MSL1_DROME
ID MSL1_DROME Reviewed; 1039 AA.
AC P50535; Q3ZAP1; Q9VJ66;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein male-specific lethal-1;
GN Name=msl-1; ORFNames=CG10385;
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].
RX PubMed=7781064; DOI=10.1016/0092-8674(95)90007-1;
RA Kelley R.L., Solovyeva I., Lyman L.M., Richman R., Solovyev V.,
RA Kuroda M.I.;
RT "Expression of msl-2 causes assembly of dosage compensation regulators on
RT the X chromosomes and female lethality in Drosophila.";
RL Cell 81:867-877(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-1039.
RC STRAIN=Canton-S;
RX PubMed=8325488; DOI=10.1093/genetics/134.2.545;
RA Palmer M.J., Mergner V.A., Richman R., Manning J.E., Kuroda M.I.,
RA Lucchesi J.C.;
RT "The male-specific lethal-one (msl-1) gene of Drosophila melanogaster
RT encodes a novel protein that associates with the X chromosome in males.";
RL Genetics 134:545-557(1993).
RN [6]
RP INTERACTION WITH TAMO.
RX PubMed=12653959; DOI=10.1046/j.1365-2443.2002.00634.x;
RA Minakhina S., Yang J., Steward R.;
RT "Tamo selectively modulates nuclear import in Drosophila.";
RL Genes Cells 8:299-310(2003).
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).
RN [8]
RP FUNCTION IN E3 UBIQUITIN LIGASE COMPLEX.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase
RT for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.";
RL Mol. Cell 43:132-144(2011).
CC -!- FUNCTION: The Msl proteins are essential for elevating transcription of
CC the single X chromosome in the male (X chromosome dosage compensation).
CC Msl-1 is a pioneer protein. Mle, msl-1 and msl-3 are colocalized on the
CC X chromosome. Each of the MSL proteins requires all the other MSLs for
CC wild-type X-chromosome binding. In complex with msl-2, promotes
CC ubiquitination of histone H2B. {ECO:0000269|PubMed:21726816}.
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 (PubMed:16543150). Interacts with tamo via the nuclear
CC localization signal (PubMed:12653959). {ECO:0000269|PubMed:12653959,
CC ECO:0000269|PubMed:16543150}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome
CC {ECO:0000269|PubMed:16543150}. Note=Msl-1 is associated with hundreds
CC of discrete sites along the length of the X chromosome in males and not
CC in females, and is also associated with 10-20 autosomal sites in males.
CC -!- SIMILARITY: Belongs to the msl-1 family. {ECO:0000305}.
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DR EMBL; L42514; AAA98918.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53689.1; -; Genomic_DNA.
DR EMBL; BT023828; AAZ86749.1; -; mRNA.
DR PIR; S52959; S52959.
DR RefSeq; NP_001286054.1; NM_001299125.1.
DR RefSeq; NP_476896.1; NM_057548.4.
DR AlphaFoldDB; P50535; -.
DR SMR; P50535; -.
DR BioGRID; 61115; 22.
DR DIP; DIP-18144N; -.
DR IntAct; P50535; 5.
DR STRING; 7227.FBpp0080674; -.
DR PaxDb; P50535; -.
DR PRIDE; P50535; -.
DR DNASU; 35121; -.
DR EnsemblMetazoa; FBtr0081130; FBpp0080674; FBgn0005617.
DR EnsemblMetazoa; FBtr0343118; FBpp0309817; FBgn0005617.
DR GeneID; 35121; -.
DR KEGG; dme:Dmel_CG10385; -.
DR CTD; 35121; -.
DR FlyBase; FBgn0005617; msl-1.
DR VEuPathDB; VectorBase:FBgn0005617; -.
DR eggNOG; ENOG502QQ0S; Eukaryota.
DR HOGENOM; CLU_002440_0_0_1; -.
DR InParanoid; P50535; -.
DR OMA; EFHCDNE; -.
DR OrthoDB; 322134at2759; -.
