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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_HUMAN              Reviewed;         692 AA.
Q9NVM4; B3KPR0; B3KUG9; B4E379; Q96PV5; Q9H9L0;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Protein arginine N-methyltransferase 7;
EC=2.1.1.321 {ECO:0000269|PubMed:25294873};
AltName: Full=Histone-arginine N-methyltransferase PRMT7;
AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7;
Name=PRMT7; Synonyms=KIAA1933;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Brain, Spleen, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-692 (ISOFORM 2).
TISSUE=Brain;
PubMed=11572484; DOI=10.1093/dnares/8.4.179;
Nagase T., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XXI.
The complete sequences of 60 new cDNA clones from brain which code for
large proteins.";
DNA Res. 8:179-187(2001).
[4]
FUNCTION.
PubMed=15044439; DOI=10.1074/jbc.M312904200;
Miranda T.B., Miranda M., Frankel A., Clarke S.;
"PRMT7 is a member of the protein arginine methyltransferase family
with a distinct substrate specificity.";
J. Biol. Chem. 279:22902-22907(2004).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15494416; DOI=10.1074/jbc.M405295200;
Lee J.-H., Cook J.R., Yang Z.-H., Mirochnitchenko O., Gunderson S.I.,
Felix A.M., Herth N., Hoffmann R., Pestka S.;
"PRMT7, a new protein arginine methyltransferase that synthesizes
symmetric dimethylarginine.";
J. Biol. Chem. 280:3656-3664(2005).
[6]
FUNCTION, AND INTERACTION WITH PRMT5 AND SNRPD3.
PubMed=17709427; DOI=10.1083/jcb.200702147;
Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I.,
Matera A.G.;
"Two distinct arginine methyltransferases are required for biogenesis
of Sm-class ribonucleoproteins.";
J. Cell Biol. 178:733-740(2007).
[7]
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).
[8]
POSSIBLE INVOLVEMENT IN ETOPOSIDE-INDUCED CYTOTOXICITY.
PubMed=19089452; DOI=10.1007/s00439-008-0607-4;
Bleibel W.K., Duan S., Huang R.S., Kistner E.O., Shukla S.J., Wu X.,
Badner J.A., Dolan M.E.;
"Identification of genomic regions contributing to etoposide-induced
cytotoxicity.";
Hum. Genet. 125:173-180(2009).
[9]
FUNCTION.
PubMed=19110445; DOI=10.1016/j.jasms.2008.11.008;
Wang H., Straubinger R.M., Aletta J.M., Cao J., Duan X., Yu H., Qu J.;
"Accurate localization and relative quantification of arginine
methylation using nanoflow liquid chromatography coupled to electron
transfer dissociation and orbitrap mass spectrometry.";
J. Am. Soc. Mass Spectrom. 20:507-519(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
CATALYTIC ACTIVITY.
PubMed=25294873; DOI=10.1074/jbc.M114.609271;
Feng Y., Hadjikyriacou A., Clarke S.G.;
"Substrate specificity of human protein arginine methyltransferase 7
(PRMT7): the importance of acidic residues in the double E loop.";
J. Biol. Chem. 289:32604-32616(2014).
[12]
INVOLVEMENT IN SBIDDS, AND VARIANTS SBIDDS THR-32; GLY-387 AND
ARG-494.
PubMed=26437029; DOI=10.1038/ng.3410;
DDD study;
Akawi N., McRae J., Ansari M., Balasubramanian M., Blyth M.,
Brady A.F., Clayton S., Cole T., Deshpande C., Fitzgerald T.W.,
Foulds N., Francis R., Gabriel G., Gerety S.S., Goodship J.,
Hobson E., Jones W.D., Joss S., King D., Klena N., Kumar A., Lees M.,
Lelliott C., Lord J., McMullan D., O'Regan M., Osio D., Piombo V.,
Prigmore E., Rajan D., Rosser E., Sifrim A., Smith A.,
Swaminathan G.J., Turnpenny P., Whitworth J., Wright C.F., Firth H.V.,
Barrett J.C., Lo C.W., FitzPatrick D.R., Hurles M.E.;
"Discovery of four recessive developmental disorders using
probabilistic genotype and phenotype matching among 4,125 families.";
Nat. Genet. 47:1363-1369(2015).
-!- 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:0000269|PubMed:15044439, ECO:0000269|PubMed:15494416,
ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:19110445}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [protein]-L-arginine
= S-adenosyl-L-homocysteine + [protein]-N(omega)-methyl-L-
arginine. {ECO:0000269|PubMed:25294873}.
