ENDOU_DROME
ID ENDOU_DROME Reviewed; 592 AA.
AC Q9VZ49; A9UNF0; Q8SY54;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Endoribonuclease CG2145 {ECO:0000305};
DE EC=4.6.1.- {ECO:0000250|UniProtKB:P21128};
DE AltName: Full=Poly(U)-specific endoribonuclease homolog;
DE AltName: Full=Uridylate-specific endoribonuclease homolog;
DE Flags: Precursor;
GN ORFNames=CG2145;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-592.
RC STRAIN=Berkeley; TISSUE=Head;
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).
CC -!- FUNCTION: Catalyzes RNA cleavage releasing a product with a 2',3'-
CC cyclic phosphate at the 3'-end. {ECO:0000250|UniProtKB:P21128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67796, Rhea:RHEA-COMP:10464, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:83064,
CC ChEBI:CHEBI:138284, ChEBI:CHEBI:173118; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67797;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ENDOU family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL68194.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABY21727.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AE014298; AAF47979.1; -; Genomic_DNA.
DR EMBL; BT031314; ABY21727.1; ALT_INIT; mRNA.
DR EMBL; AY075327; AAL68194.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285102.1; NM_001298173.1.
DR RefSeq; NP_572668.1; NM_132440.2.
DR AlphaFoldDB; Q9VZ49; -.
DR SMR; Q9VZ49; -.
DR BioGRID; 58443; 2.
DR IntAct; Q9VZ49; 1.
DR STRING; 7227.FBpp0073243; -.
DR PaxDb; Q9VZ49; -.
DR DNASU; 32027; -.
DR EnsemblMetazoa; FBtr0073387; FBpp0073243; FBgn0030251.
DR EnsemblMetazoa; FBtr0343591; FBpp0310188; FBgn0030251.
DR GeneID; 32027; -.
DR KEGG; dme:Dmel_CG2145; -.
DR UCSC; CG2145-RA; d. melanogaster.
DR FlyBase; FBgn0030251; CG2145.
DR VEuPathDB; VectorBase:FBgn0030251; -.
DR eggNOG; KOG2849; Eukaryota.
DR HOGENOM; CLU_036748_0_0_1; -.
DR InParanoid; Q9VZ49; -.
DR OMA; AWQSPLP; -.
DR OrthoDB; 823332at2759; -.
DR PhylomeDB; Q9VZ49; -.
DR BioGRID-ORCS; 32027; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32027; -.
DR PRO; PR:Q9VZ49; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030251; Expressed in head capsule and 26 other tissues.
DR ExpressionAtlas; Q9VZ49; baseline and differential.
DR Genevisible; Q9VZ49; DM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:FlyBase.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISS:FlyBase.
DR CDD; cd21159; XendoU; 1.
DR InterPro; IPR039787; ENDOU.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR018998; EndoU_C.
DR PANTHER; PTHR12439; PTHR12439; 1.
DR Pfam; PF09412; XendoU; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR PROSITE; PS51959; ENDOU; 1.
PE 2: Evidence at transcript level;
KW Endonuclease; Hydrolase; Lyase; Manganese; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..592
FT /note="Endoribonuclease CG2145"
FT /id="PRO_0000394229"
FT DOMAIN 329..592
FT /note="EndoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT REGION 83..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..266
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
FT ACT_SITE 531
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01304"
SQ SEQUENCE 592 AA; 63596 MW; 1B26858312A45E6A CRC64;
MRCLALSAVF LCLTLAGHFH LSDAYKNEVQ ITPDPLDAVE TTTKKSSWFG GFKKFFGSDG
TTTTTSTIAP PVVTSPKSVV VTPTAANKPP PLVISHAPLM PLGPRPDTPG SSPFGASQNP
QTPPQWPSST RATPSHPSQP SQPSQQPPLP GFASYRPQKP QPNSYDLSYG GGPQPAPAGT
GRPGFGLGIS STTSTTTTAK PITSTTGKTP QQKEDFPALP GPRRPSQKED FPALPAPKTP
PGSPTPTPGS PSAWQSPLPT PQHPVHPPTK ATSAATPTPT PTPSFSSSVT PTPAHGSSVG
PHKDGGGGGG GGTTTVRPGF QSSGNSVATD DEIRQLTELL YTKESNSQIG NIQVNLQGRT
RSIDSADEAP NPLLTVDSKA LESPTIVKMR LLFNNYEHDT HVNEHVTPNE RKEENDFLDA
VMATPVMRQA MLFLQQKGVV SPDPKTHRDL VKELWFTQYS RGQGKIGSSG FEHVFVYEVK
DGTIIGFHNW VYIGDEEKDG RFDYKGYMKE QDIGTKGKIV KIRFSHQGLN KPVNTVFVGT
SPELELALYT VCFQLRPDRT CPVSLGNSKF GIVTYSWRYR GKNLIGSAYP EI
