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Protein arginine N-methyltransferase 7 (EC 2.1.1.321) (Histone-arginine N-methyltransferase PRMT7) ([Myelin basic protein]-arginine N-methyltransferase PRMT7)

 ANM7_CRILO              Reviewed;         692 AA.
Q99MI9; Q5S3S4; Q5S3S5; Q5S3S6; Q99MJ0;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
10-MAY-2017, entry version 66.
RecName: Full=Protein arginine N-methyltransferase 7;
EC=2.1.1.321 {ECO:0000250|UniProtKB:Q9NVM4};
AltName: Full=Histone-arginine N-methyltransferase PRMT7;
AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7;
Name=Prmt7;
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese
hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10030;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Lung;
PubMed=12517794;
Gros L., Delaporte C., Frey S., Decesse J., de Saint-Vincent B.R.,
Cavarec L., Dubart A., Gudkov A.V., Jacquemin-Sablon A.;
"Identification of new drug sensitivity genes using genetic suppressor
elements: protein arginine N-methyltransferase mediates cell
sensitivity to DNA-damaging agents.";
Cancer Res. 63:164-171(2003).
[2]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17049166; DOI=10.1016/j.bbagen.2006.08.026;
Gros L., Renodon-Corniere A., de Saint Vincent B.R., Feder M.,
Bujnicki J.M., Jacquemin-Sablon A.;
"Characterization of prmt7alpha and beta isozymes from Chinese hamster
cells sensitive and resistant to topoisomerase II inhibitors.";
Biochim. Biophys. Acta 1760:1646-1656(2006).
[3]
INCREASED SENSITIVITY TO CAMPTOTHECIN.
PubMed=18381071; DOI=10.1016/j.febslet.2008.03.031;
Verbiest V., Montaudon D., Tautu M.T., Moukarzel J., Portail J.-P.,
Markovits J., Robert J., Ichas F., Pourquier P.;
"Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential
target for the sensitization of tumor cells to camptothecins.";
FEBS Lett. 582:1483-1489(2008).
-!- FUNCTION: Arginine methyltransferase that can both catalyze the
formation of omega-N monomethylarginine (MMA) and symmetrical
dimethylarginine (sDMA), with a preference for the formation of
MMA. Specifically mediates the symmetrical dimethylation of
arginine residues in the small nuclear ribonucleoproteins Sm D1
(SNRPD1) and Sm D3 (SNRPD3); such methylation being required for
the assembly and biogenesis of snRNP core particles. Specifically
mediates the symmetric dimethylation of histone H4 'Arg-3' to form
H4R3me2s. Plays a role in gene imprinting by being recruited by
CTCFL at the H19 imprinted control region (ICR) and methylating
histone H4 to form H4R3me2s, possibly leading to recruit DNA
methyltransferases at these sites. May also play a role in
embryonic stem cell (ESC) pluripotency. Also able to mediate the
arginine methylation of histone H2A and myelin basic protein (MBP)
in vitro; the relevance of such results is however unclear in
vivo. {ECO:0000250|UniProtKB:Q9NVM4}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [protein]-L-arginine
= S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-
arginine. {ECO:0000250|UniProtKB:Q9NVM4}.
-!- SUBUNIT: Interacts with CTCFL, PRMT5 and SNRPD3 (By similarity).
Homodimer and heterodimer. {ECO:0000250,
ECO:0000269|PubMed:17049166}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Alpha, p77, p78;
IsoId=Q99MI9-2; Sequence=Displayed;
Name=2; Synonyms=Beta, p82;
IsoId=Q99MI9-1; Sequence=VSP_005212;
Name=3;
IsoId=Q99MI9-3; Sequence=VSP_037252;
Name=4;
IsoId=Q99MI9-4; Sequence=VSP_037251;
-!- MISCELLANEOUS: Confers resistance or sensitivity to DNA-damaging
agents. Down-regulation confers increased sensitivity to the Top1
inhibitor camptothecin (CPT).
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. PRMT7 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU01015}.
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EMBL; AF336043; AAK20884.1; -; mRNA.
EMBL; AF336044; AAK20885.1; -; mRNA.
EMBL; AY781113; AAV52835.1; -; mRNA.
EMBL; AY781114; AAV52836.1; -; mRNA.
EMBL; AY781115; AAV52837.1; -; mRNA.
EMBL; AY781116; AAV52838.1; -; mRNA.
ProteinModelPortal; Q99MI9; -.
SMR; Q99MI9; -.
BRENDA; 2.1.1.125; 1695.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR014644; MeTrfase_PRMT7.
InterPro; IPR029063; SAM-dependent_MTases.
PIRSF; PIRSF036946; Arg_N-mtase; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51678; SAM_MT_PRMT; 2.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Cytoplasm; Differentiation;
Methylation; Methyltransferase; Nucleus; Repeat;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase.
CHAIN 1 692 Protein arginine N-methyltransferase 7.
/FTId=PRO_0000212334.
DOMAIN 14 345 SAM-dependent MTase PRMT-type 1.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
DOMAIN 358 684 SAM-dependent MTase PRMT-type 2.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
ACT_SITE 144 144 {ECO:0000250}.
ACT_SITE 153 153 {ECO:0000250}.
MOD_RES 32 32 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q922X9}.
VAR_SEQ 1 94 MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHD
KDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMA
VTAGADFCYAIE -> MFRVKLWDQSQ (in isoform
4). {ECO:0000303|PubMed:12517794}.
/FTId=VSP_037251.
VAR_SEQ 1 37 Missing (in isoform 3).
{ECO:0000303|PubMed:12517794}.
/FTId=VSP_037252.
VAR_SEQ 1 1 M -> MAAALAASGMLPTADLFLRRKLTRPHFCANIEELVG
NM (in isoform 2).
{ECO:0000303|PubMed:12517794}.
/FTId=VSP_005212.
SEQUENCE 692 AA; 78298 MW; 99A317328DA3AB0D CRC64;
MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ GIRAAVSRVK
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN
KHSTEVTVGP DGDLPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVQEN CEAVPHKATV
YAQLVESRRM WSWNKLFPVH VQTSLGEQVI VPPSELERCP GAPSVYDIQL NQVPSTDFTA
LSDVLPMFSV DFSKQVSSSA ACHSKQFVPL ASGQAQVVLS WWDIEMDPEG KITCTMAPFW
AQTNPQELQW RDHWMQCVYF LPQEEPVVQG SPRCLVAHHD DYCVWYSLQR TSADENEEVY
QVRPVCDCQA HLLWNRPRFG EINDQDRTDQ YAQALRTVLM PGTICLCVSD GSLLSLLAHH
LGAEQVFTVE SSAASYRLMK RIFKANHLED KVSIIKKRPE LLTSADLEGK KVSLLLGEPF
FATSLLPWHN LYFWYARTSV DQHLEPGAVV MPQAASLYAM IVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK HSLDFRESRE AEPHPLWEYP CRSLSEPQQI LTFDFQQPVP QKPVHAEGSM
ELRRPGKSHG AVLWMEYHLT PDSTVSTGLM NPLEDKGDCC WNPHCKQAVY FLSTTVDPRV
PLDGPQSVSY AVEFHPLTGD ITMEFRLADT LN


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