Q8AV13 (ANM1A_XENLA) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 45. History...
Names and origin
|Protein names||Recommended name:|
Protein arginine N-methyltransferase 1-A
Histone-arginine N-methyltransferase PRMT1-A
|Organism||Xenopus laevis (African clawed frog)|
|Taxonomic identifier||8355 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus|
|Sequence length||369 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Methylates ilf3 to regulate its DNA-binding activity. Required for neural induction, playing a key role in the control of epidermal versus neural cell fate choice. Methylates cirbp to regulate its subcellular location. Acts transiently during metamorphosis as a transcription coactivator, enhancing thyroid hormone (T3) receptor (TR)-mediated transcription by enhancing TR binding to the T3 response element (TRE), and histone modification through recruitment of other coactivators. Ref.1 Ref.5
S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
Expressed both maternally and zygotically. Expressed in oocytes (at protein level). Up-regulated during metamorphosis, peaking at stage 62 before dramatically reducing by the end of metamorphosis (stage 66). Ref.3 Ref.5
Belongs to the protein arginine N-methyltransferase family.
The sequence AAH44033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH54955.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
|This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]|
|Isoform 1 Ref.1 (identifier: Q8AV13-1) |
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
|Isoform 2 Ref.2 (identifier: Q8AV13-2) |
The sequence of this isoform differs from the canonical sequence as follows:
|Note: No experimental confirmation available.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 369||369||Protein arginine N-methyltransferase 1-A||PRO_0000391365|
|Active site||160||1||By similarity|
|Active site||169||1||By similarity|
|Binding site||61||1||S-adenosyl-L-methionine By similarity|
|Binding site||70||1||S-adenosyl-L-methionine By similarity|
|Binding site||94||1||S-adenosyl-L-methionine; via carbonyl oxygen By similarity|
|Binding site||116||1||S-adenosyl-L-methionine By similarity|
|Binding site||145||1||S-adenosyl-L-methionine By similarity|
|Alternative sequence||11 – 28||18||Missing in isoform 2. Ref.2||VSP_053193|
|||"Methylation of Xenopus CIRP2 regulates its arginine- and glycine-rich region-mediated nucleocytoplasmic distribution."|
Aoki K., Ishii Y., Matsumoto K., Tsujimoto M.
Nucleic Acids Res. 30:5182-5192(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CIRBP.
|||NIH - Xenopus Gene Collection (XGC) project|
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Tadpole and Tail bud.
|||"Cross-species hybridizations on a multi-species cDNA microarray to identify evolutionarily conserved genes expressed in oocytes."|
Vallee M., Robert C., Methot S., Palin M.F., Sirard M.A.
BMC Genomics 7:113-113(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
|||"RAP55, a cytoplasmic mRNP component, represses translation in Xenopus oocytes."|
Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.
J. Biol. Chem. 281:40096-40106(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH LSM14A.
|||"Novel functions of protein arginine methyltransferase 1 in thyroid hormone receptor-mediated transcription and in the regulation of metamorphic rate in Xenopus laevis."|
Matsuda H., Paul B.D., Choi C.Y., Hasebe T., Shi Y.B.
Mol. Cell. Biol. 29:745-757(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
|AB085173 mRNA. Translation: BAC53990.1.|
BC044033 mRNA. Translation: AAH44033.1. Different initiation.
BC054955 mRNA. Translation: AAH54955.1. Different initiation.
|RefSeq||NP_001083793.1. NM_001090324.1. |
3D structure databases
|HSSP||HSSP built from PDB template 1ORH based on UniProtKB Q63009. |
|SMR||Q8AV13. Positions 54-369. |
Protocols and materials databases
Genome annotation databases
|Xenbase||XB-GENE-6254417. prmt1. |
Family and domain databases
|InterPro||IPR025799. Arg_MeTrfase. |
|PANTHER||PTHR11006. PTHR11006. 1 hit. |
|Pfam||PF13847. Methyltransf_31. 1 hit. |
|Accession||Primary (citable) accession number: Q8AV13|
Secondary accession number(s): Q7SY97, Q7ZY05
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families