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Q5U4E8 (ANM7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 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 By similarity.

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 CTCFL, PRMT5 and SNRPD3 By similarity.

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the protein arginine N-methyltransferase family. PRMT7 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 693693Protein arginine N-methyltransferase 7
PRO_0000373902

Sequences

Sequence LengthMass (Da)Tools
Q5U4E8 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 757BB76971EFDA48

FASTA69378,346
        10         20         30         40         50         60 
MKVFCGRANP TTGSLEWLEE DEHYDYHQEI ARSSYADMLH DKDRNIKYYQ GIRAAVSRVK 

        70         80         90        100        110        120 
DKGQKALVLD IGTGTGLLSM MAVTAGADFC YAVEVFKPMA EAAVKIVEKN GFSDKIKVIN 

       130        140        150        160        170        180 
KHSTEVTVGP DGDLPCRANI LVTELFDTEL IGEGALPSYE HAHKHLVQED CEAVPHRATV 

       190        200        210        220        230        240 
YAQLVESKRM WSWNKLFPVR VQTGLGEQLI IPPSELERCP GAPSVYDIQL NQVSPADFTV 

       250        260        270        280        290        300 
LSDVLPMFSV DFSKQVSSSA ACHSKQFVPL ASGQAQVVLS WWDIEMDPEG KIKCTMAPFW 

       310        320        330        340        350        360 
AQTDPQELQW RDHWMQCVYF LPQEEPIMQG SPRCLAAHHD DYCVWYSLQR TSPDENNSAY 

       370        380        390        400        410        420 
QVRPVCDCQA HLLWNRPRFG EINDQDRTDH YARALRTMLM PGSICLCVSD GSLLSVLAHH 

       430        440        450        460        470        480 
LGAEQVFTVE SSVASYRLMK RIFKVNHLED KITVINKRPE LLTSADLEGK KVSLLLGEPF 

       490        500        510        520        530        540 
FTTSLLPWHN LYFWYVRTSV DQHLAPGAVV MPQAASLHAV IVEFRDLWRI RSPCGDCEGF 

       550        560        570        580        590        600 
DVHIMDDMIK HSLDFRESRE AEPQPLWEYP CRSLSEPRQI LTFDFQQPIP QQPMQSRGVM 

       610        620        630        640        650        660 
ELRRPGKSHG AVLWMEYQLT PDSTVSTGLM NPAEDKGDCC WNPHCKQAVY FLSATLDPSA 

       670        680        690 
PLDGPQSVSY AVEFHPLTGD ITMEFRLADD TLN 

« Hide

References

[1]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].
[2]"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].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH473972 Genomic DNA. Translation: EDL92443.1.
BC085121 mRNA. Translation: AAH85121.1.
IPIIPI00365189.
RefSeqNP_001014175.1. NM_001014153.1.
UniGeneRn.14954.

3D structure databases

ProteinModelPortalQ5U4E8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5U4E8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000275; ENSRNOP00000000275; ENSRNOG00000000258.
GeneID361402.
KEGGrno:361402.
NMPDRfig|10116.3.peg.14939.
UCSCNM_001014153. rat.

Organism-specific databases

CTD54496.
RGD1304869. Prmt7.

Phylogenomic databases

eggNOGroNOG09446.
GeneTreeENSGT00530000063495.
InParanoidQ5U4E8.
OMAYDIQLNQ.
OrthoDBEOG48KR9T.
PhylomeDBQ5U4E8.

Gene expression databases

ArrayExpressQ5U4E8.
GenevestigatorQ5U4E8.

Family and domain databases

InterProIPR014644. Arg_N-MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
[Graphical view]
KOK11438.
PfamPF06325. PrmA. 1 hit.
[Graphical view]
PIRSFPIRSF036946. Arg_N-mtase. 1 hit.
ProtoNetSearch...

Other

NextBio676175.

Entry information

Entry nameANM7_RAT
AccessionPrimary (citable) accession number: Q5U4E8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: December 7, 2004
Last modified: November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families