SGF11_DROPS
ID SGF11_DROPS Reviewed; 196 AA.
AC Q2LYX9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047};
GN Name=Sgf11 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=GA12241;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
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DR EMBL; CH379069; EAL29730.2; -; Genomic_DNA.
DR AlphaFoldDB; Q2LYX9; -.
DR SMR; Q2LYX9; -.
DR STRING; 7237.FBpp0274076; -.
DR eggNOG; KOG2612; Eukaryota.
DR HOGENOM; CLU_100743_0_0_1; -.
DR InParanoid; Q2LYX9; -.
DR OMA; EDSTYRM; -.
DR Proteomes; UP000001819; Genome assembly.
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 transcription, DNA-templated; 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; Phosphoprotein; Protein transport; Reference proteome;
KW Transcription; Transcription regulation; Translocation; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..196
FT /note="SAGA-associated factor 11 homolog"
FT /id="PRO_0000367528"
FT ZN_FING 102..123
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT REGION 140..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 21047 MW; 4661014D8F4C718F CRC64;
MPTSAAPVPA VAAQSPTTRK AIANNFRELT KDPKKLDEAA NQLYESLLED AVTGIFIEVH
HLRKIGNLSA LDGVAEESAH RICDVPNLDI FGVSTAKKAI DCTCPNCDRL VAAARFAPHL
EKCMGMGRIS SRIASRRLAT KEGTSASSNS SYVHSGANAG GTDDEDDVDW SSDKRKKKST
QNSRNNGSKK NNGKTF
