PELO_DROME
ID PELO_DROME Reviewed; 395 AA.
AC P48612; Q9VL97;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein pelota;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN Name=pelo; ORFNames=CG3959;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Testis;
RX PubMed=7588080; DOI=10.1242/dev.121.10.3477;
RA Eberhart C.G., Wasserman S.W.;
RT "The pelota locus encodes a protein required for meiotic cell division: an
RT analysis of G2/M arrest in Drosophila spermatogenesis.";
RL Development 121:3477-3486(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16280348; DOI=10.1242/dev.02151;
RA Xi R., Doan C., Liu D., Xie T.;
RT "Pelota controls self-renewal of germline stem cells by repressing a Bam-
RT independent differentiation pathway.";
RL Development 132:5365-5374(2005).
RN [6]
RP FUNCTION, INTERACTION WITH HBS1, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF PRO-210.
RX PubMed=26124316; DOI=10.15252/embr.201540084;
RA Yang F., Zhao R., Fang X., Huang H., Xuan Y., Ma Y., Chen H., Cai T.,
RA Qi Y., Xi R.;
RT "The RNA surveillance complex Pelo-Hbs1 is required for transposon
RT silencing in the Drosophila germline.";
RL EMBO Rep. 16:965-974(2015).
RN [7]
RP FUNCTION, INTERACTION WITH PINK1 AND CNOT4, AND TISSUE SPECIFICITY.
RX PubMed=29861391; DOI=10.1016/j.cmet.2018.05.007;
RA Wu Z., Wang Y., Lim J., Liu B., Li Y., Vartak R., Stankiewicz T.,
RA Montgomery S., Lu B.;
RT "Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links
RT Co-translational Quality Control to PINK1-Directed Mitophagy.";
RL Cell Metab. 28:130-144.e7(2018).
RN [8]
RP FUNCTION, INTERACTION WITH HSB1, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF PRO-210.
RX PubMed=30824860; DOI=10.1038/s41598-019-39530-6;
RA Li Z., Yang F., Xuan Y., Xi R., Zhao R.;
RT "Pelota-interacting G protein Hbs1 is required for spermatogenesis in
RT Drosophila.";
RL Sci. Rep. 9:3226-3226(2019).
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway (PubMed:29861391). In the presence of pix and HSB1,
CC is required for 48S complex formation from 80S ribosomes and
CC dissociation of vacant 80S ribosomes (By similarity). Together with
CC HBS1 and in presence of pix, recognizes stalled ribosomes and promotes
CC dissociation of elongation complexes assembled on non-stop mRNAs; this
CC triggers endonucleolytic cleavage of the mRNA, a mechanism to release
CC non-functional ribosomes and to degrade damaged mRNAs as part of the
CC No-Go Decay (NGD) pathway (By similarity). Required prior to the first
CC meiotic division for spindle formation and nuclear envelope breakdown
CC during spermatogenesis (PubMed:7588080). Together with HBS1, promotes
CC spermatid individualization during spermatogenesis (PubMed:30824860).
CC Required for ovarian germ line stem cell self-renewal and oocyte
CC development during oogenesis (PubMed:16280348). Together with HSB1,
CC required for transposon silencing in the ovary and testis
CC (PubMed:26124316). As part of the Pink1-regulated signaling, is
CC recruited to damaged mitochondrial and is required for recruitment of
CC autophagy receptors and induction of mitophagy (PubMed:29861391).
CC Required for normal eye patterning and for mitotic divisions in the
CC ovary (PubMed:7588080). {ECO:0000250|UniProtKB:Q9BRX2,
CC ECO:0000269|PubMed:16280348, ECO:0000269|PubMed:26124316,
CC ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:30824860,
CC ECO:0000269|PubMed:7588080}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P33309};
CC -!- SUBUNIT: Interacts with HBS1 (PubMed:26124316, PubMed:30824860).
CC Interacts with Pink1 and Cnot4; the interaction with Cnot4 appears to
CC be Pink1-dependent (PubMed:29861391). {ECO:0000269|PubMed:26124316,
CC ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:30824860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30824860}. Cytoplasm
CC {ECO:0000269|PubMed:16280348, ECO:0000269|PubMed:30824860}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries and muscles (at protein level)
CC (PubMed:26124316, PubMed:29861391). Expressed throughout all
CC development stages (PubMed:7588080). {ECO:0000269|PubMed:26124316,
CC ECO:0000269|PubMed:29861391, ECO:0000269|PubMed:7588080}.
CC -!- DEVELOPMENTAL STAGE: Highest levels in early embryo (0-2h) and adult
CC stages. {ECO:0000269|PubMed:7588080}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC -!- DOMAIN: The PGF motif may be involved in the interaction with HBS1 and
CC is required for silencing of germline transposons.
