GRAU_DROME
ID GRAU_DROME Reviewed; 570 AA.
AC Q9U405; Q9W2N7;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Transcription factor grauzone;
GN Name=grau; ORFNames=CG3282;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTANTS QQ36 AND QE70.
RX PubMed=10683177; DOI=10.1242/dev.127.6.1243;
RA Chen B., Harms E., Chu T., Henrion G., Strickland S.;
RT "Completion of meiosis in Drosophila oocytes requires transcriptional
RT control by grauzone, a new zinc finger protein.";
RL Development 127:1243-1251(2000).
RN [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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [5]
RP FUNCTION, DNA-BINDING, AND MUTANTS QQ36 AND QE70.
RX PubMed=10924478; DOI=10.1093/genetics/155.4.1831;
RA Harms E., Chu T., Henrion G., Strickland S.;
RT "The only function of Grauzone required for Drosophila oocyte meiosis is
RT transcriptional activation of the cortex gene.";
RL Genetics 155:1831-1839(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-81, AND SUBUNIT.
RX PubMed=14604529; DOI=10.1016/j.str.2003.09.015;
RA Jauch R., Bourenkov G.P., Chung H.-R., Urlaub H., Reidt U., Jaeckle H.,
RA Wahl M.C.;
RT "The zinc finger-associated domain of the Drosophila transcription factor
RT grauzone is a novel zinc-coordinating protein-protein interaction module.";
RL Structure 11:1393-1402(2003).
CC -!- FUNCTION: Transcription factor essential for the completion of meiosis
CC in oocytes. Grauzone binds to the promoter region of cort via the zf-AD
CC domain and activates cort expression in ovaries.
CC {ECO:0000269|PubMed:10683177, ECO:0000269|PubMed:10924478}.
CC -!- SUBUNIT: Homodimer; at the zf-AD. {ECO:0000269|PubMed:14604529}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10683177}.
CC -!- TISSUE SPECIFICITY: Present throughout embryogenesis, in larvae, in
CC ovaries and other tissues of adult females, and in adult males. In
CC ovaries, it is expressed in both follicle cells and nurse cells.
CC Expressed from stage 9 in the germarium. Weakly or not expressed in the
CC oocyte nucleus. {ECO:0000269|PubMed:10683177}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC -!- DOMAIN: The N-terminal zf-AD is an atypical treble-clef like zinc
CC binding domain which enables dimerization, and appears not to have any
CC DNA-binding ability. DNA binding is achieved through the zinc fingers
CC at the C-terminus.
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DR EMBL; AF208016; AAF25356.1; -; mRNA.
DR EMBL; AE013599; AAF46653.2; -; Genomic_DNA.
DR EMBL; AY047537; AAK77269.1; -; mRNA.
DR RefSeq; NP_788422.1; NM_176242.3.
DR PDB; 1PZW; X-ray; 2.00 A; A=2-81.
DR PDBsum; 1PZW; -.
DR AlphaFoldDB; Q9U405; -.
DR SMR; Q9U405; -.
DR BioGRID; 69943; 20.
DR DIP; DIP-20107N; -.
DR IntAct; Q9U405; 5.
DR STRING; 7227.FBpp0071477; -.
DR PaxDb; Q9U405; -.
DR PRIDE; Q9U405; -.
DR DNASU; 45871; -.
DR EnsemblMetazoa; FBtr0071548; FBpp0071477; FBgn0001133.
DR GeneID; 45871; -.
DR KEGG; dme:Dmel_CG33133; -.
DR UCSC; CG33133-RA; d. melanogaster.
DR CTD; 45871; -.
DR FlyBase; FBgn0001133; grau.
DR VEuPathDB; VectorBase:FBgn0001133; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000169568; -.
DR HOGENOM; CLU_002678_94_13_1; -.
DR InParanoid; Q9U405; -.
DR OMA; ERQSPDM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9U405; -.
DR SignaLink; Q9U405; -.
DR BioGRID-ORCS; 45871; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; Q9U405; -.
DR GenomeRNAi; 45871; -.
DR PRO; PR:Q9U405; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001133; Expressed in embryonic/larval hemocyte (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9U405; baseline and differential.
DR Genevisible; Q9U405; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007349; P:cellularization; HMP:FlyBase.
DR GO; GO:0007343; P:egg activation; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0045143; P:homologous chromosome segregation; TAS:FlyBase.
DR GO; GO:0007279; P:pole cell formation; HMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR InterPro; IPR039970; TF_Grauzone.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23225; PTHR23225; 1.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Meiosis; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..570
FT /note="Transcription factor grauzone"
FT /id="PRO_0000046923"
FT DOMAIN 2..80
FT /note="ZAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263"
FT ZN_FING 240..263
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 296..318
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..349
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..409
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..441
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..471
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 476..498
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 504..527
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 120..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..570
FT /note="DNA-binding"
FT MOTIF 383..399
FT /note="Bipartite nuclear localization signal 1"
FT /evidence="ECO:0000255"
FT MOTIF 523..539
FT /note="Bipartite nuclear localization signal 2"
FT /evidence="ECO:0000255"
FT COMPBIAS 152..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263,
FT ECO:0000269|PubMed:14604529, ECO:0007744|PDB:1PZW"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263,
FT ECO:0000269|PubMed:14604529, ECO:0007744|PDB:1PZW"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263,
FT ECO:0000269|PubMed:14604529, ECO:0007744|PDB:1PZW"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01263,
FT ECO:0000269|PubMed:14604529, ECO:0007744|PDB:1PZW"
FT MUTAGEN 298
FT /note="C->Y: In QQ36; defects in female meiosis. Abolishes
FT DNA-binding activity."
FT MUTAGEN 493
FT /note="E->K: In QE70; defects in female meiosis. Abolishes
FT DNA-binding activity."
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:1PZW"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1PZW"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:1PZW"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1PZW"
FT HELIX 54..79
FT /evidence="ECO:0007829|PDB:1PZW"
SQ SEQUENCE 570 AA; 65967 MW; 33B550B964C1EA7C CRC64;
MDICRLCLRG VSGAQMCLQI FDVDSGESKV AEVLRQHFWF EVLPNDEISK VICNVCWTQV
SEFHQFYVSI QEAQVIYATT SKFKQDPEMV NTSWPEEVLM PADVLAVDND VGAQINVNPL
DELDLSQPMS PEDSKVGIKT ERQSPDMELL FEDANNEQDE DYEDDEDDDT DDLIVTRSGR
KRKRDVAKPA KTKRGTVSVG RKGKEKMVVK RGPPKRIFKM ERLPPFCKED EELIKRYIVM
GCELCIFLAE DFDGIREHFK DKHPDERPYI KCCGRKLNKR CLIQEHARRH ENPEYIKCKD
CGKVFANSSV LRAHWLVHHV PDEECDFQCE DCGKRFSRRN LLELHKGSHV PVNERKFICP
QCPKHNAFAT EYHMQVHISM QHRKAANICH VCGKKIKDKA VFEKHVRLHF EESGPRIKCP
RPDCESWLKD EDNLKQHLRR HNDEGKLFIC SECGKSCKNS RALIGHKRYS HSNVIYTCEQ
CGKTFKKDIS LKEHMAQHTG EPLYKCPFCP RTFNSNANMH SHKKKMHPVE WDIWRKTKTG
SSQKVLPSAQ VAQMFRDDAD VAAIANDYSG
