Q9VH48 (CARM1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable histone-arginine methyltransferase CARMER
EC=2.1.1.-
EC=2.1.1.125

Alternative name(s):
Coactivator arginine methyltransferase for EcR/Usp
Protein arginine N-methyltransferase 4
Short name=DART4

Gene names

Name:	Art4
Synonyms:	Carmer
ORF Names:	CG5358

Organism

Drosophila melanogaster (Fruit fly)

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.
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 + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
Subunit structure	Homodimer By similarity. Interacts with EcR. Ref.5
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 Reference proteome
Gene Ontology (GO)
Biological process	induction of programmed cell death by ecdysone Inferred from mutant phenotype Ref.5. Source: FlyBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay Ref.6. Source: UniProtKB histone methyltransferase complex Inferred from direct assay Ref.5. Source: FlyBase
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC protein-arginine omega-N asymmetric methyltransferase activity Inferred from direct assay Ref.4. Source: FlyBase protein-arginine omega-N monomethyltransferase activity Inferred from direct assay Ref.4. Source: FlyBase
Complete GO annotation...

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
	Binding site	266	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 [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. Strain: Berkeley.
[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
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF54471.1. BT004851 mRNA. Translation: AAO45207.1.
RefSeq	NP_649963.1. NM_141706.2.
UniGene	Dm.17037.
3D structure databases
HSSP	HSSP built from PDB template 1OR8 based on UniProtKB Q63009.
ProteinModelPortal	Q9VH48.
SMR	Q9VH48. Positions 130-472.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VH48. 5 interactions.
MINT	MINT-761779.
STRING	Q9VH48.
Proteomic databases
PRIDE	Q9VH48.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082150; FBpp0081628; FBgn0037770.
GeneID	41219.
KEGG	dme:Dmel_CG5358.
NMPDR	fig|7227.3.peg.11995.
Organism-specific databases
CTD	420.
FlyBase	FBgn0037770. Art4.
Phylogenomic databases
eggNOG	inNOG05828.
GeneTree	EMGT00050000007630.
InParanoid	Q9VH48.
OMA	CHGLAFW.
OrthoDB	EOG4XKSP3.
PhylomeDB	Q9VH48.
Gene expression databases
ArrayExpress	Q9VH48.
Bgee	Q9VH48.
GermOnline	CG5358. Drosophila melanogaster.
Family and domain databases
InterPro	IPR007857. Skb1_MeTrfase. [Graphical view]
KO	K05931.
Pfam	PF05185. PRMT5. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project