Reviewed, UniProtKB/Swiss-Prot Q99MI9 (ANM7_CRILO)

Names and origin

Protein names

Recommended name:
    Protein arginine N-methyltransferase 7
    EC=2.1.1.-
Alternative name(s):
    Histone-arginine N-methyltransferase PRMT7
    EC=2.1.1.125
    [Myelin basic protein]-arginine N-methyltransferase PRMT7
    EC=2.1.1.126

Gene names

Name:

Prmt7

Organism

Cricetulus longicaudatus (Long-tailed hamster) (Chinese hamster)

Taxonomic identifier

10030 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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 H4R3sme2. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3sme2, 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 By similarity.
Catalytic activity	S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine. S-adenosyl-L-methionine + [myelin basic protein]-arginine = S-adenosyl-L-homocysteine + [myelin basic protein]-N(omega)-methyl-arginine.
Subunit structure	Interacts with CTCFL, PRMT5 and SNRPD3 By similarity. Homodimer and heterodimer.
Subcellular location	Isoform 1: Cytoplasm. Nucleus. Ref.2 Isoform 2: Cytoplasm. Ref.2
Miscellaneous	Confers resistance or sensitivity to DNA-damaging agents. Down-regulation confers increased sensitivity to the Top1 inhibitor camptothecin (CPT).
Sequence similarities	Belongs to the protein arginine N-methyltransferase family. PRMT7 subfamily.

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
Gene Ontology (GO)
Biological process	DNA methylation during gametogenesis Inferred from sequence or structural similarity. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW genetic imprinting Inferred from sequence or structural similarity. Source: UniProtKB histone arginine methylation Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-arginine methylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW spliceosomal snRNP assembly Inferred from sequence or structural similarity. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	[myelin basic protein]-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC histone methyltransferase activity (H4-R3 specific) Inferred from sequence or structural similarity. Source: UniProtKB protein-arginine omega-N symmetric methyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99MI9-2)

Also known as: Alpha; p77; p78;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q99MI9-1)

Also known as: Beta; p82;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAAALAASGMLPTADLFLRRKLTRPHFCANIEELVGNM

Isoform 3 (identifier: Q99MI9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: Missing.

Isoform 4 (identifier: Q99MI9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: MKVFCGRANP...AGADFCYAIE → MFRVKLWDQSQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 692	692	Protein arginine N-methyltransferase 7		PRO_0000212334
Natural variations
	Alternative sequence	1 – 94	94	MKVFC…CYAIE → MFRVKLWDQSQ in isoform 4.		VSP_037251
	Alternative sequence	1 – 37	37	Missing in isoform 3.		VSP_037252
	Alternative sequence	1	1	M → MAAALAASGMLPTADLFLRR KLTRPHFCANIEELVGNM in isoform 2.		VSP_005212

