ANM7_RAT
ID ANM7_RAT Reviewed; 693 AA.
AC Q5U4E8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; CH473972; EDL92443.1; -; Genomic_DNA.
DR EMBL; BC085121; AAH85121.1; -; mRNA.
DR RefSeq; NP_001014175.1; NM_001014153.1.
DR AlphaFoldDB; Q5U4E8; -.
DR SMR; Q5U4E8; -.
DR STRING; 10116.ENSRNOP00000000275; -.
DR PaxDb; Q5U4E8; -.
DR PRIDE; Q5U4E8; -.
DR Ensembl; ENSRNOT00000109438; ENSRNOP00000089074; ENSRNOG00000000258.
DR GeneID; 361402; -.
DR KEGG; rno:361402; -.
DR UCSC; RGD:1304869; rat.
DR CTD; 54496; -.
DR RGD; 1304869; Prmt7.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000156879; -.
DR HOGENOM; CLU_015180_0_0_1; -.
DR InParanoid; Q5U4E8; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; Q5U4E8; -.
DR TreeFam; TF315221; -.
DR Reactome; R-RNO-3214858; RMTs methylate histone arginines.
DR PRO; PR:Q5U4E8; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000000258; Expressed in testis and 18 other tissues.
DR Genevisible; Q5U4E8; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; ISO:RGD.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISO:RGD.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISO:RGD.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:RGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISO:RGD.
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:0016571; P:histone methylation; ISO:RGD.
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..693
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000373902"
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 693 AA; 78346 MW; 757BB76971EFDA48 CRC64;
MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ GIRAAVSRVK
DKGQKALVLD IGTGTGLLSM MAVTAGADFC YAVEVFKPMA EAAVKIVEKN GFSDKIKVIN
KHSTEVTVGP DGDLPCRANI LVTELFDTEL IGEGALPSYE HAHKHLVQED CEAVPHRATV
YAQLVESKRM WSWNKLFPVR VQTGLGEQLI IPPSELERCP GAPSVYDIQL NQVSPADFTV
LSDVLPMFSV DFSKQVSSSA ACHSKQFVPL ASGQAQVVLS WWDIEMDPEG KIKCTMAPFW
AQTDPQELQW RDHWMQCVYF LPQEEPIMQG SPRCLAAHHD DYCVWYSLQR TSPDENNSAY
QVRPVCDCQA HLLWNRPRFG EINDQDRTDH YARALRTMLM PGSICLCVSD GSLLSVLAHH
LGAEQVFTVE SSVASYRLMK RIFKVNHLED KITVINKRPE LLTSADLEGK KVSLLLGEPF
FTTSLLPWHN LYFWYVRTSV DQHLAPGAVV MPQAASLHAV IVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK HSLDFRESRE AEPQPLWEYP CRSLSEPRQI LTFDFQQPIP QQPMQSRGVM
ELRRPGKSHG AVLWMEYQLT PDSTVSTGLM NPAEDKGDCC WNPHCKQAVY FLSATLDPSA
PLDGPQSVSY AVEFHPLTGD ITMEFRLADD TLN
