PELO_RAT
ID PELO_RAT Reviewed; 385 AA.
AC Q5XIP1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN Name=Pelo;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-380; SER-381 AND
RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC083637; AAH83637.1; -; mRNA.
DR RefSeq; NP_001007635.1; NM_001007634.1.
DR AlphaFoldDB; Q5XIP1; -.
DR SMR; Q5XIP1; -.
DR IntAct; Q5XIP1; 6.
DR STRING; 10116.ENSRNOP00000038406; -.
DR iPTMnet; Q5XIP1; -.
DR PhosphoSitePlus; Q5XIP1; -.
DR jPOST; Q5XIP1; -.
DR PaxDb; Q5XIP1; -.
DR PRIDE; Q5XIP1; -.
DR Ensembl; ENSRNOT00000091499; ENSRNOP00000075562; ENSRNOG00000061128.
DR GeneID; 294754; -.
DR KEGG; rno:294754; -.
DR CTD; 53918; -.
DR RGD; 1359591; Pelo.
DR eggNOG; KOG2869; Eukaryota.
DR GeneTree; ENSGT00390000016326; -.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; Q5XIP1; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 953123at2759; -.
DR PhylomeDB; Q5XIP1; -.
DR TreeFam; TF105733; -.
DR PRO; PR:Q5XIP1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000061128; Expressed in testis and 20 other tissues.
DR Genevisible; Q5XIP1; RN.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; ISO:RGD.
DR GO; GO:0007492; P:endoderm development; ISO:RGD.
DR GO; GO:0001833; P:inner cell mass cell proliferation; ISO:RGD.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISO:RGD.
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:0030513; P:positive regulation of BMP signaling pathway; ISO:RGD.
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 GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
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 1: Evidence at protein 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_0000232836"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 43407 MW; 7C50D96BA28C48E8 CRC64;
MKLVRKDIEK DNAGQVTLVP EEPEDMWHTY NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
VLERIEQACD PAWSADVAAV VMQEGLAHVC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
ALERFYEQVV QAIQRHINFE VVKCILVASP GFVREQFCDY MFQQAVKTDN KVLLENRSKF
LQVHASSGHK YSLKEVLCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
RANEALAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLGQLT
GVAAILRFPV PELSDQEDDS SSEED