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) (p77) (p78) [UniParc]. Last modified May 5, 2009. Version 3. Checksum: 99A317328DA3AB0D	FASTA	692	78,298
	10 20 30 40 50 60 MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ GIRAAVSRVK 70 80 90 100 110 120 DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN 130 140 150 160 170 180 KHSTEVTVGP DGDLPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVQEN CEAVPHKATV 190 200 210 220 230 240 YAQLVESRRM WSWNKLFPVH VQTSLGEQVI VPPSELERCP GAPSVYDIQL NQVPSTDFTA 250 260 270 280 290 300 LSDVLPMFSV DFSKQVSSSA ACHSKQFVPL ASGQAQVVLS WWDIEMDPEG KITCTMAPFW 310 320 330 340 350 360 AQTNPQELQW RDHWMQCVYF LPQEEPVVQG SPRCLVAHHD DYCVWYSLQR TSADENEEVY 370 380 390 400 410 420 QVRPVCDCQA HLLWNRPRFG EINDQDRTDQ YAQALRTVLM PGTICLCVSD GSLLSLLAHH 430 440 450 460 470 480 LGAEQVFTVE SSAASYRLMK RIFKANHLED KVSIIKKRPE LLTSADLEGK KVSLLLGEPF 490 500 510 520 530 540 FATSLLPWHN LYFWYARTSV DQHLEPGAVV MPQAASLYAM IVEFRDLWRI RSPCGDCEGF 550 560 570 580 590 600 DVHIMDDMIK HSLDFRESRE AEPHPLWEYP CRSLSEPQQI LTFDFQQPVP QKPVHAEGSM 610 620 630 640 650 660 ELRRPGKSHG AVLWMEYHLT PDSTVSTGLM NPLEDKGDCC WNPHCKQAVY FLSTTVDPRV 670 680 690 PLDGPQSVSY AVEFHPLTGD ITMEFRLADT LN
	Isoform 2 (Beta) (p82). Checksum: 005DBE87E38FAF5E	FASTA	729	82,280
	10 20 30 40 50 60 MAAALAASGM LPTADLFLRR KLTRPHFCAN IEELVGNMKV FCGRANPTTG SLEWLEEDEH 70 80 90 100 110 120 YDYHQEIARS SYADMLHDKD RNIKYYQGIR AAVSRVKDRG QKALVLDIGT GTGLLSMMAV 130 140 150 160 170 180 TAGADFCYAI EVFKPMADAA VKIVEKNGFS DKIKVINKHS TEVTVGPDGD LPCRANILVT 190 200 210 220 230 240 ELFDTELIGE GALPSYEHAH RHLVQENCEA VPHKATVYAQ LVESRRMWSW NKLFPVHVQT 250 260 270 280 290 300 SLGEQVIVPP SELERCPGAP SVYDIQLNQV PSTDFTALSD VLPMFSVDFS KQVSSSAACH 310 320 330 340 350 360 SKQFVPLASG QAQVVLSWWD IEMDPEGKIT CTMAPFWAQT NPQELQWRDH WMQCVYFLPQ 370 380 390 400 410 420 EEPVVQGSPR CLVAHHDDYC VWYSLQRTSA DENEEVYQVR PVCDCQAHLL WNRPRFGEIN 430 440 450 460 470 480 DQDRTDQYAQ ALRTVLMPGT ICLCVSDGSL LSLLAHHLGA EQVFTVESSA ASYRLMKRIF 490 500 510 520 530 540 KANHLEDKVS IIKKRPELLT SADLEGKKVS LLLGEPFFAT SLLPWHNLYF WYARTSVDQH 550 560 570 580 590 600 LEPGAVVMPQ AASLYAMIVE FRDLWRIRSP CGDCEGFDVH IMDDMIKHSL DFRESREAEP 610 620 630 640 650 660 HPLWEYPCRS LSEPQQILTF DFQQPVPQKP VHAEGSMELR RPGKSHGAVL WMEYHLTPDS 670 680 690 700 710 720 TVSTGLMNPL EDKGDCCWNP HCKQAVYFLS TTVDPRVPLD GPQSVSYAVE FHPLTGDITM EFRLADTLN
	Isoform 3. Checksum: 32494C1F3195CC45	FASTA	655	73,966
	10 20 30 40 50 60 MLHDKDRNIK YYQGIRAAVS RVKDRGQKAL VLDIGTGTGL LSMMAVTAGA DFCYAIEVFK 70 80 90 100 110 120 PMADAAVKIV EKNGFSDKIK VINKHSTEVT VGPDGDLPCR ANILVTELFD TELIGEGALP 130 140 150 160 170 180 SYEHAHRHLV QENCEAVPHK ATVYAQLVES RRMWSWNKLF PVHVQTSLGE QVIVPPSELE 190 200 210 220 230 240 RCPGAPSVYD IQLNQVPSTD FTALSDVLPM FSVDFSKQVS SSAACHSKQF VPLASGQAQV 250 260 270 280 290 300 VLSWWDIEMD PEGKITCTMA PFWAQTNPQE LQWRDHWMQC VYFLPQEEPV VQGSPRCLVA 310 320 330 340 350 360 HHDDYCVWYS LQRTSADENE EVYQVRPVCD CQAHLLWNRP RFGEINDQDR TDQYAQALRT 370 380 390 400 410 420 VLMPGTICLC VSDGSLLSLL AHHLGAEQVF TVESSAASYR LMKRIFKANH LEDKVSIIKK 430 440 450 460 470 480 RPELLTSADL EGKKVSLLLG EPFFATSLLP WHNLYFWYAR TSVDQHLEPG AVVMPQAASL 490 500 510 520 530 540 YAMIVEFRDL WRIRSPCGDC EGFDVHIMDD MIKHSLDFRE SREAEPHPLW EYPCRSLSEP 550 560 570 580 590 600 QQILTFDFQQ PVPQKPVHAE GSMELRRPGK SHGAVLWMEY HLTPDSTVST GLMNPLEDKG 610 620 630 640 650 DCCWNPHCKQ AVYFLSTTVD PRVPLDGPQS VSYAVEFHPL TGDITMEFRL ADTLN
	Isoform 4. Checksum: C5420F7A98B6BB1A	FASTA	609	69,171
	10 20 30 40 50 60 MFRVKLWDQS QVFKPMADAA VKIVEKNGFS DKIKVINKHS TEVTVGPDGD LPCRANILVT 70 80 90 100 110 120 ELFDTELIGE GALPSYEHAH RHLVQENCEA VPHKATVYAQ LVESRRMWSW NKLFPVHVQT 130 140 150 160 170 180 SLGEQVIVPP SELERCPGAP SVYDIQLNQV PSTDFTALSD VLPMFSVDFS KQVSSSAACH 190 200 210 220 230 240 SKQFVPLASG QAQVVLSWWD IEMDPEGKIT CTMAPFWAQT NPQELQWRDH WMQCVYFLPQ 250 260 270 280 290 300 EEPVVQGSPR CLVAHHDDYC VWYSLQRTSA DENEEVYQVR PVCDCQAHLL WNRPRFGEIN 310 320 330 340 350 360 DQDRTDQYAQ ALRTVLMPGT ICLCVSDGSL LSLLAHHLGA EQVFTVESSA ASYRLMKRIF 370 380 390 400 410 420 KANHLEDKVS IIKKRPELLT SADLEGKKVS LLLGEPFFAT SLLPWHNLYF WYARTSVDQH 430 440 450 460 470 480 LEPGAVVMPQ AASLYAMIVE FRDLWRIRSP CGDCEGFDVH IMDDMIKHSL DFRESREAEP 490 500 510 520 530 540 HPLWEYPCRS LSEPQQILTF DFQQPVPQKP VHAEGSMELR RPGKSHGAVL WMEYHLTPDS 550 560 570 580 590 600 TVSTGLMNPL EDKGDCCWNP HCKQAVYFLS TTVDPRVPLD GPQSVSYAVE FHPLTGDITM EFRLADTLN

