Tag | Content |
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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 |
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508 | TYAEYVGKKQEGKQV | acetylation | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |