ANM7_XENLA
ID ANM7_XENLA Reviewed; 685 AA.
AC Q6PCI6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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 -!- 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; BC059311; AAH59311.1; -; mRNA.
DR RefSeq; NP_001080010.1; NM_001086541.1.
DR AlphaFoldDB; Q6PCI6; -.
DR SMR; Q6PCI6; -.
DR DNASU; 379700; -.
DR GeneID; 379700; -.
DR KEGG; xla:379700; -.
DR CTD; 379700; -.
DR Xenbase; XB-GENE-974631; prmt7.L.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 379700; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
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; Methyltransferase;
KW Nucleus; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..685
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373905"
FT DOMAIN 14..341
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 353..680
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"
SQ SEQUENCE 685 AA; 77291 MW; A6FCA5A47A78EFF8 CRC64;
MKVFCGRVNP TTGAMDWVEE DEHYDYHQEI ARSSYADMLH DKDRNEKYYQ GICAAVRRVK
QRGQEAVVLD IGTGTGLLSM MAVTAGADCC YAIEVFKPMS DAAVQIVKAN GFSDKIKVIN
KHSTEVTVGP DGDMKTKANI LITELFDTEL IGEGALPSYE HAQHNLMQET WEAVPHRATV
FAQLVESTRL WSWNKLFPLN LETGDIKPHP ELETCPGAPS VCDIQLSQLN PRDFKILSEV
LCVFRVDFSC QVSSAPTSHP VHFTSLASGA AQVVLSWWEI DMDPDGSITC TMQPSWMYET
QQSVPWRDHW MQCVYFLPKE CSVTQGEVCC LTAHQDDYCV WYSLNKSSAE NDPVCRERPT
CHCGAHITWN RARFGELNDR HRTQQYFEAL KKVVTPSSTC LCVSDGSLLP VLAHSLGAKQ
IYTLESSSIA QHLMKKLFQV NHLGEKIQVL HKSADSLITA DFEDRKISTL IGEPFFTTNL
LPWHNLYFWY SRTALSTNLA KDCTVLPLSA SLHVVAVEFK DLWRIRSPCG MCEGFDVSIM
DKMIKNSLNF RESQEAEPHP LWEYPCRALS EPIQVMTFNF TEPVPTEEIR ASGSLNLVRS
GQCHGAVLWM VYELTKEITV STGLIGISEE MGECQWYPHR KQGVYFFSSI LNPQTIPAQS
PSSVSYSVTF IPKEGDIRMC FEPDF
