PARN_BOVIN
ID PARN_BOVIN Reviewed; 638 AA.
AC P69341; A6QQW2;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Poly(A)-specific ribonuclease PARN;
DE EC=3.1.13.4;
DE AltName: Full=Deadenylating nuclease;
DE AltName: Full=Deadenylation nuclease;
DE AltName: Full=Polyadenylate-specific ribonuclease;
GN Name=PARN; Synonyms=DAN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 86-105; 259-267; 421-429 AND 499-514, AND FUNCTION.
RX PubMed=9736620; DOI=10.1093/emboj/17.18.5427;
RA Koerner C.G., Wormington M., Muckenthaler M., Schneider S., Dehlin E.,
RA Wahle E.;
RT "The deadenylating nuclease (DAN) is involved in poly(A) tail removal
RT during the meiotic maturation of Xenopus oocytes.";
RL EMBO J. 17:5427-5437(1998).
RN [3]
RP ENZYME ACTIVITY.
RX PubMed=9099687; DOI=10.1074/jbc.272.16.10448;
RA Koerner C.G., Wahle E.;
RT "Poly(A) tail shortening by a mammalian poly(A)-specific 3'-
RT exoribonuclease.";
RL J. Biol. Chem. 272:10448-10456(1997).
RN [4]
RP FUNCTION.
RX PubMed=10698948; DOI=10.1093/emboj/19.5.1079;
RA Dehlin E., Wormington M., Koerner C.G., Wahle E.;
RT "Cap-dependent deadenylation of mRNA.";
RL EMBO J. 19:1079-1086(2000).
CC -!- FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of
CC mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic
CC degradation of the poly(A) tail is often the first step in the decay of
CC eukaryotic mRNAs and is also used to silence certain maternal mRNAs
CC translationally during oocyte maturation and early embryonic
CC development. Involved in nonsense-mediated mRNA decay, a critical
CC process of selective degradation of mRNAs that contain premature stop
CC codons. Also involved in degradation of inherently unstable mRNAs that
CC contain AU-rich elements (AREs) in their 3'-UTR, possibly via its
CC interaction with KHSRP. Probably mediates the removal of poly(A) tails
CC of AREs mRNAs, which constitutes the first step of destabilization (By
CC similarity). Interacts with both the 3'-end poly(A) tail and the 5'-end
CC cap structure during degradation, the interaction with the cap
CC structure being required for an efficient degradation of poly(A) tails
CC (By similarity) (PubMed:10698948, PubMed:9736620). Also able to
CC recognize poly(A) tails of microRNAs such as MIR21 and H/ACA box
CC snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or
CC snoRNA increased stability (By similarity).
CC {ECO:0000250|UniProtKB:O95453, ECO:0000269|PubMed:10698948,
CC ECO:0000269|PubMed:9736620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000269|PubMed:9099687};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O95453};
CC Note=Divalent metal cations. Mg(2+) is the most probable.
CC {ECO:0000250|UniProtKB:O95453};
CC -!- SUBUNIT: Homodimer. Found in a mRNA decay complex with RENT1, RENT2 and
CC RENT3B. Interacts with KHSRP. Interacts with CELF1/CUGBP1. Interacts
CC with ZC3HAV1 in an RNA-independent manner. Interacts with DHX36.
CC {ECO:0000250|UniProtKB:O95453}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95453}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95453}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O95453}. Note=Some nuclear fraction is
CC nucleolar. {ECO:0000250|UniProtKB:O95453}.
CC -!- PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation
CC after genotoxic stress. {ECO:0000250|UniProtKB:O95453}.
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC150015; AAI50016.1; -; mRNA.
DR RefSeq; NP_001094588.1; NM_001101118.2.
DR AlphaFoldDB; P69341; -.
DR SMR; P69341; -.
DR STRING; 9913.ENSBTAP00000024087; -.
DR PaxDb; P69341; -.
DR PRIDE; P69341; -.
DR GeneID; 524155; -.
DR KEGG; bta:524155; -.
DR CTD; 5073; -.
DR eggNOG; KOG1990; Eukaryota.
DR HOGENOM; CLU_018030_1_1_1; -.
DR InParanoid; P69341; -.
DR OrthoDB; 1402758at2759; -.
DR TreeFam; TF314502; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0043169; F:cation binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000495; P:box H/ACA RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0010587; P:miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; ISS:UniProtKB.
DR CDD; cd02637; R3H_PARN; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034042; PARN_R3H.
DR InterPro; IPR014789; PolyA-riboNase_RNA-binding.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF04857; CAF1; 1.
DR Pfam; PF08675; RNA_bind; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Exonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nonsense-mediated mRNA decay; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..638
FT /note="Poly(A)-specific ribonuclease PARN"
FT /id="PRO_0000212850"
FT DOMAIN 178..245
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT REGION 143..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 382
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT SITE 326
FT /note="Interaction with poly(A)"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 557
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDG3"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDG3"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT CONFLICT 505
FT /note="R -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 73182 MW; D183F2632C55BFEE CRC64;
MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV TALTNGFDTP EERYQKLKKH
SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS SPDVKFVCQS SSIDFLASQG
FDFNKVFRNG IPYLNQEEER QLREQYDEKR SQSNGAGALS YTSPNTSKCP VTIPDDQKKF
IDQVVEKIED LLQSEENKNL DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV
ISKVDEEERK RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF
YCPLPADLNE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL KETPFNPPKV
ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF LSPPKSHVSA RSKLIEPFFN
KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV TFPKEWKTSD LYQLFSAFGN IQISWIDDTS
AFVSLSQPEQ VPIAVNTSKY AESYRIQTYA DYVGKKREEK QMKRKWTEDS WKEVEPKRLN
TQCGSYSLQN HHYHANSLTA TSTVGKRNLS PSRAEAGLEA RASGEISDTE LEQTDPCAEP
LSEGRKKAKK LKRMKKDLSP TGSISDSSAK LFEVPDTW