-!- SUBUNIT: Homodimer and heterodimer (By similarity). Interacts with
CTCFL (By similarity). Interacts with PRMT5 and SNRPD3.
{ECO:0000250, ECO:0000269|PubMed:17709427}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:15494416}. Nucleus
{ECO:0000269|PubMed:15494416}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9NVM4-1; Sequence=Displayed;
Name=2;
IsoId=Q9NVM4-2; Sequence=VSP_005213, VSP_005214;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NVM4-3; Sequence=VSP_037253;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9NVM4-4; Sequence=VSP_037254, VSP_037255;
Note=No experimental confirmation available.;
-!- DISEASE: Short stature, brachydactyly, intellectual developmental
disability, and seizures (SBIDDS) [MIM:617157]: An autosomal
recessive disease characterized by developmental delay, learning
disabilities, mild mental retardation, delayed speech, and
skeletal abnormalities. Skeletal features include short stature,
brachydactyly, and short metacarpals and metatarsals.
{ECO:0000269|PubMed:26437029}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: May be involved in etoposide-induced cytotoxicity,
a chemotherapeutic agent frequently used for testicular cancer and
small-cell lung cancer that can cause cytotoxicity in the
treatment of other cancers. 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}.
-!- SEQUENCE CAUTION:
Sequence=BAB14215.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AK001502; BAA91726.1; -; mRNA.
EMBL; AK022739; BAB14215.1; ALT_INIT; mRNA.
EMBL; AK056647; BAG51772.1; -; mRNA.
EMBL; AK097175; BAG53431.1; -; mRNA.
EMBL; AK304605; BAG65391.1; -; mRNA.
EMBL; BC000146; AAH00146.1; -; mRNA.
EMBL; AB067520; BAB67826.1; -; mRNA.
CCDS; CCDS10866.1; -. [Q9NVM4-1]
CCDS; CCDS54033.1; -. [Q9NVM4-3]
RefSeq; NP_001171753.1; NM_001184824.1. [Q9NVM4-3]
RefSeq; NP_001276947.1; NM_001290018.1. [Q9NVM4-1]
RefSeq; NP_061896.1; NM_019023.2. [Q9NVM4-1]
RefSeq; XP_016878783.1; XM_017023294.1. [Q9NVM4-1]
RefSeq; XP_016878784.1; XM_017023295.1. [Q9NVM4-1]
UniGene; Hs.640229; -.
UniGene; Hs.653193; -.
ProteinModelPortal; Q9NVM4; -.
SMR; Q9NVM4; -.
BioGrid; 119992; 25.
IntAct; Q9NVM4; 10.
MINT; MINT-4831330; -.
STRING; 9606.ENSP00000343103; -.
BindingDB; Q9NVM4; -.
ChEMBL; CHEMBL3562175; -.
GuidetoPHARMACOLOGY; 1258; -.
iPTMnet; Q9NVM4; -.
PhosphoSitePlus; Q9NVM4; -.
BioMuta; PRMT7; -.
DMDM; 20137529; -.
EPD; Q9NVM4; -.
MaxQB; Q9NVM4; -.
PaxDb; Q9NVM4; -.
PeptideAtlas; Q9NVM4; -.
PRIDE; Q9NVM4; -.
Ensembl; ENST00000339507; ENSP00000343103; ENSG00000132600. [Q9NVM4-1]
Ensembl; ENST00000441236; ENSP00000409324; ENSG00000132600. [Q9NVM4-1]
Ensembl; ENST00000449359; ENSP00000414716; ENSG00000132600. [Q9NVM4-3]
GeneID; 54496; -.
KEGG; hsa:54496; -.
UCSC; uc010vlg.3; human. [Q9NVM4-1]
CTD; 54496; -.
DisGeNET; 54496; -.
EuPathDB; HostDB:ENSG00000132600.16; -.
GeneCards; PRMT7; -.
HGNC; HGNC:25557; PRMT7.
HPA; HPA044241; -.
MalaCards; PRMT7; -.
MIM; 610087; gene.
MIM; 617157; phenotype.
neXtProt; NX_Q9NVM4; -.
OpenTargets; ENSG00000132600; -.
PharmGKB; PA143485581; -.
eggNOG; ENOG410INRX; Eukaryota.
eggNOG; COG0500; LUCA.
