XRN2_PONAB
ID XRN2_PONAB Reviewed; 950 AA.
AC Q5R4L5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=5'-3' exoribonuclease 2;
DE EC=3.1.13.-;
GN Name=XRN2;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote the
CC termination of transcription by RNA polymerase II. During transcription
CC termination, cleavage at the polyadenylation site liberates a 5'
CC fragment which is subsequently processed to form the mature mRNA and a
CC 3' fragment which remains attached to the elongating polymerase. The
CC processive degradation of this 3' fragment by this protein may promote
CC termination of transcription. Binds to RNA polymerase II (RNAp II)
CC transcription termination R-loops formed by G-rich pause sites (By
CC similarity). {ECO:0000250|UniProtKB:Q9H0D6}.
CC -!- SUBUNIT: Interacts with POLR2A and SMN1/SMN2. Interacts with CDKN2AIP
CC and NKRF. Interacts with CDKN2AIPNL; the interaction is direct.
CC Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By
CC similarity). Interacts with DHX34; the interaction is RNA-independent
CC (By similarity). {ECO:0000250|UniProtKB:Q9H0D6}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H0D6}.
CC -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC subfamily. {ECO:0000305}.
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DR EMBL; CR861231; CAH93301.1; -; mRNA.
DR RefSeq; NP_001126942.1; NM_001133470.1.
DR AlphaFoldDB; Q5R4L5; -.
DR SMR; Q5R4L5; -.
DR STRING; 9601.ENSPPYP00000012020; -.
DR GeneID; 100173960; -.
DR KEGG; pon:100173960; -.
DR CTD; 22803; -.
DR eggNOG; KOG2044; Eukaryota.
DR InParanoid; Q5R4L5; -.
DR OrthoDB; 685597at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR027073; 5_3_exoribonuclease.
DR InterPro; IPR004859; Put_53exo.
DR InterPro; IPR041412; Xrn1_helical.
DR InterPro; IPR017151; Xrn2/3/4.
DR PANTHER; PTHR12341; PTHR12341; 1.
DR Pfam; PF17846; XRN_M; 1.
DR Pfam; PF03159; XRN_N; 1.
DR PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Exonuclease; Hydrolase; Metal-binding;
KW Methylation; mRNA processing; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..950
FT /note="5'-3' exoribonuclease 2"
FT /id="PRO_0000249912"
FT ZN_FING 261..278
FT /note="CCHC-type"
FT REGION 408..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR1"
FT MOD_RES 439
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR1"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 824
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 824
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 847
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 847
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 851
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 851
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 880
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR1"
FT MOD_RES 883
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR1"
FT MOD_RES 883
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 895
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 946
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
FT MOD_RES 946
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H0D6"
SQ SEQUENCE 950 AA; 108560 MW; 82E11A4FFC2ACF1A CRC64;
MGVPAFFRWL SRKYPSIIVN CVEEKPKECN GVKIPVDASK PNPNDVEFDN LYLDMNGIIH
PCTHPEDKPA PKNEDEMMVA IFEYIDRLFS IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
ASKEGMEAAV EKQRVREEIL AKGGFLPPEE IKERFDSNCI TPGTEFMDNL AKCLRYYIAD
RLNNDPGWKN LTVILSDASA PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG
LATHEPNFTI IREEFKPNKP KPCGLCNQFG HEVKDCEGLL REKKVKHDEL ADSLPCAEGE
FIFLRLNVLR EYLERELTMA SLPFTFDVER SIDDWVFMCF FVGNDFLPHL PSLEIRENAI
DRLVNIYKNV VHKTGGYLTE SGYVNLQRVQ MIMLAVGEVE DSIFKKRKDD EDSFRRRQKE
KRKRMKRDQP AFTPSGILTP HALGSRNSPG SQVASNPRQA AYEMRMQNNS SPSISPNTSF
TSDGSPSPIG GIKRKAEDSD SEPEPEDNVR LWEAGWKQRY YKNKFDADAA DEKFRRKVVQ
SYVEGLCWVL RYYYQGCASW KWYYPFHYAP FASDFEGIAD MPSDFEKGTK PFKPLEQLMG
VFPAASGNFL PPSWRKLMSD PDSSIIDFYP EDFAIDLNGK KYAWQGVALL PFVDERRLRA
ALEEVYPDLT PEETRRNSLG GDVLFVGKHH PLHDFILELY QTGSTEPVDV PPELCHGIQG
KFSLDEEAIL PDQIVCSPVP MLRDLTQNTV VSINFKDPQF AEDYIFKAVM LPGARKPAAV
LKPSDWEKSS NGRQWKPQLG FNRDRRPVHL DQAAFRTLGH VMPRGSGTGI YSNAAPPPAT
YQGNLYRPLL RGQAQIPKLM SNMRPQDSWR GPPPLFQQQR FDRGVGAEPL LPWNRMLQTQ
NAAFQPNQYQ MLAGPGGYPP RRDDRGGRQG YPREGRKYPL SPPSGRYNWN
