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Reviewed, UniProtKB/Swiss-Prot Q5U4E8 (ANM7_RAT)

Last modified November 3, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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.
Sequence processingThe displayed sequence is not processed.
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 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

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.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Transferase
Gene Ontology (GO)
   Biological processDNA 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 componentcytosol

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 693693Protein arginine N-methyltransferase 7
PRO_0000373902

Sequences

Sequence LengthMass (Da)Tools
Q5U4E8-1 [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

CH473972 Genomic DNA. Translation: EDL92443.1.
BC085121 mRNA. Translation: AAH85121.1.
IPIIPI00365189.
RefSeqNP_001014175.1.
UniGeneRn.14954

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000275; ENSRNOP00000000275; ENSRNOG00000000258; Rattus norvegicus. [Genome view]
GeneID361402.
KEGGrno:361402.
NMPDRfig|10116.3.peg.14939.
UCSCNM_001014153. rat.

Organism-specific databases

CTD361402.
RGD1304869. Prmt7.

Phylogenomic databases

HOVERGENQ5U4E8.
OMAPSVYDIQ.

Gene expression databases

ArrayExpressQ5U4E8.
GenevestigatorQ5U4E8.

Family and domain databases

InterProIPR014644. Arg_N-MeTrfase.
[Graphical view]
PIRSFPIRSF036946. Arg_N-mtase. 1 hit.
ProtoNetSearch...

Other Resources

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 3, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents