ID A0A3Q3EPU7_9LABR Unreviewed; 672 AA.
AC A0A3Q3EPU7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000009344.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000009344.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q3EPU7; -.
DR STRING; 56723.ENSLBEP00000009344; -.
DR Ensembl; ENSLBET00000009860.1; ENSLBEP00000009344.1; ENSLBEG00000007162.1.
DR GeneTree; ENSGT00940000156879; -.
DR InParanoid; A0A3Q3EPU7; -.
DR Proteomes; UP000261660; 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:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
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:UP000261660};
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 672 AA; 75022 MW; 84C4E0380E9E7B63 CRC64;
MKTFCGRANP TTGALDWVEE SEEYDYHQEI ARSCYADMLH DRDRNEKYYQ GIQAAVARVK
QRGEKVIVLD IGTGTGLLSM MAVTAGADFC YAVEVFKPMA EAAQCIVKKN GFSDKIKIIN
KHSTDVTVGP DGDMQTKANV LITELFDTEL IGEGALPSYE HAHRNLVLEG CEAVPHRATV
YAQLVESELL WSWAQMQPVE VEGARVVPPP AVAHCAGAHS VCDIQLSQVS PNSFNPLGPL
CTMFSVDFSK PVSSALQTHS SQFASQSDGR AHVVLSWWDL DMDPSGSIVC SMAPSWTYPQ
PKSAPWRDHW MQSVYFLPVE STVTKGEELS LTVCHDDYSL WYSLRPHSQQ NSQNEAPPSR
PCCTCQAHLV WNRPRFGELN DRRRTESYVS ALRSVLKEDS VCLSVSDGSL LPVFAHILGA
KKVYSLENSR MSKQVIEQVL EANLKKGGVE LLEIRPEQLT SSDVGGEQIS VLMGEPYFST
SLLPWHSLFF WYCRTALAGL LRPDATMLPR SATLHMMAVE FQDLWRIRAP CGTCEGFDVT
PMDEMVQRSL DFRESREAEP HPLWEYPCRA LTQSSAVMTF DFTECVPKQP INSQGSLPLI
RVGRCHGIAL WMEYHLTDDI IVSAGLVGPI SEQGECEWSR HRKQGVYFLS SPWDSSGIPT
YGQLAHRNAS PR
//
