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ASTRX_DROME
ID   ASTRX_DROME             Reviewed;         167 AA.
AC   Q8SWX0; Q9VVU3;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Gametocyte-specific factor 1 homolog {ECO:0000305};
DE   AltName: Full=Protein asterix {ECO:0000312|FlyBase:FBgn0036826};
GN   Name=arx {ECO:0000312|FlyBase:FBgn0036826};
GN   Synonyms=Gtsf1 {ECO:0000303|PubMed:23913921, ECO:0000303|PubMed:23913922};
GN   ORFNames=CG3893 {ECO:0000312|FlyBase:FBgn0036826};
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 {ECO:0000312|EMBL:AAM11358.1};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAM11358.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM11358.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAM11358.1};
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   [4] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH PIWI, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF CYS-4; CYS-24; CYS-37 AND CYS-57.
RX   PubMed=23913921; DOI=10.1101/gad.221515.113;
RA   Ohtani H., Iwasaki Y.W., Shibuya A., Siomi H., Siomi M.C., Saito K.;
RT   "DmGTSF1 is necessary for Piwi-piRISC-mediated transcriptional transposon
RT   silencing in the Drosophila ovary.";
RL   Genes Dev. 27:1656-1661(2013).
RN   [5] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH PIWI, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23913922; DOI=10.1101/gad.221150.113;
RA   Doenertas D., Sienski G., Brennecke J.;
RT   "Drosophila Gtsf1 is an essential component of the Piwi-mediated
RT   transcriptional silencing complex.";
RL   Genes Dev. 27:1693-1705(2013).
CC   -!- FUNCTION: Acts via the piwi-interacting RNA (piRNA) pathway which
CC       mediates the repression of transposable elements during meiosis by
CC       forming complexes composed of piRNAs and piwi proteins and governs the
CC       methylation and subsequent repression of transposons. Required for
CC       repression of transposons and neighboring genes in ovarian somatic and
CC       germline cells. {ECO:0000269|PubMed:23913921,
CC       ECO:0000269|PubMed:23913922}.
CC   -!- SUBUNIT: Interacts with piwi. {ECO:0000269|PubMed:23913921,
CC       ECO:0000269|PubMed:23913922}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23913921,
CC       ECO:0000269|PubMed:23913922}.
CC   -!- DOMAIN: The zinc fingers are required for transcriptional silencing
CC       activity. {ECO:0000269|PubMed:23913921}.
CC   -!- DISRUPTION PHENOTYPE: Mutant females are viable but sterile
CC       (PubMed:23913922). They have small and severely deformed ovaries
CC       (PubMed:23913921, PubMed:23913922). Soma- and germline-specific
CC       transposable elements are severely derepressed in the ovary
CC       (PubMed:23913922). Ovaries lack a follicle cell layer and show
CC       misexpression of orb (PubMed:23913921). {ECO:0000269|PubMed:23913921,
CC       ECO:0000269|PubMed:23913922}.
CC   -!- SIMILARITY: Belongs to the UPF0224 (FAM112) family. {ECO:0000305}.
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DR   EMBL; AE014296; AAF49214.2; -; Genomic_DNA.
DR   EMBL; AY095030; AAM11358.1; -; mRNA.
DR   RefSeq; NP_649071.1; NM_140814.2.
DR   AlphaFoldDB; Q8SWX0; -.
DR   SMR; Q8SWX0; -.
DR   STRING; 7227.FBpp0074842; -.
DR   PaxDb; Q8SWX0; -.
DR   DNASU; 40061; -.
DR   EnsemblMetazoa; FBtr0075075; FBpp0074842; FBgn0036826.
DR   GeneID; 40061; -.
DR   KEGG; dme:Dmel_CG3893; -.
DR   UCSC; CG3893-RA; d. melanogaster.
DR   CTD; 170302; -.
DR   FlyBase; FBgn0036826; arx.
DR   VEuPathDB; VectorBase:FBgn0036826; -.
DR   eggNOG; KOG4376; Eukaryota.
DR   GeneTree; ENSGT00940000164745; -.
DR   HOGENOM; CLU_105561_0_0_1; -.
DR   InParanoid; Q8SWX0; -.
DR   OMA; HLIPEPE; -.
DR   OrthoDB; 1359124at2759; -.
DR   PhylomeDB; Q8SWX0; -.
DR   BioGRID-ORCS; 40061; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 40061; -.
DR   PRO; PR:Q8SWX0; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036826; Expressed in adult abdomen and 25 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IMP:FlyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   InterPro; IPR022776; TRM13/UPF0224_CHHC_Znf_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   Pfam; PF05253; zf-U11-48K; 2.
DR   SUPFAM; SSF57667; SSF57667; 2.
DR   PROSITE; PS51800; ZF_CHHC_U11_48K; 2.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Repeat;
KW   RNA-mediated gene silencing; Zinc; Zinc-finger.
FT   CHAIN           1..167
FT                   /note="Gametocyte-specific factor 1 homolog"
FT                   /id="PRO_0000435328"
FT   ZN_FING         1..28
FT                   /note="CHHC U11-48K-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   ZN_FING         34..61
FT                   /note="CHHC U11-48K-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   REGION          128..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT   MUTAGEN         4
FT                   /note="C->A: Decreased transposon silencing but no effect
FT                   on nuclear localization or interaction with piwi."
FT                   /evidence="ECO:0000269|PubMed:23913921"
FT   MUTAGEN         24
FT                   /note="C->A: Decreased transposon silencing but no effect
FT                   on nuclear localization or interaction with piwi."
FT                   /evidence="ECO:0000269|PubMed:23913921"
FT   MUTAGEN         37
FT                   /note="C->A: Decreased transposon silencing but no effect
FT                   on nuclear localization or interaction with piwi."
FT                   /evidence="ECO:0000269|PubMed:23913921"
FT   MUTAGEN         57
FT                   /note="C->A: Decreased transposon silencing but no effect
FT                   on nuclear localization or interaction with piwi."
FT                   /evidence="ECO:0000269|PubMed:23913921"
SQ   SEQUENCE   167 AA;  20076 MW;  484D2E198E53BFEB CRC64;
     MVYCPYNKEH KMLRKKLQQH ILKCRVIYKD TVELMVCPFN SSHLIPEPQF FQHTQSCEDR
     NIIVHYQTSA PAVLSEDTRH AKIESEENWD DDESVPDYDP QVYCSRANIV REPNGLFPAQ
     RRAFIEQEKR RHFGEDYEEE KKPRKAKARA DLRPTPYEHR RPYSRRQ
 
 
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