PELO_MOUSE
ID PELO_MOUSE Reviewed; 385 AA.
AC Q80X73; Q3TCN0; Q6PG91; Q91UZ2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN Name=Pelo;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Testis;
RX PubMed=12438745; DOI=10.1159/000064059;
RA Shamsadin R., Adham I.M., Engel W.;
RT "Mouse pelota gene (Pelo): cDNA cloning, genomic structure, and chromosomal
RT localization.";
RL Cytogenet. Genome Res. 97:95-99(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, and Pancreas;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12556505; DOI=10.1128/mcb.23.4.1470-1476.2003;
RA Adham I.M., Sallam M.A., Steding G., Korabiowska M., Brinck U.,
RA Hoyer-Fender S., Oh C., Engel W.;
RT "Disruption of the pelota gene causes early embryonic lethality and defects
RT in cell cycle progression.";
RL Mol. Cell. Biol. 23:1470-1476(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- INTERACTION:
CC Q80X73; Q3UJK4: Gtpbp2; NbExp=3; IntAct=EBI-16114899, EBI-16114877;
CC Q80X73; Q69ZS7: Hbs1l; NbExp=2; IntAct=EBI-16114899, EBI-16114976;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12438745}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to defects in chromosome
CC segregation during cell division, resulting in aneuploidy and loss of
CC genomic stability. {ECO:0000269|PubMed:12556505}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF148638; AAK58116.1; -; mRNA.
DR EMBL; AF148639; AAK58117.1; -; Genomic_DNA.
DR EMBL; AK170635; BAE41926.1; -; mRNA.
DR EMBL; BC050209; AAH50209.1; -; mRNA.
DR EMBL; BC057160; AAH57160.1; -; mRNA.
DR CCDS; CCDS26788.1; -.
DR RefSeq; NP_598819.2; NM_134058.3.
DR AlphaFoldDB; Q80X73; -.
DR SMR; Q80X73; -.
DR BioGRID; 222760; 4.
DR DIP; DIP-61683N; -.
DR IntAct; Q80X73; 2.
DR STRING; 10090.ENSMUSP00000104849; -.
DR iPTMnet; Q80X73; -.
DR PhosphoSitePlus; Q80X73; -.
DR EPD; Q80X73; -.
DR MaxQB; Q80X73; -.
DR PaxDb; Q80X73; -.
DR PRIDE; Q80X73; -.
DR ProteomicsDB; 289346; -.
DR Antibodypedia; 23309; 151 antibodies from 25 providers.
DR DNASU; 105083; -.
DR Ensembl; ENSMUST00000109226; ENSMUSP00000104849; ENSMUSG00000042275.
DR GeneID; 105083; -.
DR KEGG; mmu:105083; -.
DR UCSC; uc007ryb.2; mouse.
DR CTD; 53918; -.
DR MGI; MGI:2145154; Pelo.
DR VEuPathDB; HostDB:ENSMUSG00000042275; -.
DR eggNOG; KOG2869; Eukaryota.
DR GeneTree; ENSGT00390000016326; -.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; Q80X73; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 953123at2759; -.
DR PhylomeDB; Q80X73; -.
DR TreeFam; TF105733; -.
DR BioGRID-ORCS; 105083; 31 hits in 73 CRISPR screens.
DR PRO; PR:Q80X73; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q80X73; protein.
DR Bgee; ENSMUSG00000042275; Expressed in urethra and 83 other tissues.
DR Genevisible; Q80X73; MM.
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; IMP:MGI.
DR GO; GO:0007492; P:endoderm development; IDA:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IMP:MGI.
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; IMP:MGI.
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; IMP:MGI.
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_0000143189"
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 30
FT /note="F -> Y (in Ref. 1; AAK58116/AAK58117 and 3;
FT AAH57160)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="I -> F (in Ref. 1; AAK58116/AAK58117)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="R -> P (in Ref. 1; AAK58116/AAK58117)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="D -> H (in Ref. 1; AAK58116/AAK58117)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="G -> V (in Ref. 3; AAH50209)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="L -> F (in Ref. 3; AAH50209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43349 MW; 6D1022BF319FACCE CRC64;
MKLVRKDIEK DNAGQVTLVP EEPEDMWHTF NLVQVGDSLR ASTIRKVQTE SSTGSVGSNR
VRTTLTLCVE AIDFDSQACQ LRVKGTNIQE NEYVKMGAYH TIELEPNRQF TLAKKQWDSV
VLERIEQACD PAWSADVAAV VMQEGLAHVC LVTPSMTLTR AKVEVNIPRK RKGNCSQHDR
ALERFYEQVV QAIQRHINFE VVKCVLVASP GFVREQFCDY MFQQAVKTDN KVLLENRSKF
LQVHASSGHK YSLKEALCDP TVASRLSDTK AAGEVKALDD FYKMLQHEPD RAFYGLKQVE
RANEALAIDT LLISDELFRH QDVATRSRYV RLVDSVKENA GTVRIFSSLH VSGEQLGQLT
GVAAILRFPV PELSDQEDDS SSEED
