OSKA_DROME
ID OSKA_DROME Reviewed; 606 AA.
AC P25158; Q59DY0; Q95TT0; Q9V3P1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Maternal effect protein oskar;
GN Name=osk; ORFNames=CG10901;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=2070416; DOI=10.1016/0092-8674(91)90136-m;
RA Kim-Ha J., Smith J.L., Macdonald P.M.;
RT "Oskar mRNA is localized to the posterior pole of the Drosophila oocyte.";
RL Cell 66:23-35(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=2070417; DOI=10.1016/0092-8674(91)90137-n;
RA Ephrussi A., Dickinson L.K., Lehmann R.;
RT "Oskar organizes the germ plasm and directs localization of the posterior
RT determinant nanos.";
RL Cell 66:37-50(1991).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
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 [6]
RP FUNCTION.
RX PubMed=1641021; DOI=10.1038/358387a0;
RA Ephrussi A., Lehmann R.;
RT "Induction of germ cell formation by oskar.";
RL Nature 358:387-392(1992).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11546740; DOI=10.1242/dev.128.17.3233;
RA Nakamura A., Amikura R., Hanyu K., Kobayashi S.;
RT "Me31B silences translation of oocyte-localizing RNAs through the formation
RT of cytoplasmic RNP complex during Drosophila oogenesis.";
RL Development 128:3233-3242(2001).
RN [8]
RP INTERACTION WITH SMG.
RX PubMed=10488336; DOI=10.1016/s1097-2765(00)80368-8;
RA Dahanukar A., Walker J.A., Wharton R.P.;
RT "Smaug, a novel RNA-binding protein that operates a translational switch in
RT Drosophila.";
RL Mol. Cell 4:209-218(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-275, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Organizes the germ plasm and directs localization of the
CC posterior determinant nanos. Oskar protein is required to keep nos RNA
CC and staufen protein at the posterior pole. {ECO:0000269|PubMed:1641021,
CC ECO:0000269|PubMed:2070416, ECO:0000269|PubMed:2070417}.
CC -!- SUBUNIT: Interacts with smaug (smg). {ECO:0000269|PubMed:10488336}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P25158-1; Sequence=Displayed;
CC Name=C;
CC IsoId=P25158-2; Sequence=VSP_016006;
CC -!- TISSUE SPECIFICITY: Begins to accumulate at the posterior pole of the
CC oocyte from stage 8 onwards. {ECO:0000269|PubMed:11546740,
CC ECO:0000269|PubMed:2070416, ECO:0000269|PubMed:2070417}.
CC -!- MISCELLANEOUS: Capu, spir, and stau are required for the initial
CC localization of osk to the posterior pole.
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DR EMBL; M63492; AAA28739.1; -; Genomic_DNA.
DR EMBL; M65178; AAA28738.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54306.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65129.1; -; Genomic_DNA.
DR EMBL; AY058560; AAL13789.1; -; mRNA.
DR PIR; A40313; A40313.
DR RefSeq; NP_731295.1; NM_169248.4. [P25158-1]
DR RefSeq; NP_996186.1; NM_206464.3. [P25158-2]
DR PDB; 5A48; X-ray; 2.35 A; A/B=139-240.
DR PDB; 5A49; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=139-222.
DR PDB; 5A4A; X-ray; 1.70 A; A=401-606.
DR PDB; 5CD7; X-ray; 2.50 A; A/B/C/D/E/F=150-224.
DR PDB; 5CD8; X-ray; 3.00 A; A/B/C/D/E/F=150-240.
DR PDB; 5CD9; X-ray; 2.10 A; A=393-606.
DR PDB; 5NT7; X-ray; 1.40 A; A/C=139-240.
DR PDBsum; 5A48; -.
DR PDBsum; 5A49; -.
DR PDBsum; 5A4A; -.
DR PDBsum; 5CD7; -.
DR PDBsum; 5CD8; -.
DR PDBsum; 5CD9; -.
DR PDBsum; 5NT7; -.
DR AlphaFoldDB; P25158; -.
DR SMR; P25158; -.
DR BioGRID; 66235; 99.
DR DIP; DIP-18970N; -.
DR IntAct; P25158; 24.
DR STRING; 7227.FBpp0081435; -.
DR iPTMnet; P25158; -.
DR PaxDb; P25158; -.
DR PRIDE; P25158; -.
DR ABCD; P25158; 2 sequenced antibodies.
DR DNASU; 41066; -.
