Skip Header

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

Q6PCI6 (ANM7_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 49. 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
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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length685 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.

Subcellular location

Cytoplasm › cytosol 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 – 685685Protein arginine N-methyltransferase 7
PRO_0000373905

Sequences

Sequence LengthMass (Da)Tools
Q6PCI6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: A6FCA5A47A78EFF8

FASTA68577,291
        10         20         30         40         50         60 
MKVFCGRVNP TTGAMDWVEE DEHYDYHQEI ARSSYADMLH DKDRNEKYYQ GICAAVRRVK 

        70         80         90        100        110        120 
QRGQEAVVLD IGTGTGLLSM MAVTAGADCC YAIEVFKPMS DAAVQIVKAN GFSDKIKVIN 

       130        140        150        160        170        180 
KHSTEVTVGP DGDMKTKANI LITELFDTEL IGEGALPSYE HAQHNLMQET WEAVPHRATV 

       190        200        210        220        230        240 
FAQLVESTRL WSWNKLFPLN LETGDIKPHP ELETCPGAPS VCDIQLSQLN PRDFKILSEV 

       250        260        270        280        290        300 
LCVFRVDFSC QVSSAPTSHP VHFTSLASGA AQVVLSWWEI DMDPDGSITC TMQPSWMYET 

       310        320        330        340        350        360 
QQSVPWRDHW MQCVYFLPKE CSVTQGEVCC LTAHQDDYCV WYSLNKSSAE NDPVCRERPT 

       370        380        390        400        410        420 
CHCGAHITWN RARFGELNDR HRTQQYFEAL KKVVTPSSTC LCVSDGSLLP VLAHSLGAKQ 

       430        440        450        460        470        480 
IYTLESSSIA QHLMKKLFQV NHLGEKIQVL HKSADSLITA DFEDRKISTL IGEPFFTTNL 

       490        500        510        520        530        540 
LPWHNLYFWY SRTALSTNLA KDCTVLPLSA SLHVVAVEFK DLWRIRSPCG MCEGFDVSIM 

       550        560        570        580        590        600 
DKMIKNSLNF RESQEAEPHP LWEYPCRALS EPIQVMTFNF TEPVPTEEIR ASGSLNLVRS 

       610        620        630        640        650        660 
GQCHGAVLWM VYELTKEITV STGLIGISEE MGECQWYPHR KQGVYFFSSI LNPQTIPAQS 

       670        680 
PSSVSYSVTF IPKEGDIRMC FEPDF

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC059311 mRNA. Translation: AAH59311.1.
RefSeqNP_001080010.1. NM_001086541.1.
UniGeneXl.29881.

3D structure databases

ProteinModelPortalQ6PCI6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID379700.
KEGGxla:379700.

Organism-specific databases

CTD54496.
XenbaseXB-GENE-974631. prmt7.

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_XENLA
AccessionPrimary (citable) accession number: Q6PCI6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 49 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents