ANM5_DROME
ID ANM5_DROME Reviewed; 610 AA.
AC Q9U6Y9; O46117; Q8MKK9; Q9V7L8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein arginine N-methyltransferase 5;
DE EC=2.1.1.-;
DE AltName: Full=JBP1 homolog;
DE AltName: Full=Protein arginine N-methyltransferase capsuleen;
GN Name=csul; Synonyms=DART5; ORFNames=CG3730;
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 [MRNA] (ISOFORM 1).
RX PubMed=10531356; DOI=10.1074/jbc.274.44.31531;
RA Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.;
RT "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with
RT Jak kinases and contains protein methyltransferase activity.";
RL J. Biol. Chem. 274:31531-31542(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Anne J., Martin J.R., Merdes G., Raibaud A., Sather S., Ollo R.,
RA Mechler B.M.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RA Anne J., Mechler B.M.;
RT "Capsuleen, a 'grandchildless' gene, encodes a homologue of the human
RT HsSkb1/PRMT5 methyltransferase.";
RL (In) 43th Annual Drosophila Research Conference, pp.145A-145A, San Diego
RL (2002).
RN [7]
RP TISSUE SPECIFICITY.
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 [8]
RP INTERACTION WITH VLS.
RX PubMed=15800004; DOI=10.1242/dev.01809;
RA Anne J., Mechler B.M.;
RT "Valois, a component of the nuage and pole plasm, is involved in assembly
RT of these structures, and binds to Tudor and the methyltransferase
RT Capsuleen.";
RL Development 132:2167-2177(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18369183; DOI=10.1261/rna.940708;
RA Gonsalvez G.B., Praveen K., Hicks A.J., Tian L., Matera A.G.;
RT "Sm protein methylation is dispensable for snRNP assembly in Drosophila
RT melanogaster.";
RL RNA 14:878-887(2008).
RN [10]
RP FUNCTION.
RX PubMed=19377467; DOI=10.1038/ncb1872;
RA Kirino Y., Kim N., de Planell-Saguer M., Khandros E., Chiorean S.,
RA Klein P.S., Rigoutsos I., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for
RT Ago3 and Aub stability.";
RL Nat. Cell Biol. 11:652-658(2009).
RN [11]
RP FUNCTION.
RX PubMed=19926723; DOI=10.1261/rna.1869710;
RA Kirino Y., Vourekas A., Sayed N., de Lima Alves F., Thomson T., Lasko P.,
RA Rappsilber J., Jongens T.A., Mourelatos Z.;
RT "Arginine methylation of Aubergine mediates Tudor binding and germ plasm
RT localization.";
RL RNA 16:70-78(2010).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA) (By similarity). Specifically mediates the
CC symmetrical dimethylation of arginine residues in the small nuclear
CC ribonucleoproteins SmD1 and SmD3. Required for arginine symmetrical
CC dimethylation of piwi family proteins, piwi, aub and AGO3, during
CC germline development. Required during oogenesis for pole cell formation
CC in the pathway controlled by oskar (osk) and for abdominal segments
CC during early embryogenesis. Involved in nanos (nos) and germ cell mRNAs
CC localization. {ECO:0000250, ECO:0000269|PubMed:18369183,
CC ECO:0000269|PubMed:19377467, ECO:0000269|PubMed:19926723,
CC ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Interacts with vls. {ECO:0000269|PubMed:15800004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q9U6Y9-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9U6Y9-2; Sequence=VSP_014035;
CC -!- TISSUE SPECIFICITY: Expressed only in ovaries.
CC {ECO:0000269|PubMed:14705965}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed from stage 3 egg chambers onward, becoming restricted to the
CC cortex of the oocytes at stage 10. Evenly distributed in preblastoderm
CC embryos. {ECO:0000269|Ref.6}.
CC -!- DISRUPTION PHENOTYPE: Flies are viable and do not display neuromuscular
CC dysfunctions. Strong synthetic lethal phenotype in the presence of a
CC hypomorphic Smn mutation. {ECO:0000269|PubMed:18369183}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF167574; AAF04504.1; -; mRNA.
DR EMBL; AJ002740; CAA05712.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58030.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68510.1; -; Genomic_DNA.
DR EMBL; AY122153; AAM52665.1; -; mRNA.
DR RefSeq; NP_477184.1; NM_057836.4. [Q9U6Y9-1]
DR RefSeq; NP_725552.1; NM_166158.2. [Q9U6Y9-2]
DR AlphaFoldDB; Q9U6Y9; -.
DR SMR; Q9U6Y9; -.
