ID A0A1L8EQ87_XENLA Unreviewed; 632 AA.
AC A0A1L8EQ87;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 40.
DE RecName: Full=Poly(A)-specific ribonuclease PARN {ECO:0000256|ARBA:ARBA00015918};
DE EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
DE AltName: Full=Polyadenylate-specific ribonuclease {ECO:0000256|ARBA:ARBA00031923};
GN Name=parn.S {ECO:0000313|RefSeq:XP_018094580.1,
GN ECO:0000313|Xenbase:XB-GENE-17341054};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018094580.1};
RN [1] {ECO:0000313|RefSeq:XP_018094580.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018094580.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018094580.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001663};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the CAF1 family.
CC {ECO:0000256|ARBA:ARBA00008372}.
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DR RefSeq; XP_018094580.1; XM_018239091.2.
DR AlphaFoldDB; A0A1L8EQ87; -.
DR STRING; 8355.A0A1L8EQ87; -.
DR PaxDb; 8355-A0A1L8EQ87; -.
DR GeneID; 108703108; -.
DR KEGG; xla:108703108; -.
DR AGR; Xenbase:XB-GENE-17341054; -.
DR CTD; 108703108; -.
DR Xenbase; XB-GENE-17341054; parn.S.
DR OMA; LMHTIIG; -.
DR OrthoDB; 1432093at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 108703108; Expressed in blastula and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:1990431; P:priRNA 3'-end processing; IBA:GO_Central.
DR GO; GO:1990432; P:siRNA 3'-end processing; IBA:GO_Central.
DR CDD; cd02637; R3H_PARN; 1.
DR CDD; cd12428; RRM_PARN; 1.
DR FunFam; 3.30.420.10:FF:000035; Poly(A)-specific ribonuclease PARN; 1.
DR FunFam; 3.30.420.10:FF:000120; Poly(A)-specific ribonuclease PARN; 1.
DR FunFam; 3.30.70.330:FF:000196; Poly(A)-specific ribonuclease PARN; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR InterPro; IPR051181; CAF1_poly(A)_ribonucleases.
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 PANTHER; PTHR15092; POLY A -SPECIFIC RIBONUCLEASE/TARGET OF EGR1, MEMBER 1; 1.
DR PANTHER; PTHR15092:SF44; POLY(A)-SPECIFIC RIBONUCLEASE PARN; 1.
DR Pfam; PF04857; CAF1; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF08675; RNA_bind; 1.
DR SUPFAM; SSF82708; R3H domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51061; R3H; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT REGION 148..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 72967 MW; D33DDDC48B187125 CRC64;
MEITRNNFKD NLPKVYKAIE EADFLAIDGE FSGISDGPSV STLTNGFDTP EERYTKLKKH
SMEFLLFQFG LCTFNYDNTE EKYLIKSFNF YIFPKPFNRN SPDKKFVCQS SSIDFLANQG
FDFNKVFRNG VPYLNQEEEK LLRDQYEERR SQSNGASTMS YVSPNASKTP VSIPDEQKGF
IDKVVERVED FLKNDQKSMN VEPCTGYQRK LIYQTLNWKY PRGIHVETVE SEKKERYIVI
SKVDEEERKR MEQQKQAKER EELDDAVGFS RIIQAISSSA KLVVGHNMLL DIMHTIHQFF
CQLPDELNEF KEVTNCVFPR VLDTKLMAST NPFKEIIYNT SLAELEKRLK EAPFKPPKVD
SAEGFPSYNT ASEQLHEAGY DAYITGLCFI SMANYLGSFL SPPKGYVSSQ SKIIRPFFNK
LFLMRIMDIP YLNLEGPDLQ PKRDNVLHVA FPKEWKTSDL YQLFSAFGNI QVSWIDDTSA
FVSLSQPEQV QIAVNTSKYA ESYRIQTYAD YIEKKNEENQ TKRKWAEDGW KDLERKRLKP
QYNSYIPQNQ IFYGNCFVAP SFAVKRSMSP IQEETTASED TEVHTRENDP SNPGATEQGK
KPKNHKRQKI DSTPPETSDS GSSGLFEVPD TW
//