DR PhylomeDB; P50535; -.
DR BioGRID-ORCS; 35121; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35121; -.
DR PRO; PR:P50535; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0005617; Expressed in ovary and 30 other tissues.
DR ExpressionAtlas; P50535; baseline and differential.
DR Genevisible; P50535; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0046536; C:dosage compensation complex; IDA:FlyBase.
DR GO; GO:0072487; C:MSL complex; IDA:FlyBase.
DR GO; GO:0000228; C:nuclear 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:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase 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; NAS:FlyBase.
DR GO; GO:0043984; P:histone H4-K16 acetylation; IBA:GO_Central.
DR InterPro; IPR026711; Msl-1.
DR InterPro; IPR029332; PEHE_dom.
DR PANTHER; PTHR21656; PTHR21656; 1.
DR Pfam; PF15275; PEHE; 1.
DR SMART; SM01300; PEHE; 1.
PE 1: Evidence at protein level;
KW Chromosome; Nucleus; Reference proteome.
FT CHAIN 1..1039
FT /note="Protein male-specific lethal-1"
FT /id="PRO_0000096597"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1032..1037
FT /note="Nuclear localization signal"
FT COMPBIAS 366..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 26
FT /note="R -> G (in Ref. 1; AAA98918)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="S -> L (in Ref. 1; AAA98918)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="M -> I (in Ref. 1; AAA98918)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1039 AA; 117503 MW; 644C21C0390A2750 CRC64;
MDKRFKWPPK KRANYLESPY PHIPSRGRQR NLHGHPNQTQ HLHQHPGKIY ERQQYGNGRG
GHGGGNNNYR KLLHSLPAEH GGGAMAPPSS GGTVCAGADM VKLISENNNL RRMVMLNLNL
MQEQTDSIAA KDKELDDQSA KMSVVKAQNE ELKQAVAQLE AANQELCKQL RRKNQRRNDN
DDDDDDPPLP PAAPQQKLIR CHAETQTVFR EREQGTQTID AQPQFANALP RGINMKESPA
LDHHAGAVTN QPASKRSESK GRGEFNGKKV STFILQRMNQ DFEHHIHEQT EVAEEHEMEA
HKEQISQEED QLVAEEDHLH MQEVHTEEVV GGDIFHDALE SIEMEVVTEE LVDMEEHGQS
VDANGHIEED DDEDDEDDEN SDKDDDSEED DYPWMHSDAD VNARTEEELW QNQNYLLELD
PTEEKTCAPS AHSTPNHQQK SSTQAEIRKE GNQNRITEKL LQLKPEPMVD ALEAPILPKW
VAFKKKDKEH ESVPESPEVP KQQPHQEDAI VDHNAIKNQL EVPKPDLKPK DQPKDEQRQD
GQLDVRVEPQ EDVRKVQKET LKRQPEDAPK HLPKAVAPKV TKTSSRESTL PKANTADIKD
APAQKVIANH QSTKTQTDPV KTQRLQVKIR QYEMHPDMRT GSSAPSDIRK QKNVDPVSTP
ETKTIKSKSM LVNDKKTTSE TSQSPDQEID VETVRRKLAE HLKKELLSQS HSSQVTLKKI
RERVATNLIY PPPSAPVSST TITPAPTPST TPTPGSTPQH AVTSSMDQEI SAAKSKSKAA
EQIATPLTPQ SNSSVSSTTS TIRKTLNNCS PHTYSKATAR SGKLQSRFRT ATFPYSTRTW
EDQEFHCDNE FFLEEADELL ADNPSLEIPK WRDVPVPPSS DKIDTELLSD ATFERRHQKY
VKDEVDRKCR DARYMKEQIR LEQLRMRRNQ DEVLVALDPL RASTFYPLPE DIEAIQFVNE
VTVQAFGENV VNMEARDDFG VPWVDAIEAP TSIARSKALA EPVATLASKK IPTTAAEARH
QENHSSYVFP KRRKRQKNR
