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A2AV36 (ANM7_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 41. 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
ORF Names:ch211-51l3.2
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length683 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 caution

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

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 [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

EMBL
GenBank
DDBJ		AL929309 Genomic DNA. Translation: CAM14259.1.
BC044492 mRNA. Translation: AAH44492.1. Sequence problems.
IPIIPI00482900.
RefSeqNP_956797.2. NM_200503.2.
UniGeneDr.3855.

3D structure databases

ProteinModelPortalA2AV36.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2AV36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000073609; ENSDARP00000068099; ENSDARG00000051902.
GeneID393475.
KEGGdre:393475.

Organism-specific databases

CTD54496.
ZFINZDB-GENE-040426-1560. prmt7.

Phylogenomic databases

eggNOGfiNOG04979.
GeneTreeENSGT00530000063495.
HOGENOMHBG377790.
InParanoidA2AV36.
OMAYDIQLNQ.
OrthoDBEOG48KR9T.

Gene expression databases

ArrayExpressA2AV36.
BgeeA2AV36.

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_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: November 16, 2011
This is version 41 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

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