ID SG111_DROWI Reviewed; 209 AA. AC B4MVH6; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 12-OCT-2022, entry version 67. DE RecName: Full=SAGA-associated factor 11 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03047}; GN Name=Sgf11-1 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=GK15061; OS Drosophila willistoni (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7260; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 14030-0811.24; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- FUNCTION: Component of the transcription regulatory histone acetylation CC (HAT) complex SAGA, a multiprotein complex that activates transcription CC by remodeling chromatin and mediating histone acetylation and CC deubiquitination. Within the SAGA complex, participates in a subcomplex CC that specifically deubiquitinates histone H2B. The SAGA complex is CC recruited to specific gene promoters by activators, where it is CC required for transcription. Required for nuclear receptor-mediated CC transactivation. Binds independently on SAGA to promoters in an RNA- CC dependent manner. Binds to mRNA and is essential for total mRNA export CC from the nucleus. Required to counteract heterochromatin silencing. CC Controls the development of neuronal connectivity in visual system by CC being required for accurate axon targeting in the optic lobe. Required CC for expression of ecdysone-induced genes such as br/broad. CC {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT CC complexes, at least composed of Ada2b, not/nonstop, Pcaf/Gcn5, Sgf11 CC and Spt3. Within the SAGA complex, Sgf11, e(y)2, and not/nonstop form CC an additional subcomplex of SAGA called the DUB module CC (deubiquitination module). Interacts directly with not/nonstop. CC Interacts with the AMEX complex component xmas-2. Interacts with Cbp80; CC important for promoter recruitment of Sgf11 that is not associated with CC the DUB module. {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP- CC Rule:MF_03047}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03047}. CC Note=Localizes to nuclear periphery, in contact with the nuclear pore CC complex (NPC). {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of CC the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the CC C-terminal catalytic domain of not/nonstop forms the 'catalytic lobe' CC of the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP- CC Rule:MF_03047}. 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; CH963857; EDW75696.1; -; Genomic_DNA. DR RefSeq; XP_002064710.2; XM_002064674.2. DR AlphaFoldDB; B4MVH6; -. DR SMR; B4MVH6; -. DR STRING; 7260.FBpp0244204; -. DR eggNOG; KOG2612; Eukaryota. DR HOGENOM; CLU_100743_0_0_1; -. DR InParanoid; B4MVH6; -. DR OMA; NCNRNMA; -. DR OrthoDB; 1407283at2759; -. DR PhylomeDB; B4MVH6; -. DR Proteomes; UP000007798; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule. DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule. DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB. DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB. DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule. DR GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-UniRule. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR HAMAP; MF_03047; Sgf11; 1. DR InterPro; IPR013246; SAGA_su_Sgf11. DR Pfam; PF08209; Sgf11; 1. PE 3: Inferred from homology; KW Activator; Chromatin regulator; Cytoplasm; Metal-binding; mRNA transport; KW Nucleus; Protein transport; Reference proteome; Transcription; KW Transcription regulation; Translocation; Transport; Zinc; Zinc-finger. FT CHAIN 1..209 FT /note="SAGA-associated factor 11 homolog 1" FT /id="PRO_0000367532" FT ZN_FING 120..141 FT /note="SGF11-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 156..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..173 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..209 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 209 AA; 22684 MW; 110ABCF23F669012 CRC64; MSRTIVVKNP RTSGKDEDKA QIPSQDELPS GSSGAKTTNQ IISEFRALIK DPIKLDEAVN YLYETLVDDA AVGIFIETRQ LQKTGSLTAL EGTVEETNDM CDLPDCDIFG MSTAEKTAKC CCPNCERMVA AVRFAPHLQT CLGLGRSSSR AALRRLTVSS RSSSTSTGGG QANEKSTDDE DWSLDSRPGK STKNSRNKGS KKNQKNKLK //