GeneTree; ENSGT00870000136479; -.
HOGENOM; HOG000033951; -.
HOVERGEN; HBG018729; -.
InParanoid; Q9NVM4; -.
KO; K11438; -.
OMA; VPWRDHW; -.
OrthoDB; EOG091G07KL; -.
PhylomeDB; Q9NVM4; -.
TreeFam; TF315221; -.
BioCyc; MetaCyc:HS05660-MONOMER; -.
BRENDA; 2.1.1.125; 2681.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
ChiTaRS; PRMT7; human.
GenomeRNAi; 54496; -.
PRO; PR:Q9NVM4; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000132600; -.
CleanEx; HS_PRMT7; -.
ExpressionAtlas; Q9NVM4; baseline and differential.
Genevisible; Q9NVM4; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; IDA:HGNC.
GO; GO:0042393; F:histone binding; IC:HGNC.
GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:HGNC.
GO; GO:0016274; F:protein-arginine N-methyltransferase activity; TAS:Reactome.
GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IBA:GO_Central.
GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IDA:UniProtKB.
GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:UniProtKB.
GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:HGNC.
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:0016571; P:histone methylation; IDA:HGNC.
GO; GO:0018216; P:peptidyl-arginine methylation; IDA:HGNC.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; ISS:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; IC:HGNC.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
GO; GO:0000387; P:spliceosomal snRNP assembly; IMP: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; Complete proteome;
Cytoplasm; Differentiation; Disease mutation; Dwarfism;
Mental retardation; Methylation; Methyltransferase; Nucleus;
Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase.
CHAIN 1 692 Protein arginine N-methyltransferase 7.
/FTId=PRO_0000212335.
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 45 94 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037253.
VAR_SEQ 95 168 Missing (in isoform 2).
{ECO:0000303|PubMed:11572484}.
/FTId=VSP_005213.
VAR_SEQ 399 472 Missing (in isoform 2).
{ECO:0000303|PubMed:11572484}.
/FTId=VSP_005214.
VAR_SEQ 526 567 DLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPL
W -> VCREQQDVPLVLAATLPCVLAGGCGWGCSFLTGPVA
DPEPLW (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037254.
VAR_SEQ 568 692 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037255.
VARIANT 32 32 R -> T (in SBIDDS; dbSNP:rs149170494).
{ECO:0000269|PubMed:26437029}.
/FTId=VAR_076329.
VARIANT 387 387 R -> G (in SBIDDS; dbSNP:rs762515973).
{ECO:0000269|PubMed:26437029}.
/FTId=VAR_076330.
VARIANT 494 494 W -> R (in SBIDDS; dbSNP:rs751670999).
{ECO:0000269|PubMed:26437029}.
/FTId=VAR_076331.
CONFLICT 218 218 S -> G (in Ref. 1; BAG53431).
{ECO:0000305}.
CONFLICT 246 246 P -> L (in Ref. 1; BAG53431).
{ECO:0000305}.
CONFLICT 258 258 S -> G (in Ref. 1; BAG51772).
{ECO:0000305}.
CONFLICT 633 633 A -> S (in Ref. 1; BAB14215).
{ECO:0000305}.
SEQUENCE 692 AA; 78459 MW; 9E0DB9530154231C CRC64;
MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ GIRAAVSRVK
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN
KHSTEVTVGP EGDMPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVEEN CEAVPHRATV
YAQLVESGRM WSWNKLFPIH VQTSLGEQVI VPPVDVESCP GAPSVCDIQL NQVSPADFTV
LSDVLPMFSI DFSKQVSSSA ACHSRRFEPL TSGRAQVVLS WWDIEMDPEG KIKCTMAPFW
AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALYLVAHHD DYCVWYSLQR TSPEKNERVR
QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YVQALRTVLK PDSVCLCVSD GSLLSVLAHH
LGVEQVFTVE SSAASHKLLR KIFKANHLED KINIIEKRPE LLTNEDLQGR KVSLLLGEPF
FTTSLLPWHN LYFWYVRTAV DQHLGPGAMV MPQAASLHAV VVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK RALDFRESRE AEPHPLWEYP CRSLSEPWQI LTFDFQQPVP LQPLCAEGTV
ELRRPGQSHA AVLWMEYHLT PECTLSTGLL EPADPEGGCC WNPHCKQAVY FFSPAPDPRA
LLGGPRTVSY AVEFHPDTGD IIMEFRHADT PD


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