CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018166
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly(A)-specific ribonuclease PARN 
Protein Synonyms/Alias
 Polyadenylate-specific ribonuclease 
Gene Name
 Parn 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
508TYAEYVGKKQEGKQVacetylation[1]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (By similarity). 
Sequence Annotation
 DOMAIN 171 238 R3H.
 METAL 28 28 Divalent metal cation; catalytic (By
 METAL 30 30 Divalent metal cation; catalytic (By
 METAL 285 285 Divalent metal cation; catalytic (By
 METAL 375 375 Divalent metal cation; catalytic (By
 MOD_RES 213 213 N6-acetyllysine (By similarity).
 MOD_RES 492 492 N6-acetyllysine (By similarity).
 MOD_RES 543 543 Phosphoserine; by MAPKAPK2 (By
 MOD_RES 573 573 Phosphoserine.
 MOD_RES 575 575 Phosphoserine.
 MOD_RES 605 605 Phosphoserine (By similarity).
 MOD_RES 609 609 Phosphoserine (By similarity).
 MOD_RES 613 613 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 624 AA 
Protein Sequence
MEIIRSNFKI NLHKVYQAIE EADFFAIDGE FSGISDGPSV TALTSGFDTP EERYQKLKKH 60
SMDFLLFQFG LCAFKYDHTD SKHVTKSFNF YVFPKPFSRS SPDVKFVCQS SSIDFLASQG 120
FDFNKVFCSG IPYLNQEEER QLREQFDEKR SQANGAGALA KCPVTIPEDQ KKFIDQVIEK 180
IEDFLQSEEK RSLELDPCTG FQRKLIYQTL SWKYPKGIHV ETLETDKKER HIVISKVDEE 240
ERKRREQEKY TKEQEELNDA VGFSRVIHAI ANSGKLVVGH NMLLDVMHTI HQFYCPLPAD 300
LNEFKEMAIC VFPRLLDTKL MASTQPFKDI INNTSLAELE KRLKETPFDP PKVESAEGFP 360
SYDTASEQLH EAGYDAYITG LCFISMANYL GSLLSPPKMC VSARSKLIEP FFNKLFLMRV 420
MDIPYLNLEG PDLQPKRDHV LHVTFPKEWK TSDLYQLFSA FGNIQISWID DTSAFVSLSQ 480
PEQVQIAVNT SKYAESYRIQ TYAEYVGKKQ EGKQVKRKWT EDSWKEVDRK RPHMQGPCYH 540
SNSFTAAGVL GKRTLSPDPR EAALEDRESE EVSDSELEQT DSCTDPLPEG RKKSKKLKRM 600
KKELSLAGSV SDSPAVLFEV PDTW 624 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:EC.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
 GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:MGI.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR014789; PolyA-riboNase_RNA_binding.
 IPR001374; R3H_ss-bd.
 IPR006941; RNase_CAF1.
 IPR012337; RNaseH-like_dom. 
Pfam
 PF04857; CAF1
 PF01424; R3H
 PF08675; RNA_bind 
SMART
  
PROSITE
 PS51061; R3H 
PRINTS