STEL5_DROME
ID STEL5_DROME Reviewed; 172 AA.
AC Q7KV19;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Stellate protein CG33243;
GN Name=Ste:CG33243; ORFNames=CG33243;
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 TISSUE SPECIFICITY, AND INTERACTION WITH CKII-ALPHA.
RX PubMed=7597082; DOI=10.1073/pnas.92.13.6067;
RA Bozzetti M.P., Massari S., Finelli P., Meggio F., Pinna L.A., Boldyreff B.,
RA Issinger O.G., Palumbo G., Ciriaco C., Bonaccorsi S., Pimpinelli S.;
RT "The Ste locus, a component of the parasitic cry-Ste system of Drosophila
RT melanogaster, encodes a protein that forms crystals in primary
RT spermatocytes and mimics properties of the beta subunit of casein kinase
RT 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6067-6071(1995).
RN [4]
RP INDUCTION.
RX PubMed=11513298; DOI=10.1007/s004120100136;
RA Stapleton W., Das S., McKee B.D.;
RT "A role of the Drosophila homeless gene in repression of Stellate in male
RT meiosis.";
RL Chromosoma 110:228-240(2001).
RN [5]
RP INDUCTION.
RX PubMed=11470406; DOI=10.1016/s0960-9822(01)00299-8;
RA Aravin A.A., Naumova N.M., Tulin A.V., Vagin V.V., Rozovsky Y.M.,
RA Gvozdev V.A.;
RT "Double-stranded RNA-mediated silencing of genomic tandem repeats and
RT transposable elements in the D. melanogaster germline.";
RL Curr. Biol. 11:1017-1027(2001).
CC -!- FUNCTION: Unknown. In males lacking the Y chromosome, its strong
CC overexpression leads to the appearance of proteinaceous star-shaped
CC crystals in the primary spermatocytes causing meiotic drive, possibly
CC by interfering with normal casein kinase 2 activity.
CC -!- SUBUNIT: Interacts in vitro with the casein kinase 2 alpha subunit
CC (CkII-alpha). The relevance of such interaction is however unclear in
CC vivo. {ECO:0000269|PubMed:7597082}.
CC -!- TISSUE SPECIFICITY: Probably not expressed in wild-type flies. In males
CC lacking the Y chromosome, it is testis-specific and constitutes the
CC main component of star-shaped crystals. {ECO:0000269|PubMed:7597082}.
CC -!- INDUCTION: In wild-type flies, it is strongly down-regulated by double-
CC stranded RNA (dsRNA) interference mediated by Su(Ste) transcripts. In
CC males lacking the Y chromosome, the absence of Su(Ste) locus, relieves
CC such down-regulation, explaining why it is strongly expressed.
CC {ECO:0000269|PubMed:11470406, ECO:0000269|PubMed:11513298}.
CC -!- MISCELLANEOUS: There are multiple copies of the stellate gene in fruit
CC fly, encoding proteins that are extremely similar, which makes their
CC individual characterization difficult. Thus, most experiments probably
CC do not discriminate between the different members.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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DR EMBL; AE014298; AAS65331.2; -; Genomic_DNA.
DR RefSeq; NP_996425.2; NM_206702.2.
DR AlphaFoldDB; Q7KV19; -.
DR SMR; Q7KV19; -.
DR STRING; 7227.FBpp0289369; -.
DR PaxDb; Q7KV19; -.
DR EnsemblMetazoa; FBtr0300092; FBpp0289369; FBgn0053243.
DR GeneID; 2768897; -.
DR KEGG; dme:Dmel_CG33243; -.
DR UCSC; CG33243-RB; d. melanogaster.
DR CTD; 2768897; -.
DR FlyBase; FBgn0053243; Ste:CG33243.
DR VEuPathDB; VectorBase:FBgn0053243; -.
DR eggNOG; KOG3092; Eukaryota.
DR GeneTree; ENSGT00390000003781; -.
DR HOGENOM; CLU_034027_3_3_1; -.
DR InParanoid; Q7KV19; -.
DR PhylomeDB; Q7KV19; -.
DR GenomeRNAi; 2768897; -.
DR PRO; PR:Q7KV19; -.
DR Proteomes; UP000000803; Chromosome X.
DR Genevisible; Q7KV19; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:FlyBase.
DR GO; GO:0019887; F:protein kinase regulator activity; IMP:FlyBase.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IMP:FlyBase.
DR Gene3D; 1.10.1820.10; -; 1.
DR InterPro; IPR016149; Casein_kin_II_reg-sub_N.
DR InterPro; IPR035991; Casein_kinase_II_beta-like.
DR InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR PANTHER; PTHR11740; PTHR11740; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; SSF57798; 1.
DR PROSITE; PS01101; CK2_BETA; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..172
FT /note="Stellate protein CG33243"
FT /id="PRO_0000068265"
SQ SEQUENCE 172 AA; 19573 MW; C863151461F7CB7A CRC64;
MSSSQNNNSS WIDWFLGIKG NQFLCRVPTD YVQDTFNQMG LEYFSEILDV ILKPVIDSSS
GLLYGDEKKW YGMIHARYIR SERGLIAMHR KYLRGDFGSC PNISCYRQNT LPVGLSAVWG
KSTVKIHCPR CKSNFHPKSD TQLDGAMFGP SFPDIFFSML PNLTSPLDDP RT
