Skip Header

Contribute Send feedback
Read comments (?) or add your own

A6QQV6 (ANM7_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length695 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 – 695695Protein arginine N-methyltransferase 7
PRO_0000373901

Sequences

Sequence LengthMass (Da)Tools
A6QQV6 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: D668901147C94E95

FASTA69578,654
        10         20         30         40         50         60 
MKVFCGRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNMKYYQ GIRAAVSRVK 

        70         80         90        100        110        120 
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN 

       130        140        150        160        170        180 
KHSTEVTVGP DGDMPCRANI LITELFDTEL IGEGALPSYE HAHRHLVQAN CEAVPHRATV 

       190        200        210        220        230        240 
YAQLVESRRM WSWNKLFPIR VQTSRGERVI IPPLELERCP GAPSVCDIQL NQVSPADFTI 

       250        260        270        280        290        300 
LSDVLPMFSV DFSKQVSSSA ACHSRQFEPL VSGRAQVVLS WWDIEMDPEG KIKCTMAPSW 

       310        320        330        340        350        360 
AHSDPEELQW RDHWMQCVYF LPQEEPVVQG LALCLVAYHD DYCVWYSLQK TSPEKNGRVH 

       370        380        390        400        410        420 
PVRPVCDCQA HLLWNRPRFG EINDRNRTDQ YIQALRTVLK PDSVCLCVSD GSLLSMLAYH 

       430        440        450        460        470        480 
LGVEQVFTIE NSAVSHRLMK KIFKANHLED KINIIEKRPE LLTPADLEGK KVSLLLGEPF 

       490        500        510        520        530        540 
FTTSLLPWHN LYFWYVRTAV DQHLGPGAVV MPQAASLHVV VVEFRDLWRI RSPCGDCEGF 

       550        560        570        580        590        600 
DVHIMDDMIK RALDFRESKE AEPHPLWEYP CSSLSEPQQI LTFDFRQPVP LQPIHAEGTI 

       610        620        630        640        650        660 
ELRRCGRSHG AVLWMEYHLT ADSTVSTGLL KSAEDEGDCC WNPHCKQAVY FFNTTLDPRA 

       670        680        690 
PPGSSQTVTY TVEFHPHTGD ITMDFTLSDA LDSGC 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC150009 mRNA. Translation: AAI50010.1.
IPIIPI00867369.
RefSeqNP_001095460.1. NM_001101990.1.
UniGeneBt.21927.

3D structure databases

ProteinModelPortalA6QQV6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6QQV6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID514202.
KEGGbta:514202.

Organism-specific databases

CTD54496.

Phylogenomic databases

eggNOGmaNOG09829.
GeneTreeENSGT00530000063495.
InParanoidA6QQV6.
OrthoDBEOG48KR9T.

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...

Entry information

Entry nameANM7_BOVIN
AccessionPrimary (citable) accession number: A6QQV6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: August 21, 2007
Last modified: November 16, 2011
This is version 35 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