CHRC_DROME
ID CHRC_DROME Reviewed; 140 AA.
AC Q9V452;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Chromatin accessibility complex 16kD protein {ECO:0000312|FlyBase:FBgn0043001};
GN Name=Chrac-16 {ECO:0000303|PubMed:10856248,
GN ECO:0000312|FlyBase:FBgn0043001};
GN Synonyms=CHRAC {ECO:0000312|FlyBase:FBgn0043001},
GN CHRAC16 {ECO:0000303|PubMed:16260604, ECO:0000312|FlyBase:FBgn0043001},
GN joey {ECO:0000312|FlyBase:FBgn0043001};
GN ORFNames=CG15736 {ECO:0000312|FlyBase:FBgn0043001};
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|EMBL:CAB70603.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-23 AND 51-55,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE CHRAC
RP COMPLEX, INTERACTION WITH CHRAC-14, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10856248; DOI=10.1093/emboj/19.12.3049;
RA Corona D.F., Eberharter A., Budde A., Deuring R., Ferrari S.,
RA Varga-Weisz P., Wilm M., Tamkun J., Becker P.B.;
RT "Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally
RT regulated subunits of chromatin accessibility complex (CHRAC).";
RL EMBO J. 19:3049-3059(2000).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:AAM29520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM29520.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM29520.1};
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 [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE CHRAC COMPLEX, INTERACTION WITH CHRAC-16,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11447119; DOI=10.1093/emboj/20.14.3781;
RA Eberharter A., Ferrari S., Laengst G., Straub T., Imhof A., Varga-Weisz P.,
RA Wilm M., Becker P.B.;
RT "Acf1, the largest subunit of CHRAC, regulates ISWI-induced nucleosome
RT remodelling.";
RL EMBO J. 20:3781-3788(2001).
RN [6] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=26851213; DOI=10.1016/j.ydbio.2016.01.039;
RA Boerner K., Jain D., Vazquez-Pianzola P., Vengadasalam S., Steffen N.,
RA Fyodorov D.V., Tomancak P., Konev A., Suter B., Becker P.B.;
RT "A role for tuned levels of nucleosome remodeler subunit ACF1 during
RT Drosophila oogenesis.";
RL Dev. Biol. 411:217-230(2016).
RN [7] {ECO:0007744|PDB:2BYK, ECO:0007744|PDB:2BYM}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 29-100 IN COMPLEX WITH CHRAC-14,
RP FUNCTION, INTERACTION WITH ACF, AND MUTAGENESIS OF 2-GLY--LEU-18 AND
RP 118-ASP--GLU-140.
RX PubMed=16260604; DOI=10.1128/mcb.25.22.9886-9896.2005;
RA Hartlepp K.F., Fernandez-Tornero C., Eberharter A., Grune T., Muller C.W.,
RA Becker P.B.;
RT "The histone fold subunits of Drosophila CHRAC facilitate nucleosome
RT sliding through dynamic DNA interactions.";
RL Mol. Cell. Biol. 25:9886-9896(2005).
CC -!- FUNCTION: Histone-like protein which promotes nucleosome sliding of
CC ATP-dependent nucleosome remodeling complexes (PubMed:10856248,
CC PubMed:11447119). Part of the chromatin-accessibility complex (CHRAC)
CC which uses energy/ATP to increase the general accessibility of DNA in
CC chromatin (PubMed:10856248, PubMed:11447119). As an heterodimer with
CC Chrac-14, binds DNA and facilitates nucleosome sliding by Acf
CC (PubMed:16260604). As part of the CHRAC complex, required for oogenesis
CC (PubMed:26851213). {ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:11447119, ECO:0000269|PubMed:16260604,
CC ECO:0000269|PubMed:26851213}.
CC -!- SUBUNIT: Component of the chromatin accessibility complex (CHRAC),
CC composed of Chrac-14, Chrac-16, Acf and Iswi (PubMed:10856248,
CC PubMed:10731132). Forms an heterodimer with Chrac-14 (PubMed:10856248,
CC PubMed:16260604). The Chrac-14/Chrac-16 heterodimer interacts with Acf
CC (via N-terminus) (PubMed:16260604). Stabilizes the interaction between
CC Chrac-14 and Iswi (PubMed:10856248). {ECO:0000269|PubMed:10731132,
CC ECO:0000269|PubMed:10856248, ECO:0000269|PubMed:16260604}.
