SGF11_DROME
ID SGF11_DROME Reviewed; 196 AA.
AC Q9VVR6; Q4V5G1; Q4V623;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047};
GN Name=Sgf11 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=CG13379;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN THE SAGA COMPLEX, AND
RP INTERACTION WITH NOT.
RX PubMed=18188155; DOI=10.1038/sj.emboj.7601966;
RA Weake V.M., Lee K.K., Guelman S., Lin C.-H., Seidel C., Abmayr S.M.,
RA Workman J.L.;
RT "SAGA-mediated H2B deubiquitination controls the development of neuronal
RT connectivity in the Drosophila visual system.";
RL EMBO J. 27:394-405(2008).
RN [5]
RP FUNCTION.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CBP80 AND XMAS-2.
RX PubMed=22989713; DOI=10.1093/nar/gks857;
RA Gurskiy D., Orlova A., Vorobyeva N., Nabirochkina E., Krasnov A.,
RA Shidlovskii Y., Georgieva S., Kopytova D.;
RT "The DUBm subunit Sgf11 is required for mRNA export and interacts with
RT Cbp80 in Drosophila.";
RL Nucleic Acids Res. 40:10689-10700(2012).
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, ECO:0000269|PubMed:18188155,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:22989713}.
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 ECO:0000269|PubMed:18188155, ECO:0000269|PubMed:22989713}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03047, ECO:0000269|PubMed:22989713}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03047, ECO:0000269|PubMed:22989713}.
CC Note=Localizes to nuclear periphery, in contact with the nuclear pore
CC complex (NPC).
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 -!- DISRUPTION PHENOTYPE: Defects in the number and migration of glial
CC cells located within the lamina plexus of the developing eye; the lack
CC of glial cells causing mistargeting of the R1-R6 axons in the optic
CC lobe. Lamina neuron development is normal.
CC {ECO:0000269|PubMed:18188155}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP-
CC Rule:MF_03047}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY54899.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAY55035.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY55111.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF49243.2; -; Genomic_DNA.
DR EMBL; BT022483; AAY54899.1; ALT_FRAME; mRNA.
DR EMBL; BT022695; AAY55111.1; ALT_INIT; mRNA.
DR EMBL; BT022619; AAY55035.1; ALT_INIT; mRNA.
DR EMBL; BT044301; ACH92366.1; -; mRNA.
DR RefSeq; NP_001097638.1; NM_001104168.2.
DR AlphaFoldDB; Q9VVR6; -.
DR SMR; Q9VVR6; -.
DR BioGRID; 65316; 44.
DR IntAct; Q9VVR6; 12.
DR MINT; Q9VVR6; -.
DR STRING; 7227.FBpp0112092; -.
DR iPTMnet; Q9VVR6; -.
DR PaxDb; Q9VVR6; -.
DR DNASU; 40035; -.
DR EnsemblMetazoa; FBtr0113179; FBpp0112092; FBgn0036804.
DR GeneID; 40035; -.
DR KEGG; dme:Dmel_CG13379; -.
DR UCSC; CG13379-RB; d. melanogaster.
DR CTD; 40035; -.
DR FlyBase; FBgn0036804; Sgf11.
DR VEuPathDB; VectorBase:FBgn0036804; -.
DR eggNOG; KOG2612; Eukaryota.
DR GeneTree; ENSGT00940000167574; -.
DR HOGENOM; CLU_100743_0_0_1; -.
DR InParanoid; Q9VVR6; -.
DR OMA; EDSTYRM; -.
DR OrthoDB; 1407283at2759; -.
DR PhylomeDB; Q9VVR6; -.
DR SignaLink; Q9VVR6; -.
DR BioGRID-ORCS; 40035; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 40035; -.
DR PRO; PR:Q9VVR6; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036804; Expressed in capitellum (Drosophila) and 26 other tissues.
DR Genevisible; Q9VVR6; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071819; C:DUBm complex; IDA:FlyBase.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0016578; P:histone deubiquitination; IDA:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR Pfam; PF08209; Sgf11; 1.
PE 1: Evidence at protein level;
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_0000367525"
FT ZN_FING 106..127
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 196 AA; 21322 MW; E5A56FCFAFFB67C8 CRC64;
MSAANMPTTT GAQGSGNQVP TTSTTIVNHF RELIKEPKNL DEAANYLYQS LLDDAVVGIF
NETHHLRKSG NLAALDGVPE DSTYRMCEMP NLDIFGISTA KKPMDCTCPN CDRLVAAARF
APHLEKCMGM GRISSRIASR RLATKEGATS AHLHSSGNTG GTDDEDDVDW SSDKRRKKSN
QNSRNNGSKK NNGKTF
