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Reviewed, UniProtKB/Swiss-Prot A2AV36 (ANM7_DANRE)

Last modified October 13, 2009. Version 21. 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
ORF Names: ch211-51l3.2
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length683 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.

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity.

Sequence similarities

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

Sequence caution

The sequence AAH44492.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

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 – 683683Protein arginine N-methyltransferase 7
PRO_0000373904

Experimental info

Sequence conflict591V → I in AAH44492. Ref.2
Sequence conflict3481E → K in AAH44492. Ref.2
Sequence conflict3931I → M in AAH44492. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2AV36-1 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 33AB7ED83B972589

FASTA68376,547
        10         20         30         40         50         60 
MKTFCGRANP TTGALDWVEE SEEYDYHQEI ARSCYADMLH DKDRNEKYYE GIRAAVRRVK 

        70         80         90        100        110        120 
ARGERPVVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA QAASCIVERN GFSDKIKIIN 

       130        140        150        160        170        180 
KHSTEVTVGP DGDMQERANI LVTELFDTEL IGEGALPSYE HAHMHLVQTG CEAVPHRATI 

       190        200        210        220        230        240 
YAQLVESDML WKWAQMRPID VDGHRLMPPG AVQECAGAPS VCDIQLSQVP TDAFTAISPV 

       250        260        270        280        290        300 
CTMFSVDFSK PVSSAAQSYT VRFKSQTGGR AQVVLSWWDI DMDPEGNIVC TMAPSWSYAD 

       310        320        330        340        350        360 
PHAYPWRDHW MQSVYFLPAE ENVSEGEELM LMVSHDDYSL WYSLTHSEQN DVRVAPFRPC 

       370        380        390        400        410        420 
CTCQAHLVWT RPRFGELNDE QRTESYVSAL RSILKPDSVC LSVSDGSLLP VFAHLLGSKK 

       430        440        450        460        470        480 
VFSLESSGMA KQVIEQVLHT NSLKDGVQLL GIRAEQLSLA DLDGNQISVL MGEPYFSTSL 

       490        500        510        520        530        540 
LPWHSLFFWY CRTAVAQLLQ PDATILPRAA TLYAVAVEFQ DLWRIRFPCG TCEGFDVSPM 

       550        560        570        580        590        600 
DEMIQRSLDF RESWEAEPHP LWEYPCRALT KPCPVMTFDF TQCVPEQPIS SDGAVPFTGR 

       610        620        630        640        650        660 
GRCHGVALWM EYQLTDDISV SMGLTKAVSQ EGACEWNPHR KQGVFFFRSA KETSGDGRED 

       670        680 
LSYSLTFEPH SGDIKMDFSI TES 

« Hide

References

[1]The Danio rerio sequencing project at the Sanger Institute
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-682.
Strain: AB.
+Additional computationally mapped references.

Cross-references

Sequence databases

AL929309 Genomic DNA. Translation: CAM14259.1.
BC044492 mRNA. Translation: AAH44492.1. Sequence problems.
IPIIPI00482900.
RefSeqNP_956797.2.
UniGeneDr.3855

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSDART00000073609; ENSDARP00000068099; ENSDARG00000051902; Danio rerio. [Genome view]
GeneID393475.
KEGGdre:393475.

Organism-specific databases

CTD393475.
ZFINZDB-GENE-040426-1560. prmt7.

Phylogenomic databases

HOVERGENA2AV36.

Gene expression databases

BgeeA2AV36.

Family and domain databases

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

Entry information

Entry nameANM7_DANRE
AccessionPrimary (citable) accession number: A2AV36
Secondary accession number(s): Q803G6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: February 20, 2007
Last modified: October 13, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectZebrafish annotation project

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