Q8AV13 (ANM1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein arginine N-methyltransferase 1-A
Short name=xPRMT1
EC=2.1.1.-

Alternative name(s):
Histone-arginine N-methyltransferase PRMT1-A
EC=2.1.1.125

Gene names

Name:	prmt1-a
Synonyms:	prmt1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
Subunit structure	Component of a complex with lsm14a/rap55a. Interacts with cirbp. Ref.1 Ref.4
Subcellular location	Nucleus By similarity. Cytoplasm › cytosol By similarity UniProtKB Q99873.
Developmental stage	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
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.
Sequence caution	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.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	S-adenosyl-L-methionine
Molecular function	Activator Developmental protein Methyltransferase Transferase
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW metamorphosis Inferred from mutant phenotype Ref.5. Source: UniProtKB negative regulation of megakaryocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.5. Source: UniProtKB regulation of histone modification Inferred from mutant phenotype Ref.5. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from physical interaction Ref.4. Source: UniProtKB
Molecular_function	histone methyltransferase activity (H4-R3 specific) Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Inferred from mutant phenotype Ref.5. Source: UniProtKB
Complete GO annotation...

Alternative products

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:
     11-28: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	Protein arginine N-methyltransferase 1-A		PRO_0000391365
Sites
	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
Natural variations
	Alternative sequence	11 – 28	18	Missing in isoform 2. Ref.2		VSP_053193

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 820402CA2A28DF11	FASTA	369	42,325
	10 20 30 40 50 60 MAEATTCNME NFVAKLANGM SLRTPIEDVN SAPPEGGVKT NAEDMTSKDY YFDSYAHFGI 70 80 90 100 110 120 HEEMLKDEVR TLTYRNSMFH NRHLFKDKVV LDVGSGTGIL CMFAAKAGAK KVIGIECSSI 130 140 150 160 170 180 SDYAIKIVKA NKLDHVVTII KGKVEEVELP VEKVDIIISE WMGYCLFYES MLNTVIYARD 190 200 210 220 230 240 KWLTPDGLIF PDRATLYITA IEDRQYKDYK IHWWENVYGF DMSCIKDVAI KEPLVDVVDP 250 260 270 280 290 300 KQLVSNACLI KEVDIYTVKV DDLSFTSPFC LQVKRNDYIH ALVAYFNIEF TRCHKRTGFS 310 320 330 340 350 360 TSPESPYTHW KQTVFYMEDY LTVKTGEEIF GTIGMKPNAK NNRDLDFTFD IDFKGQLCEL SCSTDYRMR
	Isoform 2 [UniParc]. Checksum: C5648769F39E312E	FASTA	351	40,366
	10 20 30 40 50 60 MAEATTCNME VNSAPPEGGV KTNAEDMTSK DYYFDSYAHF GIHEEMLKDE VRTLTYRNSM 70 80 90 100 110 120 FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG AKKVIGIECS SISDYAIKIV KANKLDHVVT 130 140 150 160 170 180 IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVIYA RDKWLTPDGL IFPDRATLYI 190 200 210 220 230 240 TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV DPKQLVSNAC LIKEVDIYTV 250 260 270 280 290 300 KVDDLSFTSP FCLQVKRNDY IHALVAYFNI EFTRCHKRTG FSTSPESPYT HWKQTVFYME 310 320 330 340 350 DYLTVKTGEE IFGTIGMKPN AKNNRDLDFT FDIDFKGQLC ELSCSTDYRM R

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. Tissue: Oocyte.
[2]	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.
[3]	"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.
[4]	"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.
[5]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
UniGene	Xl.23295.
3D structure databases
HSSP	HSSP built from PDB template 1ORH based on UniProtKB Q63009.
ProteinModelPortal	Q8AV13.
SMR	Q8AV13. Positions 54-369.
ModBase	Search...
Proteomic databases
PRIDE	Q8AV13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399121.
KEGG	xla:399121.
Organism-specific databases
CTD	399121.
Xenbase	XB-GENE-6254417. prmt1.
Phylogenomic databases
HOVERGEN	HBG001793.
KO	K11434.
Family and domain databases
InterPro	IPR025799. Arg_MeTrfase. IPR025714. Methyltranfer_dom. [Graphical view]
PANTHER	PTHR11006. PTHR11006. 1 hit.
Pfam	PF13847. Methyltransf_31. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANM1A_XENLA

Accession

Primary (citable) accession number: Q8AV13
Secondary accession number(s): Q7SY97, Q7ZY05

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 9, 2010
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program