DMAP1_DROME
ID DMAP1_DROME Reviewed; 433 AA.
AC Q7K3D8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=DNA methyltransferase 1-associated protein 1 {ECO:0000303|PubMed:24947515};
GN Name=DMAP1 {ECO:0000303|PubMed:24947515, ECO:0000312|FlyBase:FBgn0034537};
GN ORFNames=CG11132 {ECO:0000312|FlyBase:FBgn0034537};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL13878.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13878.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL13878.1};
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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH REL; AKIRIN AND BAP55, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24947515; DOI=10.1074/jbc.c114.553719;
RA Goto A., Fukuyama H., Imler J.L., Hoffmann J.A.;
RT "The chromatin regulator DMAP1 modulates activity of the nuclear factor B
RT (NF-B) transcription factor Relish in the Drosophila innate immune
RT response.";
RL J. Biol. Chem. 289:20470-20476(2014).
CC -!- FUNCTION: Involved in transcription repression and activation (By
CC similarity). Required for larvae and pupal development, and for normal
CC innate immune responses (PubMed:24947515). Involved in modulating the
CC activation of the immune deficiency pathway (Imd), acting either
CC downstream of, or at the level of, the NF-kappa-B factor Rel
CC (PubMed:24947515). Possibly functions with akirin to regulate Rel, and
CC its interaction with the Brahma complex protein Bap55 suggests that it
CC may regulate the IMD pathway at the level of chromatin remodeling
CC (PubMed:24947515). {ECO:0000250|UniProtKB:Q9NPF5,
CC ECO:0000269|PubMed:24947515}.
CC -!- SUBUNIT: Interacts with Rel. Interacts with akirin and Bap55.
CC {ECO:0000269|PubMed:24947515}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24947515}. Cytoplasm
CC {ECO:0000269|PubMed:24947515}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is larval or pupal
CC lethal. RNAi-mediated knockdown in adults results in reduced expression
CC of the antimicrobial peptide genes DptA and Dro in response to septic
CC injury with Gram-negative bacteria E.coli. Adults infected with the
CC Gram-positive bacteria M.luteus display increased expression of the
CC antimicrobial peptide gene Drs. {ECO:0000269|PubMed:24947515}.
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DR EMBL; AE013599; AAF57436.1; -; Genomic_DNA.
DR EMBL; AY058649; AAL13878.1; -; mRNA.
DR RefSeq; NP_611503.1; NM_137659.5.
DR AlphaFoldDB; Q7K3D8; -.
DR SMR; Q7K3D8; -.
DR IntAct; Q7K3D8; 5.
DR STRING; 7227.FBpp0085546; -.
DR PaxDb; Q7K3D8; -.
DR PRIDE; Q7K3D8; -.
DR DNASU; 37339; -.
DR EnsemblMetazoa; FBtr0086232; FBpp0085546; FBgn0034537.
DR GeneID; 37339; -.
DR KEGG; dme:Dmel_CG11132; -.
DR UCSC; CG11132-RA; d. melanogaster.
DR CTD; 55929; -.
DR FlyBase; FBgn0034537; DMAP1.
DR VEuPathDB; VectorBase:FBgn0034537; -.
DR eggNOG; KOG2656; Eukaryota.
DR GeneTree; ENSGT00390000016466; -.
DR HOGENOM; CLU_018539_1_1_1; -.
DR InParanoid; Q7K3D8; -.
DR OMA; NNINNWS; -.
DR OrthoDB; 918816at2759; -.
DR PhylomeDB; Q7K3D8; -.
DR SignaLink; Q7K3D8; -.
DR BioGRID-ORCS; 37339; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37339; -.
DR PRO; PR:Q7K3D8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034537; Expressed in egg cell and 20 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0043486; P:histone exchange; 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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:FlyBase.
DR InterPro; IPR032563; DAMP1_SANT-like.
DR InterPro; IPR008468; DMAP1.
DR InterPro; IPR027109; Swc4/Dmap1.
DR PANTHER; PTHR12855; PTHR12855; 1.
DR Pfam; PF05499; DMAP1; 1.
DR Pfam; PF16282; SANT_DAMP1_like; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Coiled coil; Cytoplasm; Immunity; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..433
FT /note="DNA methyltransferase 1-associated protein 1"
FT /id="PRO_0000439672"
FT DOMAIN 148..197
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..204
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:24947515"
FT REGION 252..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..281
FT /evidence="ECO:0000255"
FT COMPBIAS 252..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 50248 MW; CE624DD14E7F1125 CRC64;
MSADVRDILD MERANTPEVT RDSFLATKKR NFERTKTASR RPEGMHREVF ALLYTDKKDA
PPLLPTDTAL GIGAGYKETK ARLGMKKVRK WEWAPFSNPA RNDSAVFHHW KRVTDNSTDY
PFAKFNKQLE VPSYTMTEYN AHLRNNINNW SKVQTDHLFD LARRFDLRFI VMADRWNRQQ
HGTKTVEELK ERYYEVVALL AKAKNQTSEK KVFVYDVEHE RRRKEQLEKL FKRTTQQVEE
ENMLINEMKK IEARKKERER KTQDLQKLIS QADQQNEHAS NTPSTRKYEK KLHKKKVHQQ
PRPSRVDSVV NAIEIGSSGI KFADLRGSGV SLRSQRMKLP ANIGQRKVKA LEQAIQEFKV
DPAPPPTEDI CTSFNELRSD MVLLCELRTA LSTCVYEMES LKHQYEAACP GKTLNIPPSL
VPIKTEALDN STN
