ANM7_CRILO
ID ANM7_CRILO Reviewed; 692 AA.
AC Q99MI9; Q5S3S4; Q5S3S5; Q5S3S6; Q99MJ0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
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 Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Lung;
RX PubMed=12517794;
RA Gros L., Delaporte C., Frey S., Decesse J., de Saint-Vincent B.R.,
RA Cavarec L., Dubart A., Gudkov A.V., Jacquemin-Sablon A.;
RT "Identification of new drug sensitivity genes using genetic suppressor
RT elements: protein arginine N-methyltransferase mediates cell sensitivity to
RT DNA-damaging agents.";
RL Cancer Res. 63:164-171(2003).
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17049166; DOI=10.1016/j.bbagen.2006.08.026;
RA Gros L., Renodon-Corniere A., de Saint Vincent B.R., Feder M.,
RA Bujnicki J.M., Jacquemin-Sablon A.;
RT "Characterization of prmt7alpha and beta isozymes from Chinese hamster
RT cells sensitive and resistant to topoisomerase II inhibitors.";
RL Biochim. Biophys. Acta 1760:1646-1656(2006).
RN [3]
RP INCREASED SENSITIVITY TO CAMPTOTHECIN.
RX PubMed=18381071; DOI=10.1016/j.febslet.2008.03.031;
RA Verbiest V., Montaudon D., Tautu M.T., Moukarzel J., Portail J.-P.,
RA Markovits J., Robert J., Ichas F., Pourquier P.;
RT "Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target
RT for the sensitization of tumor cells to camptothecins.";
RL FEBS Lett. 582:1483-1489(2008).
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: Interacts with CTCFL, PRMT5 and SNRPD3 (By similarity).
CC Homodimer and heterodimer. {ECO:0000250, ECO:0000269|PubMed:17049166}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Alpha, p77, p78;
CC IsoId=Q99MI9-2; Sequence=Displayed;
CC Name=2; Synonyms=Beta, p82;
CC IsoId=Q99MI9-1; Sequence=VSP_005212;
CC Name=3;
CC IsoId=Q99MI9-3; Sequence=VSP_037252;
CC Name=4;
CC IsoId=Q99MI9-4; Sequence=VSP_037251;
CC -!- MISCELLANEOUS: Confers resistance or sensitivity to DNA-damaging
CC agents. Down-regulation confers increased sensitivity to the Top1
CC inhibitor camptothecin (CPT).
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; AF336043; AAK20884.1; -; mRNA.
DR EMBL; AF336044; AAK20885.1; -; mRNA.
DR EMBL; AY781113; AAV52835.1; -; mRNA.
DR EMBL; AY781114; AAV52836.1; -; mRNA.
DR EMBL; AY781115; AAV52837.1; -; mRNA.
DR EMBL; AY781116; AAV52838.1; -; mRNA.
DR AlphaFoldDB; Q99MI9; -.
DR SMR; Q99MI9; -.
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 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Cytoplasm; Differentiation;
KW Methylation; Methyltransferase; Nucleus; Repeat; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..692
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000212334"
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"
FT VAR_SEQ 1..94
FT /note="MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGI
FT RAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIE -> MFRVKLWDQSQ
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12517794"
FT /id="VSP_037251"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12517794"
FT /id="VSP_037252"
FT VAR_SEQ 1
FT /note="M -> MAAALAASGMLPTADLFLRRKLTRPHFCANIEELVGNM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12517794"
FT /id="VSP_005212"
SQ 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
