ID A0A384BFN0_BALAS Unreviewed; 695 AA.
AC A0A384BFN0;
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_007198238.1};
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_007198238.1};
RN [1] {ECO:0000313|RefSeq:XP_007198238.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007198238.1};
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_007198238.1; XM_007198176.1.
DR AlphaFoldDB; A0A384BFN0; -.
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; 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: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 695 AA; 78635 MW; A1C216939A8AED43 CRC64;
MKVFCGRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNMKYYQ GIRAAVSRVK
DKGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEIFKPMA DAAVKIVEKN GFSDKIKIIN
KHSTEVTIGP DGDMPCRANI LITELFDTEL IGEGALPSYE HAHRHLVQEN CEAVPHRATV
YAQLVESRRM WSWNKLFPIR VQTSLGEQVI VPPLELERCP GAPSVYDIQL NQVSLTDFTV
LSDVLPMFSV DFSKQVSSSA ASHSRQFEPL ASGQAQVVLS WWDIEMDPEG KIKCTMAPFW
AHSDPEELQW RDHWMQCVYF LPEEEPVVQG SALCLVAHHD DYCVWYSLQR TSPEKDGRAH
PARPVCDCQA HLLWNRPRFG EINDQNRTDQ YVQALKTVLK PDGVCLCVSD GSLLSMLAHH
LGAEQVFTIE NSAASHRLMK KIFKANHLED KINIIEKRPE LLTPADLEGK KVSLLLGEPF
FTTSLLPWHN LYFWYVRTAV DRHLAPGAVV MPQAASLHMM VVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK HALDFRESKE AEPHPLWEYP CCSRSVPQQI LTFDFRQPVP LQPICAEGAI
ELRRPGRSHG AVLWMEYHLT PDSTVSTGLL KPAEDKGYCC WNPHCKQAVY FFNTTLDPRV
PPGGPQTITY TVEFHPHTGD VTVDFTLSDA LDRGC
//
