MSL3_DROME
ID MSL3_DROME Reviewed; 512 AA.
AC P50536; A8BP72; A8BP74; A8BP87; A8BP92; A8IL14; A8IL17; A8IL22; A8IL25;
AC A8IL30; A8IL33; A8IL37; A8IL41; A8IL46; Q8IQ74; Q9VS18;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein male-specific lethal-3;
GN Name=msl-3; ORFNames=CG8631;
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 [GENOMIC DNA], VARIANTS THR-184 AND GLY-352, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Larva;
RX PubMed=7768187; DOI=10.1242/dev.121.2.463;
RA Gorman M., Franke A., Baker B.S.;
RT "Molecular characterization of the male-specific lethal-3 gene and
RT investigations of the regulation of dosage compensation in Drosophila.";
RL Development 121:463-475(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-184; GLY-352 AND
RP VAL-503.
RC STRAIN=15, 3, 5, 7, Amherst, Congo13, Congo194, Congo216, and Congo346;
RX PubMed=17878295; DOI=10.1073/pnas.0707445104;
RA Rodriguez M.A., Vermaak D., Bayes J.J., Malik H.S.;
RT "Species-specific positive selection of the male-specific lethal complex
RT that participates in dosage compensation in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15412-15417(2007).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-509, AND VARIANTS THR-184;
RP MET-220; ALA-232; ASN-265; LYS-310; GLY-325; GLY-352; HIS-405; CYS-412;
RP SER-430 AND PRO-465.
RC STRAIN=399A, 591A, 639A, 732A, 774A, 799A, 820A, 852A, and 859A;
RX PubMed=18039888; DOI=10.1534/genetics.107.079459;
RA Levine M.T., Holloway A.K., Arshad U., Begun D.J.;
RT "Pervasive and largely lineage-specific adaptive protein evolution in the
RT dosage compensation complex of Drosophila melanogaster.";
RL Genetics 177:1959-1962(2007).
RN [7]
RP IDENTIFICATION IN THE MSL COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=16543150; DOI=10.1016/j.molcel.2006.02.007;
RA Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M.,
RA Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M.,
RA Stunnenberg H.G., Saumweber H., Akhtar A.;
RT "Nuclear pore components are involved in the transcriptional regulation of
RT dosage compensation in Drosophila.";
RL Mol. Cell 21:811-823(2006).
CC -!- FUNCTION: The MSL proteins are essential for elevating transcription of
CC the single X chromosome in the male (X chromosome dosage compensation).
CC Mle, msl-1 and msl-3 are colocalized on the X chromosome. Each of the
CC MSL proteins requires all the other MSLs for wild-type X-chromosome
CC binding. {ECO:0000269|PubMed:7768187}.
CC -!- SUBUNIT: Component of the male-specific lethal (MSL) histone
CC acetyltransferase complex at least composed of mof, msl-1, msl-2 and
CC msl-3. {ECO:0000269|PubMed:16543150}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972,
CC ECO:0000269|PubMed:7768187}. Chromosome {ECO:0000269|PubMed:16543150,
CC ECO:0000269|PubMed:7768187}. Note=Msl-3 is associated with hundreds of
CC discrete sites along the length of the X chromosome in males and not in
CC females, and is also associated with 10-20 autosomal sites in males.
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DR EMBL; X81321; CAA57101.1; -; Genomic_DNA.
DR EMBL; EF653847; ABV49039.1; -; Genomic_DNA.
DR EMBL; EF653848; ABV49040.1; -; Genomic_DNA.
DR EMBL; EF653849; ABV49041.1; -; Genomic_DNA.
DR EMBL; EF653850; ABV49042.1; -; Genomic_DNA.
DR EMBL; EF653851; ABV49043.1; -; Genomic_DNA.
DR EMBL; EF653852; ABV49044.1; -; Genomic_DNA.
DR EMBL; EF653853; ABV49045.1; -; Genomic_DNA.
DR EMBL; EF653854; ABV49046.1; -; Genomic_DNA.
DR EMBL; EF653855; ABV49047.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50612.1; -; Genomic_DNA.
DR EMBL; AY071074; AAL48696.1; -; mRNA.
DR EMBL; EU167107; ABV82500.1; -; Genomic_DNA.
DR EMBL; EU167108; ABV82501.1; -; Genomic_DNA.
DR EMBL; EU167109; ABV82502.1; -; Genomic_DNA.
DR EMBL; EU167110; ABV82503.1; -; Genomic_DNA.
DR EMBL; EU167112; ABV82504.1; -; Genomic_DNA.
DR EMBL; EU167113; ABV82505.1; -; Genomic_DNA.
DR EMBL; EU167114; ABV82506.1; -; Genomic_DNA.
DR EMBL; EU167115; ABV82507.1; -; Genomic_DNA.
DR EMBL; EU167116; ABV82508.1; -; Genomic_DNA.
DR PIR; S48828; S48828.
DR RefSeq; NP_523951.1; NM_079227.3.
DR PDB; 3M9Q; X-ray; 1.29 A; A/B=1-92.
