PARN_PONAB
ID PARN_PONAB Reviewed; 639 AA.
AC Q5RC51;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Poly(A)-specific ribonuclease PARN;
DE EC=3.1.13.4;
DE AltName: Full=Polyadenylate-specific ribonuclease;
GN Name=PARN;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. 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 Involved in nonsense-mediated mRNA decay, a critical process of
CC selective degradation of mRNAs that contain premature stop codons. Also
CC involved in degradation of inherently unstable mRNAs that contain AU-
CC rich elements (AREs) in their 3'-UTR, possibly via its interaction with
CC KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs,
CC which constitutes the first step of destabilization (By similarity).
CC Also able to recognize poly(A) tails of microRNAs such as MIR21 and
CC H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs
CC degradation or snoRNA increased stability (By similarity).
CC {ECO:0000250|UniProtKB:O95453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
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}.
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DR EMBL; CR858430; CAH90659.1; -; mRNA.
DR RefSeq; NP_001125357.1; NM_001131885.1.
DR AlphaFoldDB; Q5RC51; -.
DR SMR; Q5RC51; -.
DR STRING; 9601.ENSPPYP00000008052; -.
DR GeneID; 100172259; -.
DR KEGG; pon:100172259; -.
DR CTD; 5073; -.
DR eggNOG; KOG1990; Eukaryota.
DR InParanoid; Q5RC51; -.
DR OrthoDB; 1402758at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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: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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..639
FT /note="Poly(A)-specific ribonuclease PARN"
FT /id="PRO_0000212853"
FT DOMAIN 178..245
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT REGION 563..611
FT /note="Disordered"
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:0000250|UniProtKB:O95453"
FT BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT BINDING 382
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O95453"
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 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
FT MOD_RES 631
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95453"
SQ SEQUENCE 639 AA; 73430 MW; E48330BCA4C8E673 CRC64;
MEIIRSNFKC NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP EERYQKLKKH
SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS PPDVKFVCQS SSIDFLASQG
FDFNKVFRNG IPYLNQEEER QLREQYDEKR SQANGAGALS YVSPNTSKCP VTIPEDQKKF
IDQVVEKIED LLQSEENKNL DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV
ISKVDEEERK RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF
YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL KETPFSPPKV
ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF LSPPKIHVSA RSKLIEPFFN
KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV TFPKEWKTSD LYQLFSAFGN IQISWIDDTS
AFVSLSQPEQ VKIAVNTSKY AESYRIQTYA EYVGRKQEEK QIKRKWTEDS WKEADSKRLN
PQCIPYALQN HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP
LSEGRKKAKK LKRMKKELSP AVSISKNSPA TLFEVPDTW
