SG112_DROWI
ID SG112_DROWI Reviewed; 228 AA.
AC B4N4E1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=SAGA-associated factor 11 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03047};
GN Name=Sgf11-2 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=GK10782;
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 -!- SEQUENCE CAUTION:
CC Sequence=EDW79015.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; CH964095; EDW79015.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002068029.2; XM_002067993.2.
DR AlphaFoldDB; B4N4E1; -.
DR STRING; 7260.FBpp0239925; -.
DR EnsemblMetazoa; FBtr0241433; FBpp0239925; FBgn0212793.
DR GeneID; 6645423; -.
DR KEGG; dwi:6645423; -.
DR eggNOG; KOG2612; Eukaryota.
DR InParanoid; B4N4E1; -.
DR OrthoDB; 1407283at2759; -.
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 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..228
FT /note="SAGA-associated factor 11 homolog 2"
FT /id="PRO_0000367533"
FT ZN_FING 122..143
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 24113 MW; 9F98379152D9EA80 CRC64;
MSTTAAATTT TPSTMSNNQG QGQTTIPGTG TGTGAAKTTN RIINNFRALL KDPNNLDEAV
NYLYRTLIDD ATAGIFIETH HLRKTGNLAA LDGLAEESAY RICEMPNLDI FGISTAKKPM
DCTCPNCDRL VAAARFAPHL EKCMGMGRIS SRIASRRLAT KEGTSASSSS SSTYMHSGGD
RGGGGGHHAG AGGTDDEDDV DWSSDKRKKK STQSSRNNGS KKNNGKTF