PELO_BOVIN
ID PELO_BOVIN Reviewed; 385 AA.
AC Q58DV0; Q1JPI6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN Name=PELO;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BT021497; AAX46344.1; -; mRNA.
DR EMBL; BT025367; ABF57323.1; -; mRNA.
DR RefSeq; NP_001029738.1; NM_001034566.1.
DR AlphaFoldDB; Q58DV0; -.
DR SMR; Q58DV0; -.
DR STRING; 9913.ENSBTAP00000004233; -.
DR PaxDb; Q58DV0; -.
DR PRIDE; Q58DV0; -.
DR GeneID; 528728; -.
DR KEGG; bta:528728; -.
DR CTD; 53918; -.
DR eggNOG; KOG2869; Eukaryota.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; Q58DV0; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 953123at2759; -.
DR TreeFam; TF105733; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IBA:GO_Central.
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:0032790; P:ribosome disassembly; IBA:GO_Central.
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 Cytoplasm; Endonuclease; Hydrolase; Isopeptide bond; Metal-binding;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..385
FT /note="Protein pelota homolog"
FT /id="PRO_0000232834"
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"
FT CONFLICT 192
FT /note="A -> G (in Ref. 1; ABF57323)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="N -> D (in Ref. 1; ABF57323)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="D -> DE (in Ref. 1; AAX46344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43421 MW; E4F3B8C96A27626E CRC64;
MKLVRKDIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
VLERIEQACD PAWSADVAAV VMQEGLAHIC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
ALERFYEQVV QAIQRHIHFD VVKCVLVASP GFVREQFCDY MFQQAVKTDN KVLLENRSKF
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
KANEAMAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLSQLT
GIAAILRFPV PELSDQENDS SSEED
