Reviewed, UniProtKB/Swiss-Prot Q9VH48 (CARM1_DROME)

Names and origin

Protein names

Recommended name:
    Probable histone-arginine methyltransferase CARMER
    EC=2.1.1.125
    EC=2.1.1.-
Alternative name(s):
    Protein arginine N-methyltransferase 4
      Short name=DART4
    Coactivator arginine methyltransferase for EcR/Usp

Gene names

Name:	Art4
Synonyms:	Carmer
ORF Names:	CG5358

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 at 'Arg-17' and activate transcription via chromatin remodeling. Coordinates ecdysone-mediated expression of cell death genes. Ref.4 Ref.5
Catalytic activity	S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine.
Subunit structure	Homodimer By similarity. Interacts with EcR.
Subcellular location	Cytoplasm. Nucleus. Ref.4 Ref.6
Tissue specificity	Present ubiquitously (at protein level). Expressed in the imaginal disks and in larval brains, and to a much lesser degree in the polytene larval tissue such as salivary glands. Ref.4 Ref.6
Developmental stage	Expression is high in early embryos, reduced in late embryonic and larval stages, up-regulated at the early prepupal stage and then reduced until the adult stage where it is again up-regulated. Ref.5
Post-translational modification	The dimethylated protein is the major form By similarity.
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Methylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histone methylation Ref.4 Ref.5 Inferred from direct assay. Source: FlyBase induction of programmed cell death by ecdysone Ref.5 Inferred from mutant phenotype. Source: FlyBase peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Ref.4 Inferred from direct assay. Source: FlyBase regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.6 Inferred from direct assay. Source: UniProtKB histone methyltransferase complex Ref.5 Inferred from direct assay. Source: FlyBase
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct protein-arginine omega-N asymmetric methyltransferase activity Ref.4 Inferred from direct assay. Source: FlyBase protein-arginine omega-N monomethyltransferase activity Ref.4 Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9VV94	1	EBI-128534,EBI-152906
Ldlr	Q9VER6	1	EBI-128534,EBI-170453
snRNP-U1	Q9VE17	1	EBI-128534,EBI-156295
sty	O44783	1	EBI-128534,EBI-132097

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 530	530	Probable histone-arginine methyltransferase CARMER		PRO_0000249253
Sites
	Binding site	154	1	S-adenosyl-L-methionine By similarity
	Binding site	163	1	S-adenosyl-L-methionine By similarity
	Binding site	187	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	209	1	S-adenosyl-L-methionine By similarity
	Binding site	238	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	501	1	Asymmetric dimethylarginine; by autocatalysis By similarity
Experimental info
	Sequence conflict	121	1	E → G in AAO45207. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9VH48-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 61590959D6B91EEA	FASTA	530	59,728
	10 20 30 40 50 60 MSSLRPEEAR KLATAASVSP LSNCQFCGVV ISSIADEQKL EFTNKYKGSC TLLCSYDSQG 70 80 90 100 110 120 VVLRVVSDDD RSHVLKEYMI AADTDAAQMG RRSYAVSLDA DNLVLRFASE QDQQLFRKVV 130 140 150 160 170 180 ENVKHLRPKS VFSQRTEESS ASQYFQFYGY LSQQQNMMQD YVRTSTYQRA ILGNAVDFQD 190 200 210 220 230 240 KIVLDVGAGS GILSFFAVQA GAAKVYAIEA SNMAQYAQQL VESNNVQHKI SVIPGKIEEI 250 260 270 280 290 300 ELPEKVDVII SEPMGYMLYN ERMLETYLHA RKWLKPQGKM YPTHGDLHIA PFSDESLYSE 310 320 330 340 350 360 QYNKANFWYQ SAFHGVDLTT LHKEGMKEYF RQPIVDTFDI RICMAKSVRH VCDFLNDKED 370 380 390 400 410 420 DLHLISIPLE FHILQTGICH GLAFWFDVEF SGSSQNVWLS TSPTAPLTHW YQVRCLLPMP 430 440 450 460 470 480 IFIKQGQTLT GRVLLEANRR QSYDVTIDLH IEGTLISSSN TLDLKNPYFR YTGAPVQAPP 490 500 510 520 530 GTSTQSPSEQ YWTQVDTQGS RNSSSMLNGG ISVNGIGEGM DITHGLMHPH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4." Boulanger M.-C., Miranda T.B., Clarke S., Di Fruscio M., Suter B., Lasko P., Richard S. Biochem. J. 379:283-289(2004) [PubMed: 14705965] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[5]	"An arginine-histone methyltransferase, CARMER, coordinates ecdysone-mediated apoptosis in Drosophila cells." Cakouros D., Daish T.J., Mills K., Kumar S. J. Biol. Chem. 279:18467-18471(2004) [PubMed: 14976192] [Abstract] Cited for: FUNCTION, INTERACTION WITH ECR, DEVELOPMENTAL STAGE.
[6]	"Tissue-dependent subcellular localization of Drosophila arginine methyl-transferase 4 (DART4), a coactivator whose overexpression affects neither viability nor differentiation." Urwyler O., Zhang L., Li X., Imboden H., Suter B. Differentiation 75:757-765(2007) [PubMed: 17459088] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF54471.1. BT004851 mRNA. Translation: AAO45207.1.
RefSeq	NP_649963.1.
UniGene	Dm.17037
3D structure databases
HSSP	HSSP built from PDB template 1OR8 based on UniProtKB Q63009.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VH48. 13 interactions.
STRING	Q9VH48.
Proteomic databases
PRIDE	Q9VH48.
Genome annotation databases
Ensembl	FBtr0082150; FBpp0081628; FBgn0037770; Drosophila melanogaster. [Genome view]
GeneID	41219.
KEGG	dme:Dmel_CG5358.
NMPDR	fig|7227.3.peg.11995.
Organism-specific databases
CTD	41219.
FlyBase	FBgn0037770. Art4.
Phylogenomic databases
OMA	VFSQRTE.
Enzyme and pathway databases
BRENDA	2.1.1.125. 48.
Gene expression databases
ArrayExpress	Q9VH48.
Bgee	Q9VH48.
GermOnline	CG5358. Drosophila melanogaster.
Family and domain databases
InterPro	IPR013217. Methyltransf_12. [Graphical view]
Pfam	PF08242. Methyltransf_12. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	822787.

Entry information

Entry name

CARM1_DROME

Accession

Primary (citable) accession number: Q9VH48
Secondary accession number(s): Q86NL6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project