cycle arrest Source: UniProtKB
  9. mRNA catabolic process Source: UniProtKB
  10. negative regulation of growth Source: UniProtKB
  11. nuclear polyadenylation-dependent mRNA catabolic process Source: UniProtKB
  12. positive regulation of miRNA catabolic process Source: UniProtKB
  13. positive regulation of mitochondrial RNA catabolic process Source: UniProtKB
  14. positive regulation of mRNA catabolic process Source: UniProtKB
  15. protein homooligomerization Source: UniProtKB
  16. protein homotrimerization Source: UniProtKB
  17. regulation of cellular respiration Source: UniProtKB
  18. regulation of cellular senescence Source: UniProtKB
  19. RNA catabolic process Source: UniProtKB
  20. RNA import into mitochondrion Source: UniProtKB
  21. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  22. RNA polyadenylation Source: UniProtKB
  23. rRNA import into mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA processing, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC:2.7.7.8)
Alternative name(s):
Polynucleotide phosphorylase 1
Short name:
PNPase 1
Gene namesi
Name:PNPT1
Synonyms:PNPASE
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion intermembrane space By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. membrane Source: UniProtKB-KW
  2. mitochondrial degradosome Source: UniProtKB
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence AnalysisAdd
BLAST
Chaini47 – 783737Polyribonucleotide nucleotidyltransferase 1, mitochondrialPRO_0000024753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei250 – 2501N6-acetyllysineBy similarity
Modified residuei264 – 2641N6-acetyllysineBy similarity
Modified residuei285 – 2851N6-acetyllysineBy similarity
Modified residuei289 – 2891N6-acetyllysineBy similarity
Modified residuei552 – 5521N6-succinyllysineBy similarity
Modified residuei782 – 7821PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5RCW2.

Interactioni

Subunit structurei

Homotrimer; in free form. Homooligomer. Component of the mitochondrial degradosome (mtEXO) complex which is a heteropentamer containing 2 copies of SUPV3L1 and 3 copies of PNPT1. Interacts with TCL1A; the interaction has no effect on PNPT1 exonuclease activity (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5RCW2.
SMRiQ5RCW2. Positions 273-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini605 – 66460KHPROSITE-ProRule annotationAdd
BLAST
Domaini679 – 75072S1 motifPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 KH domain.PROSITE-ProRule annotation
Contains 1 S1 motif domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG053625.
InParanoidiQ5RCW2.
KOiK00962.

Family and domain databases

Gene3Di1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR027408. PNPase/RNase_PH_dom.
IPR015848. PNPase_PH_RNA-bd_bac/org-type.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR022967. S1_dom.
[Graphical view]
PANTHERiPTHR11252. PTHR11252. 1 hit.
PfamiPF00013. 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]
PIRSFiPIRSF005499. PNPase. 1 hit.
SMARTiSM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF46915. SSF46915. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsiTIGR03591. polynuc_phos. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5RCW2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAACRYCCSC LRLRPLSDGP FCLPGRDRAL TQLLVRALWS STGSRAVAVD
60 70 80 90 100
LGNRKLEISS GKLARFADGS AVVQSGDTAV MVTAVSKTKP SPSQFMPLVV
110 120 130 140 150
DYRQKAAAAG RIPTNYLRRE IGTSDKEILT SRIIDRSIRP LFPAGYFYDT
160 170 180 190 200
QVLCNLLAVD GVNEPDVLAI NGASVALSLS DIPWNGPVGA VRIGIIDGEC
210 220 230 240 250
VVNPTRKEMS SSTLNLVVAG APKSQIVMLE ASAENILQQD FCHAIKVGVK
260 270 280 290 300
YTQQIIQGIQ QLVKETGVTK RTPQKLFTPS PEIVKHTHKL AMERLYAVFT
310 320 330 340 350
DYEHDKVSRD EAVNKIRLDT EEQLKEKFPQ ADPYEIIESF NVVAKEVFRN
360 370 380 390 400
IILNEYKRCD GRDLTSLRNV SCEVDMFKTL HGSALFQRGQ TQVLCTVTFD
410 420 430 440 450
SLESGIKSDQ VITAINGIKD KNFMLHYEFP PYATNEIGKV TGLNRRELGH
460 470 480 490 500
GALAEKALYP VIPRDFPFTI RVTSEVLESN GSSSMASACG GSLALMDSGV
510 520 530 540 550
PISSAVAGVA IGLVTKTDPE KGEIEDYRLL TDILGIEDYN GDMDFKIAGT
560 570 580 590 600
NKGITALQAD IKLPGIPIKI VMEAIQQASV AKKEILQIMN KTISKPRTSR
610 620 630 640 650
KENGPVVETV QVPLSKRAKF VGPGGYNLKK LQAETGVTIS QVDEETFSVF
660 670 680 690 700
APTPSALHEA RDFITEICKD DQEQQLEFGA VYTATITEIR DTGVMVKLYP
710 720 730 740 750
NMTAVLLHNT QLDQRKIRHP TALGLEVGQE IQVKYFGRDP ADGRMRLSRK
760 770 780
VLQSPATTVV RTLNDRSSIV MGEPISQSSS NSQ
Length:783
Mass (Da):85,851
Last modified:May 10, 2005 - v2
Checksum:iC9AE6896AC130CA8
GO

Sequence cautioni

The sequence CAH90395.1 differs from that shown. Reason: Frameshift at position 75.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858156 mRNA. Translation: CAH90395.1. Frameshift.
RefSeqiNP_001125193.1. NM_001131721.1.
UniGeneiPab.14131.

Genome annotation databases

GeneIDi100172084.
KEGGipon:100172084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR858156 mRNA. Translation: CAH90395.1 . Frameshift.
RefSeqi NP_001125193.1. NM_001131721.1.
UniGenei Pab.14131.

3D structure databases

ProteinModelPortali Q5RCW2.
SMRi Q5RCW2. Positions 273-363.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5RCW2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100172084.
KEGGi pon:100172084.

Organism-specific databases

CTDi 87178.

Phylogenomic databases

HOVERGENi HBG053625.
InParanoidi Q5RCW2.
KOi K00962.

Family and domain databases

Gene3Di 1.10.10.400. 1 hit.
2.40.50.140. 1 hit.
3.30.1370.10. 1 hit.
3.30.230.70. 2 hits.
InterProi IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012340. NA-bd_OB-fold.
IPR012162. PNPase.
IPR027408. PNPase/RNase_PH_dom.
IPR015848. PNPase_PH_RNA-bd_bac/org-type.
IPR003029. Rbsml_prot_S1_RNA-bd_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR022967. S1_dom.
[Graphical view ]
PANTHERi PTHR11252. PTHR11252. 1 hit.
Pfami 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 ]
PIRSFi PIRSF005499. PNPase. 1 hit.
SMARTi SM00322. KH. 1 hit.
SM00316. S1. 1 hit.
[Graphical view ]
SUPFAMi SSF46915. SSF46915. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54211. SSF54211. 2 hits.
SSF54791. SSF54791. 1 hit.
SSF55666. SSF55666. 2 hits.
TIGRFAMsi TIGR03591. polynuc_phos. 1 hit.
PROSITEi PS50084. KH_TYPE_1. 1 hit.
PS50126. S1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiPNPT1_PONAB
AccessioniPrimary (citable) accession number: Q5RCW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: October 29, 2014
This is version 66 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3