ANM5_XENLA
ID ANM5_XENLA Reviewed; 633 AA.
AC Q6NUA1;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein arginine N-methyltransferase 5;
DE Short=prmt5;
DE EC=2.1.1.320 {ECO:0000269|PubMed:22009756};
DE AltName: Full=Histone synthetic lethal 7 protein;
DE Short=Hsl7;
DE AltName: Full=Histone-arginine N-methyltransferase PRMT5;
GN Name=prmt5; Synonyms=hsl7;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH WEE2-A, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15583029; DOI=10.1083/jcb.200406048;
RA Yamada A., Duffy B., Perry J.A., Kornbluth S.;
RT "DNA replication checkpoint control of Wee1 stability by vertebrate Hsl7.";
RL J. Cell Biol. 167:841-849(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WDR77, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=22009756; DOI=10.1074/jbc.m111.303677;
RA Wilczek C., Chitta R., Woo E., Shabanowitz J., Chait B.T., Hunt D.F.,
RA Shechter D.;
RT "Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and
RT H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs.";
RL J. Biol. Chem. 286:42221-42231(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH WDR77 AND
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, SUBUNIT, AND INTERACTION WITH WDR77.
RX PubMed=23451136; DOI=10.1371/journal.pone.0057008;
RA Ho M.C., Wilczek C., Bonanno J.B., Xing L., Seznec J., Matsui T.,
RA Carter L.G., Onikubo T., Kumar P.R., Chan M.K., Brenowitz M., Cheng R.H.,
RA Reimer U., Almo S.C., Shechter D.;
RT "Structure of the arginine methyltransferase PRMT5-MEP50 reveals a
RT mechanism for substrate specificity.";
RL PLoS ONE 8:E57008-E57008(2013).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA), with a preference for the formation of MMA.
CC Specifically mediates the symmetrical dimethylation of arginine
CC residues in the small nuclear ribonucleoproteins; such methylation
CC being required for the assembly and biogenesis of snRNP core particles.
CC Methylates the arginine in the motif G-R-G-X-G in its substrates
CC histone H2A, H2AX and H4, producing both monomethylated and
CC symmetrically dimethylated 'Arg-3'. Methylates nucleoplasmin at 'Arg-
CC 192', producing both monomethylated and symmetrically dimethylated
CC 'Arg-192'. Involved in the DNA replication checkpoint. Promotes entry
CC into mitosis by promoting the proteasomal degradation of wee2-a. May
CC act as a transcriptional corepressor in CRY1-mediated repression of the
CC core circadian component PER1. Involved in spliceosome maturation and
CC mRNA splicing (By similarity). {ECO:0000250|UniProtKB:Q8CIG8,
CC ECO:0000269|PubMed:15583029, ECO:0000269|PubMed:22009756,
CC ECO:0000269|PubMed:23451136}.
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:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000269|PubMed:22009756};
CC -!- SUBUNIT: Heterotetramer; dimer of heterodimer with wdr77. Interacts
CC with wee2-a; this interaction is disrupted upon activation of the DNA
CC replication checkpoint. {ECO:0000269|PubMed:15583029,
CC ECO:0000269|PubMed:22009756, ECO:0000269|PubMed:23451136}.
CC -!- INTERACTION:
CC Q6NUA1; Q6NUD0: wdr77; NbExp=5; IntAct=EBI-21229405, EBI-21229433;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytosol.
CC Note=Enriched on chromatin.
CC -!- TISSUE SPECIFICITY: Detected in egg (at protein level).
CC {ECO:0000269|PubMed:15583029, ECO:0000269|PubMed:22009756}.
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; AY535008; AAS98802.1; -; mRNA.
DR EMBL; BC068696; AAH68696.1; -; mRNA.
DR RefSeq; NP_001084480.1; NM_001091011.1.
DR PDB; 4G56; X-ray; 2.95 A; A/C=2-633.
DR PDBsum; 4G56; -.
DR AlphaFoldDB; Q6NUA1; -.
DR SMR; Q6NUA1; -.
DR BioGRID; 100851; 1.
DR IntAct; Q6NUA1; 1.
DR DNASU; 407754; -.
DR GeneID; 407754; -.
DR KEGG; xla:407754; -.
DR CTD; 407754; -.
DR Xenbase; XB-GENE-17343549; prmt5.S.
DR OrthoDB; 475852at2759; -.
DR BRENDA; 2.1.1.320; 6725.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 407754; Expressed in ovary and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0034709; C:methylosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; IDA:UniProtKB.
DR GO; GO:0043985; P:histone H4-R3 methylation; ISS:UniProtKB.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
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 3D-structure; Biological rhythms; Cell cycle; Cell division;
KW Chromatin regulator; Cytoplasm; Methyltransferase; Mitosis; Nucleus;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..633
FT /note="Protein arginine N-methyltransferase 5"
FT /id="PRO_0000422972"
FT DOMAIN 304..611
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 431
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 440
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 323
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 329..330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 388
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 414..416
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 431
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 440
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 440
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 92..111
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 327..344
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 348..352
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:4G56"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 463..472
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 530..537
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 542..556
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 578..588
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 593..602
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 604..613
FT /evidence="ECO:0007829|PDB:4G56"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:4G56"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:4G56"
SQ SEQUENCE 633 AA; 72285 MW; F3A61499DF6623CC CRC64;
MAAGDGGRVS SGRDVACVTE VADTLGAMAN QGFDFLCMPI FHPRFKREFY KEPAKSRPGP
QTRSDLLLSG RDWNTLIVGK LSDWIKTDSE VSRIRKTSEA AMQQELNFSA YLGLPAFLIP
LKQEDNSNLS RLLINHIHVG HHSTMFWMRV PLMAPNDLRD DLIENEPISL SEEDNSGEER
TWIWWHNFRS LCDYNKKIAL AIEIGADLPS GHVIDRWLGE PIKAAFLPTS IFLTNKKGFP
VLTKVHQRLI FKLFKLEVQF VISGSHHHSE KDLCSYLQYL EYLSQNSPPP NAYEMFAKGY
EDYLQSPLQP LMDNLESQTY EVFEKDPVKY SQYQQAVYKC LLDRVPEEEK ETNIQILMVL
GAGRGPLVNA SLRAAKQAER KIKVYAVEKN PNAVITLEGW RYEEWGSQVT VVSGDMREWK
APEKADIIVS ELLGSFGDNE LSPECLDGAQ HFLKDDGVSI PGEYTSYLAP ISSSKLYNEV
RACREKDRDP EAQFEMPYVV RLHNFHQLSD PLPCFTFHHP NKDDVIDNNR YCCLQYRVDL
NTVLHGFAGY FNTVLYKDVT LSICPESHSP GMFSWFPILF PIKQPIPMRE GDTVCVRFWR
CNNGKKVWYE WAVTSPVCSA IHNPTGRSYT IGL
