ID A0A1S3W493_ERIEU Unreviewed; 658 AA.
AC A0A1S3W493;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein arginine N-methyltransferase {ECO:0000256|PIRNR:PIRNR036946};
DE EC=2.1.1.321 {ECO:0000256|PIRNR:PIRNR036946};
GN Name=PRMT7 {ECO:0000313|RefSeq:XP_016041323.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016041323.1};
RN [1] {ECO:0000313|RefSeq:XP_016041323.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Sm D1 (SNRPD1) and Sm
CC D3 (SNRPD3); such methylation being required for the assembly and
CC biogenesis of snRNP core particles. Specifically mediates the symmetric
CC dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in
CC gene imprinting by being recruited by CTCFL at the H19 imprinted
CC control region (ICR) and methylating histone H4 to form H4R3me2s,
CC possibly leading to recruit DNA methyltransferases at these sites. May
CC also play a role in embryonic stem cell (ESC) pluripotency. Also able
CC to mediate the arginine methylation of histone H2A and myelin basic
CC protein (MBP) in vitro; the relevance of such results is however
CC unclear in vivo. {ECO:0000256|ARBA:ARBA00025570,
CC ECO:0000256|PIRNR:PIRNR036946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280; EC=2.1.1.321;
CC Evidence={ECO:0000256|ARBA:ARBA00000482,
CC ECO:0000256|PIRNR:PIRNR036946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|PIRNR:PIRNR036946}. Nucleus
CC {ECO:0000256|PIRNR:PIRNR036946}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000256|PIRNR:PIRNR036946}.
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DR RefSeq; XP_016041323.1; XM_016185837.1.
DR AlphaFoldDB; A0A1S3W493; -.
DR GeneID; 103108792; -.
DR CTD; 54496; -.
DR OrthoDB; 2914957at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044020; F:histone H4R3 methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR014644; MeTrfase_PRMT7.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11006:SF4; PROTEIN ARGININE N-METHYLTRANSFERASE 7; 1.
DR Pfam; PF06325; PrmA; 1.
DR PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR036946};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR036946};
KW Differentiation {ECO:0000256|PIRNR:PIRNR036946};
KW Methyltransferase {ECO:0000256|PIRNR:PIRNR036946, ECO:0000256|PROSITE-
KW ProRule:PRU01015}; Nucleus {ECO:0000256|PIRNR:PIRNR036946};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR036946};
KW Transcription {ECO:0000256|PIRNR:PIRNR036946};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR036946};
KW Transferase {ECO:0000256|PIRNR:PIRNR036946, ECO:0000256|PROSITE-
KW ProRule:PRU01015}.
SQ SEQUENCE 658 AA; 74081 MW; BCBCCBB73A770BAA CRC64;
MLHDKDRNIK YYQGIRAAVA RVKEKGQKAL VLDIGTGTGL LSMMAVTAGA DFCYAIEVFK
PMADAATKIV EKNGFSDKIK VINKHSTEVT VGPDGDMPCR ANILVTELFD TELIGEGALP
SYEHAHKHLV QENCEAVPHR ATVYAQLVES RKMWSWNKLF PIHVQTNCGE QIIIPPLELE
RCPGAPSVYD IQLNQVSPAD FTVLSDVLPM FSVDFSKQVS SSAACHHKQF ESLASGQAQV
VLSWWDIEMD PEGTIKCTMA PFWAHSDPEE LQWRDHWMQC VYFLPQAEPV TQGSVLCLVA
HHDDYCIWYS LQRASPPKNR SICLTRPVCD CQAHLLWNRP RFGEINDQDR TDLYVQALKT
VLNPGGACLC VSDGSLLPML AHHLGAEQVF TIESSSASHR LMKKIFKANH LEEKINIIEK
RPELITSADL ESKKVSLLLG EPFFTTSLLP WHNLYFWYVR TAVDKHLEPG AVVLPQAASL
HAVVVEFKDL WRIRSPCGSC EGFDVHIMDD MIKHALDFRE SKEAEPHPLW EYPCRSLSDP
QQILTFDFRQ PVPLQPVHAE GSIELRRPGR SHGVVLWMEY HLTPDSTVST GLLKSTEDKG
DCCWNPHCKQ AVYFFGSVLD HRAPLGNTQT ISYTVEFHPH TGDVSMDFSY SDTPDNGH
//
