ID A0A384BEU2_BALAS Unreviewed; 699 AA.
AC A0A384BEU2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_007198236.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007198236.1};
RN [1] {ECO:0000313|RefSeq:XP_007198236.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007198236.1};
RG RefSeq;
RL Submitted (JAN-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_007198236.1; XM_007198174.1.
DR AlphaFoldDB; A0A384BEU2; -.
DR GeneID; 102997779; -.
DR CTD; 54496; -.
DR OrthoDB; 2914957at2759; -.
DR Proteomes; UP000261681; 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; 3.
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; 2.
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:UP000261681};
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 699 AA; 79371 MW; DF109F065A4EC61A CRC64;
MERFSWPRLL RIRPVYRQLA RLLFYANTEE LIGTMKVFCG RANPTTGSVE WLEEDEHYDY
HQEIARSSYA DMLHDKDRNM KYYQGIRAAV SRVKDKGQKA LVLDIGTGTG LLSMMAVTAG
ADFCYAIEIF KPMADAAVKI VEKNGFSDKI KIINKHSTEV TIGPDGDMPC RANILITELF
DTELIGEGAL PSYEHAHRHL VQENCEAVPH RATVYAQLVE SRRMWSWNKL FPIRVQTSLG
EQVIVPPLEL ERCPGAPSVY DIQLNQVSLT DFTVLSDVLP MFSVDFSKQV SSSAASHSRQ
FEPLASGQAQ VVLSWWDIEM DPEGKIKCTM APFWAHSDPE ELQWRDHWMQ CVYFLPEEEP
VVQGSALCLV AHHDDYCVWY SLQRTSPEKD GRAHPARPVC DCQAHLLWNR PRFGEINDQN
RTDQYVQALK TVLKPDGVCL CVSDGSLLSM LAHHLGAEQV FTIENSAASH RLMKKVSLLL
GEPFFTTSLL PWHNLYFWYV RTAVDRHLAP GAVVMPQAAS LHMMVVEFRD LWRIRSPCGD
CEGFDVHIMD DMIKHALDFR ESKEAEPHPL WEYPCCSRSV PQQILTFDFR QPVPLQPICA
EGAIELRRPG RSHGAVLWME YHLTPDSTVS TGLLKPAEDK GYCCWNPHCK QAVYFFNTTL
DPRVPPGGPQ TITYTVEFHP HTGDVTVDFT LSDALDRGC
//
