GUS_DROME
ID GUS_DROME Reviewed; 279 AA.
AC A1Z6E0; A1Z6D7; A1Z6D9; A1Z6E2; F2FB59; Q7JUY1;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein gustavus {ECO:0000312|EMBL:AAM68373.2};
GN Name=gus; ORFNames=CG2944;
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] {ECO:0000312|EMBL:AAM68373.2}
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] {ECO:0000312|EMBL:AAM68373.2}
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] {ECO:0000312|EMBL:AAM50263.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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:0000312|EMBL:ADZ74173.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ADZ74173.1}; TISSUE=Embryo;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH VAS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=12479811; DOI=10.1016/s1534-5807(02)00361-1;
RA Styhler S., Nakamura A., Lasko P.;
RT "VASA localization requires the SPRY-domain and SOCS-box containing
RT protein, GUSTAVUS.";
RL Dev. Cell 3:865-876(2002).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH VAS AND CUL-5, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP TRP-219.
RX PubMed=20123973; DOI=10.1128/mcb.01100-09;
RA Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
RT "Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3
RT ligase specificity receptors.";
RL Mol. Cell. Biol. 30:1769-1782(2010).
RN [7] {ECO:0000305, ECO:0000312|PDB:2FNJ}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 27-251 IN COMPLEX WITH MOUSE
RP ELONGIN-B AND ELONGIN-C, INTERACTION WITH VAS, AND MUTAGENESIS OF TYR-131;
RP GLY-147; ARG-148; GLU-187; ARG-204 AND TRP-219.
RX PubMed=16498413; DOI=10.1038/sj.emboj.7600994;
RA Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.;
RT "Structural and functional insights into the B30.2/SPRY domain.";
RL EMBO J. 25:1353-1363(2006).
RN [8] {ECO:0000305, ECO:0000312|PDB:2IHS}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 27-232 IN COMPLEX WITH VAS
RP FRAGMENT, AND MUTAGENESIS OF TRP-219.
RX PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT "Structural basis for protein recognition by B30.2/SPRY domains.";
RL Mol. Cell 24:967-976(2006).
CC -!- FUNCTION: Involved in the localization of vas to the posterior pole of
CC the oocyte. Required maternally in the germ line for efficient
CC primordial germ cell formation. {ECO:0000269|PubMed:12479811,
CC ECO:0000269|PubMed:20123973}.
CC -!- SUBUNIT: Interacts (via B30.2/SPRY domain) with vas; this interaction
CC may be necessary for the transport of vas to the posterior pole of the
CC oocyte. Interacts with Cul-5. May associate with the Elongin BC complex
CC composed of Elongin-B and Elongin-C. {ECO:0000269|PubMed:12479811,
CC ECO:0000269|PubMed:16498413, ECO:0000269|PubMed:17189197,
CC ECO:0000269|PubMed:20123973}.
CC -!- INTERACTION:
CC A1Z6E0; O96757: stumps; NbExp=3; IntAct=EBI-75338, EBI-74922;
CC A1Z6E0; P09052: vas; NbExp=5; IntAct=EBI-75338, EBI-134067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811,
CC ECO:0000269|PubMed:20123973}. Nucleus {ECO:0000269|PubMed:12479811,
CC ECO:0000269|PubMed:20123973}. Note=Component of the cytoplasmic
CC ribonucleoprotein (RNP) bodies which concentrate at the perinuclear
CC region of the nurse cell and in punctate aggregates throughout the
CC cytoplasm. Some cortical enrichment of these aggregates is also
CC observed. At stage 7, accumulates in the anterior cytoplasm of the
CC oocyte, whereas during stage 10 accumulates at the posterior pole. This
CC posterior distribution is not maintained in later developmental stages.
CC {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries, primarily in nurse cells and
CC oocytes (at protein level). {ECO:0000269|PubMed:12479811,
CC ECO:0000269|PubMed:20123973}.
CC -!- DEVELOPMENTAL STAGE: Expressed during oogenesis, in early embryos (0 to
CC 4 hours) and in fertile adult females (at protein level).
CC {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}.
CC -!- DISRUPTION PHENOTYPE: Homozygous females produce defective eggs, which
CC desiccate and collapse soon after egg laying, or embryos, which hatch
CC very rarely. Mutants exhibit wing morphology defects, including
CC blistering, formation of ectopic vein material, and loss of material at
CC the margin. {ECO:0000269|PubMed:20123973}.
CC -!- SIMILARITY: Belongs to the SPSB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50263.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACU12389.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACX32987.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADZ74173.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ADZ74173.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; AAF57346.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF57347.3; -; Genomic_DNA.
DR EMBL; AE013599; AAG22337.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68372.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68373.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68374.2; -; Genomic_DNA.
DR EMBL; AY119609; AAM50263.1; ALT_INIT; mRNA.
DR EMBL; BT089043; ACU12389.1; ALT_INIT; mRNA.
DR EMBL; BT099916; ACX32987.1; ALT_INIT; mRNA.
DR EMBL; BT126146; ADZ74173.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001246140.1; NM_001259211.2.
DR RefSeq; NP_610158.3; NM_136314.4.
DR RefSeq; NP_724398.2; NM_165418.3.
DR RefSeq; NP_724399.2; NM_165419.3.
DR RefSeq; NP_724400.2; NM_165420.3.
DR RefSeq; NP_724401.2; NM_165421.3.
