CUFF_DROME
ID CUFF_DROME Reviewed; 384 AA.
AC Q9V629; Q29QR5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein cutoff;
GN Name=cuff; ORFNames=CG13190;
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;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17363252; DOI=10.1016/j.cub.2007.02.027;
RA Chen Y., Pane A., Schuepbach T.;
RT "Cutoff and aubergine mutations result in retrotransposon upregulation and
RT checkpoint activation in Drosophila.";
RL Curr. Biol. 17:637-642(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RHI.
RX PubMed=21952049; DOI=10.1038/emboj.2011.334;
RA Pane A., Jiang P., Zhao D.Y., Singh M., Schuepbach T.;
RT "The Cutoff protein regulates piRNA cluster expression and piRNA production
RT in the Drosophila germline.";
RL EMBO J. 30:4601-4615(2011).
CC -!- FUNCTION: Involved in the piRNA pathway in germline. tissues.
CC {ECO:0000269|PubMed:17363252, ECO:0000269|PubMed:21952049}.
CC -!- SUBUNIT: Interacts with rhi. {ECO:0000269|PubMed:21952049}.
CC -!- INTERACTION:
CC Q9V629; Q9VIF5: del; NbExp=4; IntAct=EBI-185996, EBI-151790;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Chromosome. Note=Localized to
CC perinuclear puncta in the nurse cells of younger egg chambers.
CC Accumulates at centromeric/pericentromeric positions in germ-cell
CC nuclei and strongly colocalizes with the major heterochromatic domains.
CC -!- DISRUPTION PHENOTYPE: Females exhibit severely reduced fecundity.
CC Defects in germline cyst development and result in ventralized eggs as
CC a result of reduced Grk expression. Increase in the transcript levels
CC of two retrotransposable elements, Het-A and Tart.
CC {ECO:0000269|PubMed:17363252}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family that display
CC ribonuclease activity, lacks the conserved catalytic sites that bind
CC the divalent metal cations. Ribonuclease activity is therefore unsure.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC86387.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF58610.1; -; Genomic_DNA.
DR EMBL; BT024325; ABC86387.1; ALT_INIT; mRNA.
DR RefSeq; NP_610709.1; NM_136865.3.
DR AlphaFoldDB; Q9V629; -.
DR SMR; Q9V629; -.
DR BioGRID; 62054; 7.
DR ComplexPortal; CPX-3213; Rhino-Deadlock-Cutoff Complex.
DR IntAct; Q9V629; 4.
DR MINT; Q9V629; -.
DR STRING; 7227.FBpp0087141; -.
DR PaxDb; Q9V629; -.
DR PRIDE; Q9V629; -.
DR DNASU; 36269; -.
DR EnsemblMetazoa; FBtr0088034; FBpp0087141; FBgn0260932.
DR GeneID; 36269; -.
DR KEGG; dme:Dmel_CG13190; -.
DR UCSC; CG13190-RA; d. melanogaster.
DR CTD; 36269; -.
DR FlyBase; FBgn0260932; cuff.
DR VEuPathDB; VectorBase:FBgn0260932; -.
DR eggNOG; KOG1982; Eukaryota.
DR GeneTree; ENSGT00390000006425; -.
DR HOGENOM; CLU_024877_1_1_1; -.
DR InParanoid; Q9V629; -.
DR OMA; RNTMYIC; -.
DR OrthoDB; 1034620at2759; -.
DR PhylomeDB; Q9V629; -.
DR SignaLink; Q9V629; -.
DR BioGRID-ORCS; 36269; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36269; -.
DR PRO; PR:Q9V629; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0260932; Expressed in secondary oocyte and 9 other tissues.
DR Genevisible; Q9V629; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:1990470; F:piRNA cluster binding; IDA:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0030727; P:germarium-derived female germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0110155; P:NAD-cap decapping; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0030719; P:P granule organization; IMP:FlyBase.
DR GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR GO; GO:0140543; P:positive regulation of piRNA transcription; IMP:FlyBase.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0030422; P:siRNA processing; IMP:UniProtKB.
DR GO; GO:0001015; P:snoRNA transcription by RNA polymerase II; IMP:FlyBase.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395; PTHR12395; 1.
DR Pfam; PF08652; RAI1; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; Reference proteome.
FT CHAIN 1..384
FT /note="Protein cutoff"
FT /id="PRO_0000249826"
SQ SEQUENCE 384 AA; 44833 MW; 0FF9AC48BCCB1AEC CRC64;
MNSNYTILNI RAHSWAEKDN LVFPTITKPV SNGWFAWSPI GQFEPNSQKV PYVVVPPSIK
FPISLRYKDS PPKLEKKPNI FLDNMLQYIE SSSYMYVMVR NNQQAQLNAN IVCTSEVLEL
MMCAPYEKKT GWSLGVTRYR NTMYICRIDV EQPDPIDQDN LKRAMQEFWL RNLRTHCVFE
NGIKMHQHNQ SSEEHLRFHG VFSFDLNGNR VLFDSPVLAE MPSTTLNGSA LSWVDLQIRP
MFMSRLDWPE HNRTEALKWW VKCFLLGIES LYIARRDENA HVHNIEKTLV RDLWKSCEKD
WSPTVCANFM IYLLNCISQV MAPIDCPSTV YLFQFDASQG TVSYKGLRGR NQYTFVSDWF
RMMLDDHTND MCKTPNLQTM SSIV
