OTU_DROME
ID OTU_DROME Reviewed; 853 AA.
AC P10383; A4V451; Q8SYF4; Q9GYD8; Q9TWA9; Q9W3E4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Protein ovarian tumor locus;
GN Name=otu; ORFNames=CG12743;
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] (ISOFORM A).
RC STRAIN=Canton-S; TISSUE=Ovary;
RX PubMed=2498839; DOI=10.1093/nar/17.8.3304;
RA Champe M.A., Laird C.D.;
RT "Nucleotide sequence of a cDNA from the putative ovarian tumor locus of
RT Drosophila melanogaster.";
RL Nucleic Acids Res. 17:3304-3304(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=2511440; DOI=10.1128/mcb.9.12.5726-5732.1989;
RA Steinhauer W.R., Walsh R.C., Kalfayan L.J.;
RT "Sequence and structure of the Drosophila melanogaster ovarian tumor gene
RT and generation of an antibody specific for the ovarian tumor protein.";
RL Mol. Cell. Biol. 9:5726-5732(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Canton-S;
RX PubMed=1737618; DOI=10.1101/gad.6.2.233;
RA Steinhauer W.R., Kalfayan L.J.;
RT "A specific ovarian tumor protein isoform is required for efficient
RT differentiation of germ cells in Drosophila oogenesis.";
RL Genes Dev. 6:233-243(1992).
RN [4]
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 [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [7]
RP ACTIVATION BY STIL.
RX PubMed=10101125; DOI=10.1242/dev.126.9.1917;
RA Sahut-Barnola I., Pauli D.;
RT "The Drosophila gene stand still encodes a germline chromatin-associated
RT protein that controls the transcription of the ovarian tumor gene.";
RL Development 126:1917-1926(1999).
CC -!- FUNCTION: Essential for female fertility; germ cell division and
CC differentiation. {ECO:0000269|PubMed:1737618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1737618}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=C;
CC IsoId=P10383-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P10383-2; Sequence=VSP_004354;
CC -!- TISSUE SPECIFICITY: Expressed in both oocyte and nurse cells of the
CC germarium.
CC -!- INDUCTION: Expression is cooperatively activated by Ovo and Stil.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL49210.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X13693; CAA31983.1; -; mRNA.
DR EMBL; M30825; AAA28740.1; -; Genomic_DNA.
DR EMBL; M30825; AAF97987.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46384.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09234.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65286.1; -; Genomic_DNA.
DR EMBL; AY071588; AAL49210.1; ALT_FRAME; mRNA.
DR PIR; B41760; B41760.
DR PIR; S04085; S04085.
DR RefSeq; NP_001259332.1; NM_001272403.1. [P10383-2]
DR RefSeq; NP_001259333.1; NM_001272404.1. [P10383-2]
DR RefSeq; NP_511089.2; NM_078534.4. [P10383-1]
DR RefSeq; NP_727271.1; NM_167158.3. [P10383-2]
DR RefSeq; NP_996379.1; NM_206656.2. [P10383-1]
DR AlphaFoldDB; P10383; -.
DR SMR; P10383; -.
DR BioGRID; 58248; 23.
DR DIP; DIP-19612N; -.
DR IntAct; P10383; 1.
DR STRING; 7227.FBpp0071181; -.
DR PaxDb; P10383; -.
DR PRIDE; P10383; -.
DR EnsemblMetazoa; FBtr0071236; FBpp0071180; FBgn0003023. [P10383-2]
DR EnsemblMetazoa; FBtr0071237; FBpp0071181; FBgn0003023. [P10383-1]
DR EnsemblMetazoa; FBtr0071238; FBpp0089325; FBgn0003023. [P10383-1]
DR EnsemblMetazoa; FBtr0333146; FBpp0305351; FBgn0003023. [P10383-2]
DR EnsemblMetazoa; FBtr0333147; FBpp0305352; FBgn0003023. [P10383-2]
DR GeneID; 31789; -.
DR KEGG; dme:Dmel_CG12743; -.
DR CTD; 31789; -.
DR FlyBase; FBgn0003023; otu.
DR VEuPathDB; VectorBase:FBgn0003023; -.
DR eggNOG; KOG2605; Eukaryota.
DR GeneTree; ENSGT00940000174398; -.
DR InParanoid; P10383; -.
DR OMA; QLYTCHI; -.
DR PhylomeDB; P10383; -.
DR SignaLink; P10383; -.
DR BioGRID-ORCS; 31789; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31789; -.
DR PRO; PR:P10383; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003023; Expressed in cleaving embryo and 9 other tissues.
DR ExpressionAtlas; P10383; baseline and differential.
DR Genevisible; P10383; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0101005; F:deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:FlyBase.
DR GO; GO:0019099; P:female germ-line sex determination; NAS:FlyBase.
DR GO; GO:0007281; P:germ cell development; TAS:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:FlyBase.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IMP:FlyBase.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF02338; OTU; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Reference proteome.
FT CHAIN 1..853
FT /note="Protein ovarian tumor locus"
FT /id="PRO_0000058104"
FT DOMAIN 29..150
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 336..396
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 340..381
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2498839"
FT /id="VSP_004354"
FT CONFLICT 300
FT /note="K -> Q (in Ref. 1; CAA31983)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="T -> P (in Ref. 3; AAA28740/AAF97987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 97452 MW; D7C1F9453377B075 CRC64;
MDMQVQRPIT SGSRQAPDPY DQYLESRGLY RKHTARDASS LFRVIAEQMY DTQMLHYEIR
LECVRFMTLK RRIFEKEIPG DFDSYMQDMS KPKTYGTMTE LRAMSCLYRR NVILYEPYNM
GTSVVFNRRY AENFRVFFNN ENHFDSVYDV EYIERAAICQ SIAFKLLYQK LFKLPDVSFA
VEIMLHPHTF NWDRFNVEFD DKGYMVRIHC TDGRVFKLDL PGDTNCILEN YKLCNFHSTN
GNQSINARKG GRLEIKNQEE RKASGSSGHE PNDLLPMCPN RLESCVRQLL DDGISPFPYK
VAKSMDPYMY RNIEFDCWND MRKEAKLYNV YINDYNFKVG AKCKVELPNE TEMYTCHVQN
ISKDKNYCHV FVERIGKEIV VPYESLHPLP PDEYRPWSLP FRYHRQMPRL PLPKYAGKAN
KSSKWKKNKL FEMDQYFEHS KCDLMPYMPV DNCYQGVHIQ DDEQRDHNDP EQNDQNPTTE
QRDREEPQAQ KQHQRTKASR VQPQNSSSSQ NQEVSGSAAP PPTQYMNYVP MIPSRPGHLP
PPWPASPMAI AEEFPFPISG TPHPPPTEGC VYMPFGGYGP PPPGAVALSG PHPFMPLPSP
PLNVTGIGEP RRSLHPNGED LPVDMVTLRY FYNMGVDLHW RMSHHTPPDE LGMFGYHQQN
NTDQQAGRTV VIGATEDNLT AVESTPPPSP EVANATEQSP LEKSAYAKRN LNSVKVRGKR
PEQLQDIKDS LGPAAFLPTP TPSPSSNGSQ FSFYTTPSPH HHLITPPRLL QPPPPPPIFY
HKAGPPQLGG AAQGQTPYAW GMPAPVVSPY EVINNYNMDP SAQPQQQQPA TLQPAPLSVQ
SQPAAVYAAT RHH
