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