CC -!- INTERACTION:
CC Q9V452; Q9V444: Chrac-14; NbExp=10; IntAct=EBI-193917, EBI-138718;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:11447119}.
CC -!- DEVELOPMENTAL STAGE: Expressed in nurse cells and oocytes of all stages
CC (PubMed:26851213). Expressed in oocytes and embryos and down-regulated
CC afterwards (PubMed:10856248). {ECO:0000269|PubMed:10856248,
CC ECO:0000269|PubMed:26851213}.
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DR EMBL; AJ271142; CAB70603.1; -; mRNA.
DR EMBL; AE014298; AAF48131.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59618.1; -; Genomic_DNA.
DR EMBL; AY113515; AAM29520.1; -; mRNA.
DR RefSeq; NP_001285148.1; NM_001298219.1.
DR RefSeq; NP_572776.1; NM_132548.3.
DR PDB; 2BYK; X-ray; 2.40 A; A/C=1-140.
DR PDB; 2BYM; X-ray; 2.80 A; A/C=1-140.
DR PDBsum; 2BYK; -.
DR PDBsum; 2BYM; -.
DR AlphaFoldDB; Q9V452; -.
DR SMR; Q9V452; -.
DR DIP; DIP-20460N; -.
DR IntAct; Q9V452; 5.
DR STRING; 7227.FBpp0073475; -.
DR PaxDb; Q9V452; -.
DR DNASU; 32166; -.
DR EnsemblMetazoa; FBtr0073642; FBpp0073475; FBgn0043001.
DR EnsemblMetazoa; FBtr0339625; FBpp0308688; FBgn0043001.
DR GeneID; 32166; -.
DR KEGG; dme:Dmel_CG15736; -.
DR UCSC; CG15736-RA; d. melanogaster.
DR CTD; 32166; -.
DR FlyBase; FBgn0043001; Chrac-16.
DR VEuPathDB; VectorBase:FBgn0043001; -.
DR eggNOG; KOG1657; Eukaryota.
DR GeneTree; ENSGT00940000166127; -.
DR HOGENOM; CLU_045277_11_3_1; -.
DR InParanoid; Q9V452; -.
DR OMA; DHSENEA; -.
DR OrthoDB; 1622159at2759; -.
DR PhylomeDB; Q9V452; -.
DR BioGRID-ORCS; 32166; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Chrac-16; fly.
DR EvolutionaryTrace; Q9V452; -.
DR GenomeRNAi; 32166; -.
DR PRO; PR:Q9V452; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0043001; Expressed in secondary oocyte and 25 other tissues.
DR GO; GO:0008623; C:CHRAC; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR DisProt; DP00811; -.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Reference proteome.
FT CHAIN 1..140
FT /note="Chromatin accessibility complex 16kD protein"
FT /id="PRO_0000448482"
FT REGION 111..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 2..18
FT /note="Missing: When in a heterodimer with Chrac-14, does
FT not affect DNA binding or Acf nucleosome sliding activity."
FT /evidence="ECO:0000269|PubMed:16260604"
FT MUTAGEN 118..140
FT /note="Missing: When in a heterodimer with Chrac-14,
FT enhances DNA binding."
FT /evidence="ECO:0000269|PubMed:16260604"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2BYK"
FT HELIX 40..66
FT /evidence="ECO:0007829|PDB:2BYK"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:2BYK"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2BYK"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2BYK"
SQ SEQUENCE 140 AA; 16003 MW; 12E1D381432F1360 CRC64;
MGEPRSQPPV ERPPTAETFL PLSRVRTIMK SSMDTGLITN EVLFLMTKCT ELFVRHLAGA
AYTEEFGQRP GEALKYEHLS QVVNKNKNLE FLLQIVPQKI RVHQFQEMLR LNRSAGSDDD
DDDDDDDDEE ESESESESDE
