RMT2_YEAST
ID RMT2_YEAST Reviewed; 412 AA.
AC Q03305; D6VT90;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein arginine N-methyltransferase 2 {ECO:0000303|PubMed:9873020};
DE EC=2.1.1.- {ECO:0000269|PubMed:11856739, ECO:0000269|PubMed:9873020};
DE AltName: Full=Protein-arginine N5-methyltransferase {ECO:0000305|PubMed:9873020};
DE AltName: Full=Type IV protein arginine N-methyltransferase {ECO:0000303|PubMed:17448464};
DE Short=Type IV PRMT {ECO:0000305|PubMed:17448464};
GN Name=RMT2 {ECO:0000303|PubMed:9873020};
GN OrderedLocusNames=YDR465C {ECO:0000312|SGD:S000002873};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9873020; DOI=10.1074/jbc.274.2.814;
RA Niewmierzycka A., Clarke S.;
RT "S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae.
RT Identification of a novel protein arginine methyltransferase.";
RL J. Biol. Chem. 274:814-824(1999).
RN [4]
RP FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND CATALYTIC ACTIVITY.
RX PubMed=11856739; DOI=10.1074/jbc.m111379200;
RA Chern M.-K., Chang K.-N., Liu L.-F., Tam T.-C.S., Liu Y.-C., Liang Y.-L.,
RA Tam M.F.;
RT "Yeast ribosomal protein L12 is a substrate of protein-arginine
RT methyltransferase 2.";
RL J. Biol. Chem. 277:15345-15353(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NUP49; NUP57 AND NUP100.
RX PubMed=17448464; DOI=10.1016/j.yexcr.2007.03.007;
RA Olsson I., Berrez J.M., Leipus A., Ostlund C., Mutvei A.;
RT "The arginine methyltransferase Rmt2 is enriched in the nucleus and co-
RT purifies with the nuclear porins Nup49, Nup57 and Nup100.";
RL Exp. Cell Res. 313:1778-1789(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that methylates the delta-nitrogen atom of arginine
CC residues to form N5-methylarginine (type IV) in target proteins
CC (PubMed:9873020). Monomethylates ribosomal protein L12 (RPL12A/RPL12B)
CC at 'Arg-67' (PubMed:11856739). {ECO:0000269|PubMed:11856739,
CC ECO:0000269|PubMed:9873020}.
CC -!- SUBUNIT: Monomer. Interacts with nucleoporins NUP49, NUP57 and NUP100.
CC {ECO:0000269|PubMed:11856739, ECO:0000269|PubMed:17448464}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:17448464}. Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:17448464}. Note=Appears often very close to the
CC nuclear membrane and the nuclear pores. {ECO:0000269|PubMed:17448464}.
CC -!- MASS SPECTROMETRY: Mass=47339; Mass_error=2; Method=Electrospray;
CC Note=Measured from a recombinant protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:11856739};
CC -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RMT2 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00892}.
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; U33050; AAB64933.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12300.1; -; Genomic_DNA.
DR PIR; S69633; S69633.
DR RefSeq; NP_010753.1; NM_001180773.1.
DR AlphaFoldDB; Q03305; -.
DR SMR; Q03305; -.
DR BioGRID; 32519; 54.
DR DIP; DIP-4490N; -.
DR IntAct; Q03305; 7.
DR STRING; 4932.YDR465C; -.
DR iPTMnet; Q03305; -.
DR MaxQB; Q03305; -.
DR PaxDb; Q03305; -.
DR PRIDE; Q03305; -.
DR EnsemblFungi; YDR465C_mRNA; YDR465C; YDR465C.
DR GeneID; 852076; -.
DR KEGG; sce:YDR465C; -.
DR SGD; S000002873; RMT2.
DR VEuPathDB; FungiDB:YDR465C; -.
DR eggNOG; KOG1709; Eukaryota.
DR HOGENOM; CLU_033831_0_0_1; -.
DR InParanoid; Q03305; -.
DR OMA; YWVVDNY; -.
DR BioCyc; MetaCyc:G3O-29993-MON; -.
DR BioCyc; YEAST:G3O-29993-MON; -.
DR BRENDA; 2.1.1.322; 984.
DR Reactome; R-SCE-71288; Creatine metabolism.
DR PRO; PR:Q03305; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03305; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019702; F:protein-arginine N5-methyltransferase activity; IDA:SGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR017408; Arginine_N-MeTrfase_2.
DR InterPro; IPR026480; RMT2_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF038148; Arginine_N-mtfrase-2; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51559; SAM_RMT2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..412
FT /note="Protein arginine N-methyltransferase 2"
FT /id="PRO_0000228980"
FT DOMAIN 189..412
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 48..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 250..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 271..273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 298..299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 412 AA; 47469 MW; 932B52EE4C4FFCF3 CRC64;
MSELHALLTF PERPISQSYY VPKLQHFLKS GIPATYTLEQ VAAFEHEEKN RNGDKEFRES
TDDNKTSNTT PLHVLARSLP LDIKDEELQV VMDMMNILFE YGAGWNFIDY EDKTVGDLFL
ERNQSRESPL YRRLVEAGVS AELLLRKLNG GDVEFLDTDE LIGIEPEESV QTAVDGQKEE
SVGSDDDATA ANQQVYLKTE LEYKDDALIT KENKDGVMMD WETKIMELAS ETLFPDPEAT
NSATILNIGF GMGIIDTFIQ ARKPYRHYIC EAHPDVLAKM KMDGWYEKDN VVILEGRWQD
TLNNLLDKGE VFFDGIYYDT FSEHYQDILD LYDVVVGLIK PEGVFSFFNG LGADRSLCYD
VYKEIVEIDV ATYGMKCDYT RYSLDEQLPD WNDVKRSYFN CNYYYHPRIT FA