DR BioGRID; 62528; 3.
DR STRING; 7227.FBpp0088810; -.
DR PaxDb; Q9U6Y9; -.
DR PRIDE; Q9U6Y9; -.
DR DNASU; 36809; -.
DR EnsemblMetazoa; FBtr0089871; FBpp0088810; FBgn0015925. [Q9U6Y9-1]
DR EnsemblMetazoa; FBtr0089872; FBpp0088811; FBgn0015925. [Q9U6Y9-2]
DR GeneID; 36809; -.
DR KEGG; dme:Dmel_CG3730; -.
DR CTD; 36809; -.
DR FlyBase; FBgn0015925; csul.
DR VEuPathDB; VectorBase:FBgn0015925; -.
DR eggNOG; KOG0822; Eukaryota.
DR GeneTree; ENSGT00390000001141; -.
DR HOGENOM; CLU_010247_3_0_1; -.
DR InParanoid; Q9U6Y9; -.
DR OMA; KIDNTRC; -.
DR PhylomeDB; Q9U6Y9; -.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR BioGRID-ORCS; 36809; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36809; -.
DR PRO; PR:Q9U6Y9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0015925; Expressed in egg cell and 27 other tissues.
DR ExpressionAtlas; Q9U6Y9; baseline and differential.
DR Genevisible; Q9U6Y9; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008276; F:protein methyltransferase activity; IMP:FlyBase.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IMP:FlyBase.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; IBA:GO_Central.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0030719; P:P granule organization; IMP:FlyBase.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IMP:UniProtKB.
DR GO; GO:0035247; P:peptidyl-arginine omega-N-methylation; IEA:UniProt.
DR GO; GO:0007315; P:pole plasm assembly; IMP:FlyBase.
DR GO; GO:0007318; P:pole plasm protein localization; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PTHR10738; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Methyltransferase; Oogenesis; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..610
FT /note="Protein arginine N-methyltransferase 5"
FT /id="PRO_0000212340"
FT DOMAIN 284..587
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 470..610
FT /note="Interaction with vls"
FT ACT_SITE 412
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 421
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 309..310
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 396..397
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 421
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_note="substrate"
FT /ligand_part="L-arginine residue"
FT /ligand_part_id="ChEBI:CHEBI:29965"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT VAR_SEQ 126..130
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014035"
FT CONFLICT 39
FT /note="L -> M (in Ref. 2; CAA05712)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="D -> A (in Ref. 2; CAA05712)"
FT /evidence="ECO:0000305"
FT CONFLICT 350..355
FT /note="AVFNAA -> LFSMTS (in Ref. 2; CAA05712)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="S -> F (in Ref. 1; AAF04504)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..488
FT /note="EP -> K (in Ref. 2; CAA05712)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="F -> V (in Ref. 1; AAF04504)"
FT /evidence="ECO:0000305"
FT CONFLICT 501..502
FT /note="EN -> GD (in Ref. 1; AAF04504)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="R -> P (in Ref. 2; CAA05712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 69741 MW; 3531ACE5BEE9713E CRC64;
MNYYVCLHQE GVNSIPKLIE KAFANNYNVV STSINANMLP FEPHESDPTY PATILSGSDW
NSKVIFTMSD VNVDSPNDKL REHAKEVFMR DVAWAEHLQN VGNLMVRLRG PENENLASIV
LAKTKDDFPS GNWFIQVPIT NPELATFEHR KDATAEEVAE AESNDPWNWW NNLRMVTKHS
TKVKVVIELN DADRPSKETV RRWLGEPIEA IIIPSSLFVR NRSNYCVLKK EWQLIVGHFI
SVRANIIIST NPNDKALCQY ADYVNKLIND NCDKHMLNSY ENMLEIPLQP LCDNLDTYTY
EVFETDPVKY KLYQDAVQAA LLDRVSAAEA KTKLTVVMLL GGGRGPLARA VFNAAELTKR
KVRLYIIEKN PNAIRTLSNM VKTLWADKDV HIFSKDMRDF SPPELADIMV SELLGSFGDN
ELSPECLDGA LKLLKPDGIS IPYKSTSYIN PLMSAVLHQN VCQLLPTYPA FDYGYVSLLK
NIYHIDEPQA LFEFVHPNRA ENIDNTRCKT VSFKVNKDCV LHGIGGYFDT HLYKDICLSI
NPLTHTPGMF SWFPMFFATR PRTLREGQTI SIQFWRCVDA TKVWYEWQVV NSPDDWEHHN
TRGTGYNMRL
