OSA_DROYA
ID OSA_DROYA Reviewed; 324 AA.
AC Q9NGB4;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 02-JUN-2021, entry version 77.
DE RecName: Full=Trithorax group protein osa;
DE AltName: Full=Protein eyelid;
DE Flags: Fragment;
GN Name=osa; Synonyms=eld;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10823947; DOI=10.1073/pnas.97.11.5960;
RA Begun D.J., Whitley P.;
RT "Reduced X-linked nucleotide polymorphism in Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5960-5965(2000).
CC -!- FUNCTION: Trithorax group (trxG) protein required for embryonic
CC segmentation, development of the notum and wing margin, and
CC photoreceptor differentiation. Required for the activation of genes
CC such as Antp, Ubx and Eve. Binds to DNA without specific affinity,
CC suggesting that it is recruited to promoters by promoter-specific
CC proteins. Essential component of the Brahma complex, a multiprotein
CC complex which is the equivalent of the yeast SWI/SNF complex and acts
CC by remodeling the chromatin by catalyzing an ATP-dependent alteration
CC in the structure of nucleosomal DNA. This complex can both serve as a
CC transcriptional coactivator or corepressor, depending on the context.
CC Acts as an essential coactivator for Zeste, which recruits the whole
CC complex to specific genes. In contrast, it acts as a corepressor for Wg
CC target genes, possibly via an interaction with Pan and Gro. It also
CC acts as a negative regulator for proneural achaete-scute, when it is
CC directly recruited by Pan and Chi. Also represses E2f activation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Brahma complex, which is composed of Brm,
CC Osa, Mor, Snr1/Bap45, Bap111/Dalao, Bap55, Bap60 and Bap47. Interacts
CC with Pnr and Chi via its EHD domain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AF255314; AAF68611.1; -; Genomic_DNA.
DR STRING; 7245.FBpp0270263; -.
DR EnsemblMetazoa; FBtr0401414; FBpp0360329; FBgn0041640.
DR eggNOG; KOG2510; Eukaryota.
DR ChiTaRS; osa; fly.
DR GO; GO:0035060; C:brahma complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; ISS:UniProtKB.
DR GO; GO:0046530; P:photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007379; P:segment specification; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR InterPro; IPR021906; BAF250/Osa.
DR InterPro; IPR033388; BAF250_C.
DR PANTHER; PTHR12656; PTHR12656; 1.
DR Pfam; PF12031; BAF250_C; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; Developmental protein; DNA-binding;
KW Nucleus; Repressor; Transcription; Transcription regulation.
FT CHAIN <1..>324
FT /note="Trithorax group protein osa"
FT /id="PRO_0000200595"
FT DOMAIN <1..126
FT /note="EHD"
FT REGION 132..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 324
SQ SEQUENCE 324 AA; 32653 MW; 65BA271ED4DDE03D CRC64;
YLAAADSAMA RTVALQSPCI SYLVAFIEQA EQTALGVANQ HGINYLRENP DSMGTSLDML
RRAAGTLLHL AKHPDNRSLF MQQEQRLLGL VMSHILDQQV ALIISRVLYQ VSRGTGPIHS
VEFRLLQQRQ QQQLRPASAE KQAASAGGSA PVKAEAASTE TSSTEAKPAP AATTAVVNDE
NSNSSQQLPP AATFNDVSNS STNSNSCGTV SSNQTNXXXX NSSHSSSAIS SQSAITVTAP
SAPATGATSA XXXAITSDQQ QVSKVAAAAA AAAALSNASA AAAAAAAAAA ASVGPPTSSS
VSAGAAVAQP AAPPPTNAGT TTAV