DR RefSeq; NP_724402.2; NM_165422.3.
DR PDB; 2FNJ; X-ray; 1.80 A; A=27-251.
DR PDB; 2IHS; X-ray; 2.20 A; A/B=27-232.
DR PDBsum; 2FNJ; -.
DR PDBsum; 2IHS; -.
DR AlphaFoldDB; A1Z6E0; -.
DR SMR; A1Z6E0; -.
DR BioGRID; 61396; 50.
DR IntAct; A1Z6E0; 35.
DR MINT; A1Z6E0; -.
DR STRING; 7227.FBpp0301582; -.
DR PaxDb; A1Z6E0; -.
DR DNASU; 35478; -.
DR EnsemblMetazoa; FBtr0309846; FBpp0301580; FBgn0026238.
DR EnsemblMetazoa; FBtr0309847; FBpp0301581; FBgn0026238.
DR EnsemblMetazoa; FBtr0309848; FBpp0301582; FBgn0026238.
DR EnsemblMetazoa; FBtr0309849; FBpp0301583; FBgn0026238.
DR EnsemblMetazoa; FBtr0309850; FBpp0301584; FBgn0026238.
DR EnsemblMetazoa; FBtr0309851; FBpp0301585; FBgn0026238.
DR EnsemblMetazoa; FBtr0309852; FBpp0301586; FBgn0026238.
DR GeneID; 35478; -.
DR KEGG; dme:Dmel_CG2944; -.
DR UCSC; CG2944-RA; d. melanogaster.
DR UCSC; CG2944-RB; d. melanogaster.
DR UCSC; CG2944-RD; d. melanogaster.
DR UCSC; CG2944-RE; d. melanogaster.
DR UCSC; CG2944-RF; d. melanogaster.
DR CTD; 35478; -.
DR FlyBase; FBgn0026238; gus.
DR VEuPathDB; VectorBase:FBgn0026238; -.
DR eggNOG; KOG3953; Eukaryota.
DR GeneTree; ENSGT01030000234629; -.
DR HOGENOM; CLU_046756_0_1_1; -.
DR InParanoid; A1Z6E0; -.
DR OMA; SWNADDR; -.
DR OrthoDB; 938259at2759; -.
DR PhylomeDB; A1Z6E0; -.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; A1Z6E0; -.
DR BioGRID-ORCS; 35478; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; A1Z6E0; -.
DR GenomeRNAi; 35478; -.
DR PRO; PR:A1Z6E0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026238; Expressed in cleaving embryo and 28 other tissues.
DR ExpressionAtlas; A1Z6E0; baseline and differential.
DR Genevisible; A1Z6E0; DM.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070449; C:elongin complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0045495; C:pole plasm; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:UniProtKB.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; IMP:UniProtKB.
DR GO; GO:0007315; P:pole plasm assembly; IMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:UniProtKB.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR Pfam; PF07525; SOCS_box; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome.
FT CHAIN 1..279
FT /note="Protein gustavus"
FT /id="PRO_0000422158"
FT DOMAIN 36..233
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 234..279
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 236..279
FT /note="Involved in binding to the Elongin BC complex"
FT /evidence="ECO:0000269|PubMed:16498413"
FT MUTAGEN 131
FT /note="Y->A: Does not affect binding to Elongin BC complex.
FT Abolishes interaction with vas."
FT /evidence="ECO:0000269|PubMed:16498413"
FT MUTAGEN 147
FT /note="G->Y: Does not affect binding to Elongin BC complex.
FT Abolishes interaction with vas."
FT /evidence="ECO:0000269|PubMed:16498413"
FT MUTAGEN 148
FT /note="R->W: Does not affect binding to Elongin BC complex.
FT Abolishes interaction with vas."
FT /evidence="ECO:0000269|PubMed:16498413"
FT MUTAGEN 187
FT /note="E->A: Does not affect binding to Elongin BC complex
FT or vas."
FT /evidence="ECO:0000269|PubMed:16498413"
FT MUTAGEN 204
FT /note="R->S: Does not affect binding to Elongin BC complex
FT or vas."
FT /evidence="ECO:0000269|PubMed:16498413"
FT MUTAGEN 219
FT /note="W->L: Does not affect binding to Elongin BC complex.
FT Decreases interaction with vas."
FT /evidence="ECO:0000269|PubMed:16498413,
FT ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:20123973"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 97..105
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2FNJ"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2FNJ"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2FNJ"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2FNJ"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:2FNJ"
FT HELIX 239..247
FT /evidence="ECO:0007829|PDB:2FNJ"
SQ SEQUENCE 279 AA; 31713 MW; DCA657FEEA83D785 CRC64;
MGQKISGGVK TVSRNDSQST FKPIIPRELQ ADFVKPARID ILLDMPPASR DLQLKHSWNS
EDRSLNIFVK EDDKLTFHRH PVAQSTDCIR GKVGLTKGLH IWEIYWPTRQ RGTHAVVGVC
TADAPLHSVG YQSLVGSTEQ SWGWDLGRNK LYHDSKNCAG VTYPAILKND EAFLVPDKFL
VALDMDEGTL SFIVDQQYLG IAFRGLRGKK LYPIVSAVWG HCEITMRYIG GLDPEPLPLM
DLCRRTIRQK IGRTNLEEHI QQLQLPLSMK TYLLYKNRR