DR EnsemblMetazoa; FBtr0081954; FBpp0081435; FBgn0003015. [P25158-1]
DR EnsemblMetazoa; FBtr0081956; FBpp0089372; FBgn0003015. [P25158-2]
DR GeneID; 41066; -.
DR KEGG; dme:Dmel_CG10901; -.
DR UCSC; CG10901-RA; d. melanogaster. [P25158-1]
DR CTD; 41066; -.
DR FlyBase; FBgn0003015; osk.
DR VEuPathDB; VectorBase:FBgn0003015; -.
DR eggNOG; ENOG502SUPD; Eukaryota.
DR InParanoid; P25158; -.
DR OMA; LPEMTQI; -.
DR PhylomeDB; P25158; -.
DR SignaLink; P25158; -.
DR BioGRID-ORCS; 41066; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41066; -.
DR PRO; PR:P25158; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003015; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; P25158; baseline and differential.
DR Genevisible; P25158; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0043073; C:germ cell nucleus; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0045495; C:pole plasm; TAS:FlyBase.
DR GO; GO:0061803; C:posterior cell cortex; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; TAS:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:1903863; P:P granule assembly; IMP:FlyBase.
DR GO; GO:0030719; P:P granule organization; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; TAS:FlyBase.
DR GO; GO:0019094; P:pole plasm mRNA localization; TAS:FlyBase.
DR GO; GO:0007318; P:pole plasm protein localization; TAS:FlyBase.
DR GO; GO:0007359; P:posterior abdomen determination; IMP:FlyBase.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:FlyBase.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:FlyBase.
DR GO; GO:0046011; P:regulation of oskar mRNA translation; TAS:FlyBase.
DR GO; GO:0035282; P:segmentation; IMP:FlyBase.
DR GO; GO:0040040; P:thermosensory behavior; IMP:FlyBase.
DR GO; GO:0007632; P:visual behavior; IMP:FlyBase.
DR GO; GO:0008542; P:visual learning; IMP:FlyBase.
DR Gene3D; 3.30.420.610; -; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR041966; LOTUS-like.
DR InterPro; IPR033447; OSK.
DR InterPro; IPR025605; OST-HTH/LOTUS_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF17182; OSK; 1.
DR Pfam; PF12872; OST-HTH; 1.
DR PROSITE; PS51644; HTH_OST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..606
FT /note="Maternal effect protein oskar"
FT /id="PRO_0000058086"
FT DOMAIN 152..221
FT /note="HTH OST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT REGION 425..439
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..138
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_016006"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5NT7"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:5NT7"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5NT7"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:5NT7"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:5NT7"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:5A4A"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5A4A"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:5A4A"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 461..469
FT /evidence="ECO:0007829|PDB:5A4A"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 485..489
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 494..510
FT /evidence="ECO:0007829|PDB:5A4A"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 530..546
FT /evidence="ECO:0007829|PDB:5A4A"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5A4A"
FT HELIX 590..602
FT /evidence="ECO:0007829|PDB:5A4A"
SQ SEQUENCE 606 AA; 69284 MW; 9381287153E2D549 CRC64;
MAAVTSEFPS KPISYTSTNT SAKTYYLKSV KKRVTTCFQQ LRDKLQSSGS FRKSSSSCLN
QIFVRSDFSA CGERFRKIFK SARKTELPEL WKVPLVAHEL TSRQSSQQLQ VVARLFSSTQ
ISTKEITYNS NSNTSENNMT IIESNYISVR EEYPDIDSEV RAILLSHAQN GITISSIKSE
YRKLTGNPFP LHDNVTDFLL TIPNVTAECS ESGKRIFNLK ASLKNGHLLD MVLNQKERTS
DYSSGAPSLE NIPRAPPRYW KNPFKRRALS QLNTSPRTVP KITDEKTKDI ATRPVSLHQM
ANEAAESNWC YQDNWKHLNN FYQQASVNAP KMPVPINIYS PDAPEEPINL APPGHQPSCR
TQSQKTEPTE NRHLGIFVHP FNGMNIMKRR HEMTPTPTIL TSGTYNDSLL TINSDYDAYL
LDFPLMGDDF MLYLARMELK CRFRRHERVL QSGLCVSGLT INGARNRLKR VQLPEGTQII
VNIGSVDIMR GKPLVQIEHD FRLLIKEMHN MRLVPILTNL APLGNYCHDK VLCDKIYRFN
KFIRSECCHL KVIDIHSCLI NERGVVRFDC FQASPRQVTG SKEPYLFWNK IGRQRVLQVI
ETSLEY
