CARM1_DROME
ID CARM1_DROME Reviewed; 530 AA.
AC Q9VH48; Q86NL6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Probable histone-arginine methyltransferase CARMER;
DE EC=2.1.1.319 {ECO:0000250|UniProtKB:Q7Q2B7};
DE AltName: Full=Coactivator arginine methyltransferase for EcR/Usp;
DE AltName: Full=Protein arginine N-methyltransferase 4;
DE Short=DART4;
GN Name=Art4; Synonyms=Carmer; ORFNames=CG5358;
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; 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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14705965; DOI=10.1042/bj20031176;
RA Boulanger M.-C., Miranda T.B., Clarke S., Di Fruscio M., Suter B.,
RA Lasko P., Richard S.;
RT "Characterization of the Drosophila protein arginine methyltransferases
RT DART1 and DART4.";
RL Biochem. J. 379:283-289(2004).
RN [5]
RP FUNCTION, INTERACTION WITH ECR, AND DEVELOPMENTAL STAGE.
RX PubMed=14976192; DOI=10.1074/jbc.m400972200;
RA Cakouros D., Daish T.J., Mills K., Kumar S.;
RT "An arginine-histone methyltransferase, CARMER, coordinates ecdysone-
RT mediated apoptosis in Drosophila cells.";
RL J. Biol. Chem. 279:18467-18471(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17459088; DOI=10.1111/j.1432-0436.2007.00175.x;
RA Urwyler O., Zhang L., Li X., Imboden H., Suter B.;
RT "Tissue-dependent subcellular localization of Drosophila arginine methyl-
RT transferase 4 (DART4), a coactivator whose overexpression affects neither
RT viability nor differentiation.";
RL Differentiation 75:757-765(2007).
CC -!- FUNCTION: Methylates (mono- and asymmetric dimethylation) the guanidino
CC nitrogens of arginyl residues in proteins. May methylate histone H3 at
CC 'Arg-17' and activate transcription via chromatin remodeling.
CC Coordinates ecdysone-mediated expression of cell death genes.
CC {ECO:0000269|PubMed:14705965, ECO:0000269|PubMed:14976192}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000250|UniProtKB:Q7Q2B7};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with EcR. {ECO:0000250,
CC ECO:0000269|PubMed:14976192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Present ubiquitously (at protein level). Expressed
CC in the imaginal disks and in larval brains, and to a much lesser degree
CC in the polytene larval tissue such as salivary glands.
CC {ECO:0000269|PubMed:14705965, ECO:0000269|PubMed:17459088}.
CC -!- DEVELOPMENTAL STAGE: Expression is high in early embryos, reduced in
CC late embryonic and larval stages, up-regulated at the early prepupal
CC stage and then reduced until the adult stage where it is again up-
CC regulated. {ECO:0000269|PubMed:14976192}.
CC -!- PTM: The dimethylated protein is the major form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; AE014297; AAF54471.1; -; Genomic_DNA.
DR EMBL; BT004851; AAO45207.1; -; mRNA.
DR RefSeq; NP_001262445.1; NM_001275516.1.
DR RefSeq; NP_649963.1; NM_141706.3.
DR AlphaFoldDB; Q9VH48; -.
DR SMR; Q9VH48; -.
DR BioGRID; 66376; 29.
DR IntAct; Q9VH48; 5.
DR STRING; 7227.FBpp0305840; -.
DR PaxDb; Q9VH48; -.
DR PRIDE; Q9VH48; -.
DR DNASU; 41219; -.
DR EnsemblMetazoa; FBtr0082150; FBpp0081628; FBgn0037770.
DR EnsemblMetazoa; FBtr0333687; FBpp0305840; FBgn0037770.
DR GeneID; 41219; -.
DR KEGG; dme:Dmel_CG5358; -.
DR CTD; 420; -.
DR FlyBase; FBgn0037770; Art4.
DR VEuPathDB; VectorBase:FBgn0037770; -.
DR eggNOG; KOG1500; Eukaryota.
DR GeneTree; ENSGT00940000169584; -.
DR HOGENOM; CLU_017375_0_1_1; -.
DR InParanoid; Q9VH48; -.
DR OMA; KWLKPQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q9VH48; -.
DR Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR SignaLink; Q9VH48; -.
DR BioGRID-ORCS; 41219; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41219; -.
DR PRO; PR:Q9VH48; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037770; Expressed in wing disc and 39 other tissues.
DR ExpressionAtlas; Q9VH48; baseline and differential.
DR Genevisible; Q9VH48; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:FlyBase.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:FlyBase.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:FlyBase.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034969; P:histone arginine methylation; IMP:FlyBase.
DR GO; GO:0016571; P:histone methylation; IDA:FlyBase.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:FlyBase.
DR GO; GO:0120142; P:positive regulation of ecdysone receptor-mediated signaling pathway; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Methylation; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..530
FT /note="Probable histone-arginine methyltransferase CARMER"
FT /id="PRO_0000249253"
FT DOMAIN 141..450
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 501
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 121
FT /note="E -> G (in Ref. 3; AAO45207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 59728 MW; 61590959D6B91EEA CRC64;
MSSLRPEEAR KLATAASVSP LSNCQFCGVV ISSIADEQKL EFTNKYKGSC TLLCSYDSQG
VVLRVVSDDD RSHVLKEYMI AADTDAAQMG RRSYAVSLDA DNLVLRFASE QDQQLFRKVV
ENVKHLRPKS VFSQRTEESS ASQYFQFYGY LSQQQNMMQD YVRTSTYQRA ILGNAVDFQD
KIVLDVGAGS GILSFFAVQA GAAKVYAIEA SNMAQYAQQL VESNNVQHKI SVIPGKIEEI
ELPEKVDVII SEPMGYMLYN ERMLETYLHA RKWLKPQGKM YPTHGDLHIA PFSDESLYSE
QYNKANFWYQ SAFHGVDLTT LHKEGMKEYF RQPIVDTFDI RICMAKSVRH VCDFLNDKED
DLHLISIPLE FHILQTGICH GLAFWFDVEF SGSSQNVWLS TSPTAPLTHW YQVRCLLPMP
IFIKQGQTLT GRVLLEANRR QSYDVTIDLH IEGTLISSSN TLDLKNPYFR YTGAPVQAPP
GTSTQSPSEQ YWTQVDTQGS RNSSSMLNGG ISVNGIGEGM DITHGLMHPH
