ZN277_DROME
ID ZN277_DROME Reviewed; 452 AA.
AC Q9W1V7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Zinc finger protein 277 {ECO:0000250|UniProtKB:Q9NRM2};
GN ORFNames=CG9890 {ECO:0000312|FlyBase:FBgn0034814};
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|Proteomes:UP000000803};
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:AAL29058.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL29058.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL29058.1};
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 E(Y)2; ORC2; ORC3; GCN5; THOC5; TBP AND
RP POLYBROMO, AND SUBCELLULAR LOCATION.
RX PubMed=30713769;
RA Fursova N.A., Nikolenko J.V., Soshnikova N.V., Mazina M.Y., Vorobyova N.E.,
RA Krasnov A.N.;
RT "Zinc Finger Protein CG9890 - New Component of ENY2-Containing Complexes of
RT Drosophila.";
RL Acta Naturae 10:110-114(2018).
RN [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=33456983; DOI=10.32607/actanaturae.11056;
RA Fursova N.A., Mazina M.Y., Nikolenko J.V., Vorobyova N.E., Krasnov A.N.;
RT "Drosophila Zinc Finger Protein CG9890 Is Colocalized with Chromatin
RT Modifying and Remodeling Complexes on Gene Promoters and Involved in
RT Transcription Regulation.";
RL Acta Naturae 12:114-119(2020).
CC -!- FUNCTION: DNA binding protein which is involved in the positive
CC regulation of both basal and inducible transcription (PubMed:33456983).
CC Mainly localizes to active promoter sites and interacts with components
CC of various transcription and replication regulatory complexes, such as
CC the ORC, SAGA, THO, TFIID and SWI/SNF complexes (PubMed:30713769,
CC PubMed:33456983). It may therefore regulate transcription by promoting
CC the association of these complexes to their binding sites
CC (PubMed:30713769, PubMed:33456983). {ECO:0000269|PubMed:30713769,
CC ECO:0000269|PubMed:33456983}.
CC -!- SUBUNIT: Interacts with components of the origin recognition complex
CC (ORC) complex, Orc2 and Orc3, components of the SAGA transcription
CC coactivator-HAT complex, Gcn5 and e(y)2, components of the mRNP
CC biogenesis THO complex, thoc5 and e(y)2, and a component of the TFIID
CC complex, TBP (PubMed:30713769). Also interacts with polybromo, a
CC component of the chromatin remodeling SWI/SNF complex
CC (PubMed:30713769). {ECO:0000269|PubMed:30713769}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30713769,
CC ECO:0000269|PubMed:33456983}. Cytoplasm {ECO:0000269|PubMed:30713769}.
CC Note=Predominantly localizes to the cell nucleus (PubMed:30713769).
CC Associates with chromatin (PubMed:33456983).
CC {ECO:0000269|PubMed:30713769, ECO:0000269|PubMed:33456983}.
CC -!- SIMILARITY: Belongs to the ZNF277 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF46945.1; -; Genomic_DNA.
DR EMBL; AY061510; AAL29058.1; -; mRNA.
DR RefSeq; NP_611750.1; NM_137906.4.
DR IntAct; Q9W1V7; 6.
DR STRING; 7227.FBpp0071893; -.
DR DNASU; 37659; -.
DR EnsemblMetazoa; FBtr0071984; FBpp0071893; FBgn0034814.
DR GeneID; 37659; -.
DR KEGG; dme:Dmel_CG9890; -.
DR UCSC; CG9890-RA; d. melanogaster.
DR FlyBase; FBgn0034814; CG9890.
DR VEuPathDB; VectorBase:FBgn0034814; -.
DR eggNOG; KOG2482; Eukaryota.
DR GeneTree; ENSGT00390000010852; -.
DR HOGENOM; CLU_033436_0_0_1; -.
DR OMA; HEFEQYC; -.
DR OrthoDB; 1498904at2759; -.
DR BioGRID-ORCS; 37659; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37659; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034814; Expressed in oviduct (Drosophila) and 20 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040048; ZNF277.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13267; PTHR13267; 1.
DR Pfam; PF12756; zf-C2H2_2; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Zinc; Zinc-finger.
FT CHAIN 1..452
FT /note="Zinc finger protein 277"
FT /id="PRO_0000455831"
FT ZN_FING 200..224
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 361..385
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ SEQUENCE 452 AA; 53217 MW; 5CC0EB6AAE12C9CD CRC64;
MEHEVAVSGG DSSLEEITGS SKLKPSKNTA IKCLKCDKVY IFPSDKDDCL AHLYMEHRLV
IADVEDIALL EDYLQYWEKE FHTHEFEQYC TTMFLDQLPD GKYAKNEKYY LLCDILPQDY
ELRRRLKEKR LSEALERHQF ELTDRTFSKE CLFCRAIIKG LRADYLDHLF DKHFLLVGKP
EKLVYVDELL DHLEENLNRL MCLYCEKIFR DRPTLKEHMR KKGHKRINPN RREYDKYFLI
NYNRVPTAPT PRKQHLQKRR RETASVSTVA DPETGSVDFD KHFARPDSDG EHDSDWSDWA
ADGEPSSIKC LFCHHLGDNF TALKKHMHEV HRLDFEKATS SLNFYQRVKV VNYLRRQMCL
LRCVTCDLQF DEEELLVEHM AQESHHGIGD KESWDKPEFF FPYIENDGLL CVLDDSGGDD
PDVDTVRIIS EDSLAQINKD AERLSLENFK LL
