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 15-FEB-2017, entry version 42. 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; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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 CC acetylation (HAT) complex SAGA, a multiprotein complex that CC activates transcription by remodeling chromatin and mediating CC histone acetylation and deubiquitination. Within the SAGA complex, CC participates in a subcomplex that specifically deubiquitinates CC histone H2B. The SAGA complex is recruited to specific gene CC promoters by activators, where it is required for transcription. CC Required for nuclear receptor-mediated transactivation. Binds CC independently on SAGA to promoters in an RNA-dependent manner. CC Binds to mRNA and is essential for total mRNA export from the CC nucleus. Required to counteract heterochromatin silencing. CC Controls the development of neuronal connectivity in visual system CC by being required for accurate axon targeting in the optic lobe. CC Required for expression of ecdysone-induced genes such as CC br/broad. {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, CC Sgf11 and Spt3. Within the SAGA complex, Sgf11, e(y)2, and CC not/nonstop form an additional subcomplex of SAGA called the DUB CC module (deubiquitination module). Interacts directly with CC not/nonstop. Interacts with the AMEX complex component xmas-2. CC Interacts with Cbp80; important for promoter recruitment of Sgf11 CC that is not associated with the DUB module. {ECO:0000255|HAMAP- CC Rule:MF_03047}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP- CC Rule:MF_03047}. Nucleus, nuclear pore complex {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 CC pore complex (NPC). {ECO:0000255|HAMAP-Rule:MF_03047}. CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly CC lobe' of the SAGA deubiquitination module. {ECO:0000255|HAMAP- CC Rule:MF_03047}. CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with CC the C-terminal catalytic domain of not/nonstop forms the CC 'catalytic lobe' of the SAGA deubiquitination module. CC {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 STRING; 7260.FBpp0244204; -. DR EnsemblMetazoa; FBtr0245712; FBpp0244204; FBgn0217066. DR GeneID; 6642765; -. DR KEGG; dwi:Dwil_GK15061; -. DR FlyBase; FBgn0217066; Dwil\GK15061. DR eggNOG; KOG2612; Eukaryota. DR eggNOG; ENOG4111IPI; LUCA. DR InParanoid; B4MVH6; -. DR KO; K11363; -. DR OMA; CERTVAP; -. DR OrthoDB; EOG09150F8A; -. DR PhylomeDB; B4MVH6; -. DR Proteomes; UP000007798; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell. DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB. DR GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; 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; Complete proteome; Cytoplasm; KW Metal-binding; mRNA transport; Nuclear pore complex; Nucleus; KW Protein transport; Reference proteome; Transcription; KW Transcription regulation; Translocation; Transport; Zinc; Zinc-finger. FT CHAIN 1 209 SAGA-associated factor 11 homolog 1. FT /FTId=PRO_0000367532. FT ZN_FING 120 141 SGF11-type. {ECO:0000255|HAMAP- FT Rule:MF_03047}. 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 //