Reviewed, UniProtKB/Swiss-Prot Q922X9 (ANM7_MOUSE)

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
Synonyms:	Kiaa1933

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	692 AA.
Sequence status	Complete.
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. Ref.7
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. S-adenosyl-L-methionine + [myelin basic protein]-arginine = S-adenosyl-L-homocysteine + [myelin basic protein]-N(omega)-methyl-arginine.
Subunit structure	Homodimer and heterodimer. Interacts with PRMT5 and SNRPD3 By similarity. Interacts with CTCFL. Ref.7
Subcellular location	Cytoplasm › cytosol By similarity. Nucleus By similarity.
Developmental stage	Present in undifferentiated embryonic stem and germ cells; expression is lost when cells differentiate. In the developing testis, it is expressed at all stages. Present in all cells within the developing tubule, including gonocytes and spermatogonia (at protein level). It the developing kidney, it is confined to the nephrogenic zone in the cortical region, where the tips of the ureteric bud induce de novo formation of epithelia in the metanephric mesenchyme and early glomeruli. Expression is around 8-fold lower in adult kidneys. Ref.7 Ref.6 Ref.8
Sequence similarities	Belongs to the protein arginine N-methyltransferase family. PRMT7 subfamily.

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Transferase
Gene Ontology (GO)
Biological process	DNA methylation during gametogenesis Ref.7 Inferred from direct assay. Source: UniProtKB cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW histone arginine methylation Ref.7 Inferred from direct assay. Source: UniProtKB peptidyl-arginine methylation Inferred from sequence or structural similarity. Source: HGNC regulation of gene expression by genetic imprinting Ref.7 Inferred from direct assay. 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 sequence or structural similarity. Source: HGNC histone methyltransferase activity (H4-R3 specific) Ref.7 Inferred from direct assay. Source: UniProtKB protein binding Ref.7 Inferred from physical interaction. Source: UniProtKB protein-arginine omega-N monomethyltransferase activity Inferred from sequence or structural similarity. Source: HGNC protein-arginine omega-N symmetric methyltransferase activity Ref.7 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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_0000212336
Experimental info
	Sequence conflict	37	1	D → E in AAH57177. Ref.5
	Sequence conflict	612	1	V → G in BAE36880. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q922X9-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: D61A9500956BF02D	FASTA	692	78,301
	10 20 30 40 50 60 MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ GIRAAVSRVK 70 80 90 100 110 120 DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA EAAVKIVERN GFSDKIKVIN 130 140 150 160 170 180 KHSTEVTVGP DGDLPCRANI LITELFDTEL IGEGALPSYE HAHKHLVQED CEAVPHRATV 190 200 210 220 230 240 YAQLVESRRM WSWNKLFPVR VRTSLGEQVI VPPSELERCP GAPSVCDIQL NQVSPADFTV 250 260 270 280 290 300 LSDVLPMFSV DFSKQVSSSA ACHSRQFVPL ASGQAQVVLS WWDIEMDPEG KIKCTMAPFW 310 320 330 340 350 360 AQTDPQELQW RDHWMQCVYF LPQEEPVVQG SPRCLVAHHD DYCVWYSLQR TSPDENDSAY 370 380 390 400 410 420 QVRPVCDCQA HLLWNRPRFG EINDQDRTDH YAQALRTVLL PGSVCLCVSD GSLLSMLAHH 430 440 450 460 470 480 LGAEQVFTVE SSVASYRLMK RIFKVNHLED KISVINKRPE LLTAADLEGK KVSLLLGEPF 490 500 510 520 530 540 FTTSLLPWHN LYFWYVRTSV DQHLAPGAVV MPQAASLHAV IVEFRDLWRI RSPCGDCEGF 550 560 570 580 590 600 DVHIMDDMIK HSLDFRESRE AEPHPLWEYP CRSLSKPQEI LTFDFQQPIP QQPMQSKGTM 610 620 630 640 650 660 ELTRPGKSHG AVLWMEYQLT PDSTISTGLI NPAEDKGDCC WNPHCKQAVY FLSTTLDLRV 670 680 690 PLNGPRSVSY VVEFHPLTGD ITMEFRLADT LS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Increased protein arginine methylation in chronic hypoxia: role of protein arginine methyltransferases." Yildirim A.O., Bulau P., Zakrzewicz D., Kitowska K.E., Weissmann N., Grimminger F., Morty R.E., Eickelberg O. Am. J. Respir. Cell Mol. Biol. 35:436-443(2006) [PubMed: 16690984] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryonic tail.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Epididymis.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Mammary tumor.
[6]	"A Mendelian locus on chromosome 16 determines susceptibility to doxorubicin nephropathy in the mouse." Zheng Z., Schmidt-Ott K.M., Chua S., Foster K.A., Frankel R.Z., Pavlidis P., Barasch J., D'Agati V.D., Gharavi A.G. Proc. Natl. Acad. Sci. U.S.A. 102:2502-2507(2005) [PubMed: 15699352] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[7]	"The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation." Jelinic P., Stehle J.-C., Shaw P. PLoS Biol. 4:E355-E355(2006) [PubMed: 17048991] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH CTCFL.
[8]	"Nuclear proteome analysis of undifferentiated mouse embryonic stem and germ cells." Buhr N., Carapito C., Schaeffer C., Kieffer E., Van Dorsselaer A., Viville S. Electrophoresis 29:2381-2390(2008) [PubMed: 18449859] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY673972 mRNA. Translation: AAT76979.1. AK173304 mRNA. Translation: BAD32582.1. Different initiation. AK154255 mRNA. Translation: BAE32467.1. AK162376 mRNA. Translation: BAE36880.1. CH466525 Genomic DNA. Translation: EDL11358.1. BC006705 mRNA. Translation: AAH06705.1. BC057177 mRNA. Translation: AAH57177.1.
IPI	IPI00469937.
RefSeq	NP_663379.1.
UniGene	Mm.251804 Mm.446217
3D structure databases
SMR	Q922X9. Positions 23-350.
ModBase	Search...
Protein-protein interaction databases
STRING	Q922X9.
Proteomic databases
PRIDE	Q922X9.
Genome annotation databases
Ensembl	ENSMUST00000071592; ENSMUSP00000071521; ENSMUSG00000060098; Mus musculus. [Genome view]
GeneID	214572.
KEGG	mmu:214572.
UCSC	uc009nfu.1. mouse.
Organism-specific databases
CTD	214572.
MGI	MGI:2384879. Prmt7.
Rouge	Search...
Phylogenomic databases
eggNOG	roNOG09446.
HOGENOM	HBG377790.
HOVERGEN	Q922X9.
InParanoid	Q922X9.
OMA	YDIQLNQ.
OrthoDB	EOG9K0T74.
PhylomeDB	Q922X9.
Gene expression databases
ArrayExpress	Q922X9.
Bgee	Q922X9.
CleanEx	MM_PRMT7.
Genevestigator	Q922X9.
GermOnline	ENSMUSG00000060098. Mus musculus.
Family and domain databases
InterPro	IPR014644. Arg_N-MeTrfase. IPR010456. PrmA_MeTrfase. [Graphical view]
Pfam	PF06325. PrmA. 1 hit. [Graphical view]
PIRSF	PIRSF036946. Arg_N-mtase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	374360.
SOURCE	Search...

Entry information

Entry name

ANM7_MOUSE

Accession

Primary (citable) accession number: Q922X9
Secondary accession number(s): Q3TRZ6 , Q69Z62, Q6B955, Q6PG80

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	December 1, 2001
Last modified:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)