DR PDBsum; 3M9Q; -.
DR AlphaFoldDB; P50536; -.
DR SMR; P50536; -.
DR BioGRID; 64224; 35.
DR DIP; DIP-23734N; -.
DR IntAct; P50536; 15.
DR STRING; 7227.FBpp0076635; -.
DR PaxDb; P50536; -.
DR ABCD; P50536; 3 sequenced antibodies.
DR DNASU; 38779; -.
DR EnsemblMetazoa; FBtr0076926; FBpp0076635; FBgn0002775.
DR GeneID; 38779; -.
DR KEGG; dme:Dmel_CG8631; -.
DR CTD; 38779; -.
DR FlyBase; FBgn0002775; msl-3.
DR VEuPathDB; VectorBase:FBgn0002775; -.
DR eggNOG; KOG3001; Eukaryota.
DR GeneTree; ENSGT00950000182965; -.
DR HOGENOM; CLU_039566_5_2_1; -.
DR InParanoid; P50536; -.
DR OMA; PPEKSMV; -.
DR OrthoDB; 1624495at2759; -.
DR PhylomeDB; P50536; -.
DR SignaLink; P50536; -.
DR BioGRID-ORCS; 38779; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; P50536; -.
DR GenomeRNAi; 38779; -.
DR PRO; PR:P50536; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0002775; Expressed in cleaving embryo and 20 other tissues.
DR ExpressionAtlas; P50536; baseline and differential.
DR Genevisible; P50536; DM.
DR GO; GO:0010369; C:chromocenter; IDA:FlyBase.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0072487; C:MSL complex; IDA:FlyBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000228; C:nuclear chromosome; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0000805; C:X chromosome; IDA:FlyBase.
DR GO; GO:0016456; C:X chromosome located dosage compensation complex, transcription activating; NAS:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0035064; F:methylated histone binding; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IPI:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0007549; P:dosage compensation; IMP:FlyBase.
DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; TAS:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IBA:GO_Central.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR Pfam; PF05712; MRG; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS51640; MRG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..512
FT /note="Protein male-specific lethal-3"
FT /id="PRO_0000080245"
FT DOMAIN 11..90
FT /note="Chromo"
FT DOMAIN 196..500
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 98..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 184
FT /note="A -> T (in strain: 399A, 774A, 852A, 859A, Congo13,
FT Congo194 and Congo346)"
FT /evidence="ECO:0000269|PubMed:17878295,
FT ECO:0000269|PubMed:18039888, ECO:0000269|PubMed:7768187"
FT VARIANT 220
FT /note="K -> M (in strain: 799A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 232
FT /note="V -> A (in strain: 399A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 265
FT /note="S -> N (in strain: 859A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 310
FT /note="E -> K (in strain: 820A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 325
FT /note="S -> G (in strain: 639A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 352
FT /note="V -> G (in strain: 5, 7, 399A, 591A, 799A, 852A,
FT 859A, Amherst, Congo13, Congo194, Congo216 and Congo346)"
FT /evidence="ECO:0000269|PubMed:17878295,
FT ECO:0000269|PubMed:18039888, ECO:0000269|PubMed:7768187"
FT VARIANT 405
FT /note="Y -> H (in strain: 639A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 412
FT /note="R -> C (in strain: 732A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 430
FT /note="P -> S (in strain: 639A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 465
FT /note="L -> P (in strain: 820A)"
FT /evidence="ECO:0000269|PubMed:18039888"
FT VARIANT 503
FT /note="L -> V (in strain: Congo194)"
FT /evidence="ECO:0000269|PubMed:17878295"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3M9Q"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:3M9Q"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:3M9Q"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3M9Q"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3M9Q"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3M9Q"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3M9Q"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:3M9Q"
SQ SEQUENCE 512 AA; 58853 MW; 3101BC92B2339991 CRC64;
MTELRDETPL FHKGEIVLCY EPDKSKARVL YTSKVLNVFE RRNEHGLRFY EYKIHFQGWR
PSYDRCVRAT VLLKDTEENR QLQRELAEAA KLQIRGDYSY KGTPDKPSAK KKRGGKAAHV
EEPIVVPMDT GHLEAEHEMA PTPRAAGNRT RDNSGGKRKE KPPSGDGRLK GNRGRQTETF
YNNAINDVSV YNHVPQEDRI MMRVSERLRE LIEYDRNMIK VLGKQHALPA RVPIVTIMEN
FVKQQAVELA ISIKQDSSRA RNTQSRNARM EREYDRVMST VCMLKEVVDG LRIYFEFHVD
DHLLYTEEKE YVHNYLTDDN MRNCSLILNK SYEYINPSGD TELIGLDGTP VVEGSGDTNG
QIGVINIGGP EYEKQLQKCL LYIVTASGKN TAQAYERTSP YTAAYKLPVE MRGFLNETFK
WRLLSAESPP EKSMVFGAPH LVRLMIKMPM FLNASPISNK KLEDLLPHLD AFINYLENHR
EWFDRENFVN STALPQEDLQ RELLDSLDGI AA
