ID   PELO_PONAB              Reviewed;         385 AA.
AC   Q5RCE3;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Protein pelota homolog;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=PELO;
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: Cotranslational quality control factor involved in the No-Go
CC       Decay (NGD) pathway. In the presence of ABCE1 and HBS1L, is required
CC       for 48S complex formation from 80S ribosomes and dissociation of vacant
CC       80S ribosomes. Together with HBS1L and in presence of ABCE1, recognizes
CC       stalled ribosomes and promotes dissociation of elongation complexes
CC       assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of
CC       the mRNA, a mechanism to release non-functional ribosomes and to
CC       degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway. As part
CC       of the PINK1-regulated signaling, upon mitochondrial damage is
CC       recruited to the ribosome/mRNA-ribonucleoprotein complex associated to
CC       mitochondrial outer membrane thereby enabling the recruitment of
CC       autophagy receptors and induction of mitophagy.
CC       {ECO:0000250|UniProtKB:Q9BRX2}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P33309};
CC   -!- SUBUNIT: Interacts with PINK1, ABCE1 and CNOT4.
CC       {ECO:0000250|UniProtKB:Q9BRX2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC       the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR858328; CAH90564.1; -; mRNA.
DR   RefSeq; NP_001125300.1; NM_001131828.1.
DR   AlphaFoldDB; Q5RCE3; -.
DR   SMR; Q5RCE3; -.
DR   STRING; 9601.ENSPPYP00000017265; -.
DR   GeneID; 100172199; -.
DR   KEGG; pon:100172199; -.
DR   CTD; 53918; -.
DR   eggNOG; KOG2869; Eukaryota.
DR   InParanoid; Q5RCE3; -.
DR   OrthoDB; 953123at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:InterPro.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR   Gene3D; 2.30.30.870; -; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR005141; eRF1_2.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR038069; Pelota/DOM34_N.
DR   InterPro; IPR004405; Transl-rel_pelota.
DR   PANTHER; PTHR10853; PTHR10853; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03464; eRF1_2; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF159065; SSF159065; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   TIGRFAMs; TIGR00111; pelota; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Endonuclease; Hydrolase;
KW   Isopeptide bond; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome; Translation regulation; Ubl conjugation.
FT   CHAIN           1..385
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000232835"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRX2"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRX2"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRX2"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRX2"
FT   CROSSLNK        162
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BRX2"
SQ   SEQUENCE   385 AA;  43391 MW;  7116E96F01436630 CRC64;
     MKLVRKNIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
     VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
     VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
     ALERFYEQVV QAIQRHIHFD VVKCILVASP GFVREQFCDY MFQQAVKTDN KLLLENRSKF
     LQVHASSGHK YSLKEVLCDP TVASRLSDTK AAGEVKALDD FYKMLQHGPD RAFYGLKQVE
     KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT
     GVAAILRFPV PELSDQEDDS SSEED