ANM7_BOVIN
ID ANM7_BOVIN Reviewed; 695 AA.
AC A6QQV6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein arginine N-methyltransferase 7;
DE EC=2.1.1.321 {ECO:0000250|UniProtKB:Q9NVM4};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT7;
DE AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7;
GN Name=PRMT7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9NVM4}.
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:0000250|UniProtKB:Q9NVM4};
CC -!- SUBUNIT: Homodimer and heterodimer. Interacts with CTCFL, PRMT5 and
CC SNRPD3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; BC150009; AAI50010.1; -; mRNA.
DR RefSeq; NP_001095460.1; NM_001101990.2.
DR AlphaFoldDB; A6QQV6; -.
DR SMR; A6QQV6; -.
DR STRING; 9913.ENSBTAP00000012699; -.
DR PaxDb; A6QQV6; -.
DR PRIDE; A6QQV6; -.
DR GeneID; 514202; -.
DR KEGG; bta:514202; -.
DR CTD; 54496; -.
DR eggNOG; KOG1501; Eukaryota.
DR InParanoid; A6QQV6; -.
DR OrthoDB; 408622at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0004984; F:olfactory receptor activity; IBA:GO_Central.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR014644; MeTrfase_PRMT7.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Differentiation; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..695
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373901"
FT DOMAIN 14..345
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 358..684
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q922X9"
SQ SEQUENCE 695 AA; 78654 MW; D668901147C94E95 CRC64;
MKVFCGRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNMKYYQ GIRAAVSRVK
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN
KHSTEVTVGP DGDMPCRANI LITELFDTEL IGEGALPSYE HAHRHLVQAN CEAVPHRATV
YAQLVESRRM WSWNKLFPIR VQTSRGERVI IPPLELERCP GAPSVCDIQL NQVSPADFTI
LSDVLPMFSV DFSKQVSSSA ACHSRQFEPL VSGRAQVVLS WWDIEMDPEG KIKCTMAPSW
AHSDPEELQW RDHWMQCVYF LPQEEPVVQG LALCLVAYHD DYCVWYSLQK TSPEKNGRVH
PVRPVCDCQA HLLWNRPRFG EINDRNRTDQ YIQALRTVLK PDSVCLCVSD GSLLSMLAYH
LGVEQVFTIE NSAVSHRLMK KIFKANHLED KINIIEKRPE LLTPADLEGK KVSLLLGEPF
FTTSLLPWHN LYFWYVRTAV DQHLGPGAVV MPQAASLHVV VVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK RALDFRESKE AEPHPLWEYP CSSLSEPQQI LTFDFRQPVP LQPIHAEGTI
ELRRCGRSHG AVLWMEYHLT ADSTVSTGLL KSAEDEGDCC WNPHCKQAVY FFNTTLDPRA
PPGSSQTVTY TVEFHPHTGD ITMDFTLSDA LDSGC