CC {ECO:0000269|PubMed:26124316}.
CC -!- DISRUPTION PHENOTYPE: During spermatogenesis results in blockage of
CC cell division preventing spermatocytes to enter meiosis and lack of
CC spermatic individualization resulting in sterility (PubMed:30824860).
CC In germlines, increases transposable elements transcription at both
CC mRNA and protein levels (PubMed:26124316).
CC {ECO:0000269|PubMed:26124316, ECO:0000269|PubMed:30824860}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000305}.
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DR EMBL; U27197; AAC46879.1; -; mRNA.
DR EMBL; AY058644; AAL13873.1; -; mRNA.
DR EMBL; AE014134; AAF52799.1; -; Genomic_DNA.
DR PIR; T47122; T47122.
DR RefSeq; NP_476982.1; NM_057634.5.
DR AlphaFoldDB; P48612; -.
DR SMR; P48612; -.
DR BioGRID; 60384; 12.
DR IntAct; P48612; 3.
DR STRING; 7227.FBpp0079444; -.
DR PaxDb; P48612; -.
DR PRIDE; P48612; -.
DR DNASU; 34286; -.
DR EnsemblMetazoa; FBtr0079847; FBpp0079444; FBgn0011207.
DR GeneID; 34286; -.
DR KEGG; dme:Dmel_CG3959; -.
DR UCSC; CG3959-RA; d. melanogaster.
DR CTD; 53918; -.
DR FlyBase; FBgn0011207; pelo.
DR VEuPathDB; VectorBase:FBgn0011207; -.
DR eggNOG; KOG2869; Eukaryota.
DR GeneTree; ENSGT00390000016326; -.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; P48612; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 953123at2759; -.
DR PhylomeDB; P48612; -.
DR SignaLink; P48612; -.
DR BioGRID-ORCS; 34286; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34286; -.
DR PRO; PR:P48612; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011207; Expressed in cleaving embryo and 25 other tissues.
DR Genevisible; P48612; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:1990533; C:Dom34-Hbs1 complex; IPI:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0008315; P:G2/MI transition of meiotic cell cycle; TAS:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007141; P:male meiosis I; TAS:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:FlyBase.
DR GO; GO:0051078; P:meiotic nuclear membrane disassembly; IMP:FlyBase.
DR GO; GO:0000212; P:meiotic spindle organization; IMP:FlyBase.
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:0016441; P:post-transcriptional gene silencing; IMP:FlyBase.
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:0007291; P:sperm individualization; IGI:UniProtKB.
DR GO; GO:0048137; P:spermatocyte division; IMP:FlyBase.
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; Meiosis;
KW Metal-binding; Mitosis; Nuclease; Nucleus; Reference proteome;
KW Translation regulation.
FT CHAIN 1..395
FT /note="Protein pelota"
FT /id="PRO_0000143190"
FT REGION 371..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 210..212
FT /note="PGF motif"
FT /evidence="ECO:0000269|PubMed:26124316"
FT COMPBIAS 373..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 210
FT /note="P->A: Reduces ability to repress transposon levels.
FT Unable to rescue spermatogenesis defects in null mutants.
FT Rescues germ stem cells defects in null mutants."
FT /evidence="ECO:0000269|PubMed:26124316,
FT ECO:0000269|PubMed:30824860"
FT CONFLICT 81
FT /note="L -> V (in Ref. 1; AAC46879)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="N -> D (in Ref. 1; AAC46879)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="V -> A (in Ref. 1; AAC46879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44212 MW; 66B41D62BEEB43D3 CRC64;
MKLLGKYVDK GMQGNVTLVP EESEDMWHAY NLIAKGDSVR STTIRKVQNE TATGSSTSSR
VRTTLTIAVE SIDFDTQACV LRLKGRNIEE NQYVKMGAYH TLDLELNRKF ELRKPEWDTI
ALERIEMACD PTQSADVAAV VMQEGLAHVC LITASMTLVR SKIEVSIPRK RKGSVQQHEK
GLAKFYEQVM QSILRHVNFD VVKCVLIASP GFVRDQFYDY MFQQAVKMDY KLLLDNKSKF
MLVHASSGFK HSLREILQDP AVLAKMSDTK AAGEVKALEQ FYMMLQCEPA KAFYGKKHVL
QAAESQAIET LLISDNLFRC QDVSLRKEYV NLVESIRDAG GEVKIFSSMH ISGEQLAQLT
GIAALLRFPM PELEDSDDDD DEDGAAGGVA DSDSD