References

[1]	"Identification of new drug sensitivity genes using genetic suppressor elements: protein arginine N-methyltransferase mediates cell sensitivity to DNA-damaging agents." Gros L., Delaporte C., Frey S., Decesse J., de Saint-Vincent B.R., Cavarec L., Dubart A., Gudkov A.V., Jacquemin-Sablon A. Cancer Res. 63:164-171(2003) [PubMed: 12517794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). Tissue: Lung.
[2]	"Characterization of prmt7alpha and beta isozymes from Chinese hamster cells sensitive and resistant to topoisomerase II inhibitors." Gros L., Renodon-Corniere A., de Saint Vincent B.R., Feder M., Bujnicki J.M., Jacquemin-Sablon A. Biochim. Biophys. Acta 1760:1646-1656(2006) [PubMed: 17049166] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[3]	"Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target for the sensitization of tumor cells to camptothecins." Verbiest V., Montaudon D., Tautu M.T., Moukarzel J., Portail J.-P., Markovits J., Robert J., Ichas F., Pourquier P. FEBS Lett. 582:1483-1489(2008) [PubMed: 18381071] [Abstract] Cited for: INCREASED SENSITIVITY TO CAMPTOTHECIN.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF336043 mRNA. Translation: AAK20884.1. AF336044 mRNA. Translation: AAK20885.1. AY781113 mRNA. Translation: AAV52835.1. AY781114 mRNA. Translation: AAV52836.1. AY781115 mRNA. Translation: AAV52837.1. AY781116 mRNA. Translation: AAV52838.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q99MI9.
Family and domain databases
InterPro	IPR014644. Arg_N-MeTrfase. [Graphical view]
PIRSF	PIRSF036946. Arg_N-mtase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ANM7_CRILO

Accession

Primary (citable) accession number: Q99MI9
Secondary accession number(s): Q5S3S4 , Q5S3S5, Q5S3S6, Q99MJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	May 5, 2009
Last modified:	October 13, 2009
This is version 34 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)