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Database: UniProt
Entry: A0A287CS17_ICTTR
LinkDB: A0A287CS17_ICTTR
Original site: A0A287CS17_ICTTR 
ID   A0A287CS17_ICTTR        Unreviewed;       371 AA.
AC   A0A287CS17;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=type I protein arginine methyltransferase {ECO:0000256|ARBA:ARBA00011925};
DE            EC=2.1.1.319 {ECO:0000256|ARBA:ARBA00011925};
GN   Name=PRMT1 {ECO:0000313|Ensembl:ENSSTOP00000024079.1};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000024079.1, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000024079.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC         Evidence={ECO:0000256|ARBA:ARBA00036963};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC         Evidence={ECO:0000256|ARBA:ARBA00036963};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:65280;
CC         Evidence={ECO:0000256|ARBA:ARBA00036919};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC         Evidence={ECO:0000256|ARBA:ARBA00036919};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-methionine
CC         = H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + S-adenosyl-
CC         L-homocysteine; Xref=Rhea:RHEA:48104, Rhea:RHEA-COMP:11990,
CC         Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61897, ChEBI:CHEBI:65280;
CC         Evidence={ECO:0000256|ARBA:ARBA00035899};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48105;
CC         Evidence={ECO:0000256|ARBA:ARBA00035899};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Nucleus, nucleoplasm
CC       {ECO:0000256|ARBA:ARBA00004642}.
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DR   EMBL; AGTP01089717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005336744.1; XM_005336687.1.
DR   AlphaFoldDB; A0A287CS17; -.
DR   SMR; A0A287CS17; -.
DR   STRING; 43179.ENSSTOP00000024079; -.
DR   Ensembl; ENSSTOT00000036214.1; ENSSTOP00000024079.1; ENSSTOG00000025543.2.
DR   GeneID; 101962619; -.
DR   CTD; 3276; -.
DR   eggNOG; KOG1499; Eukaryota.
DR   GeneTree; ENSGT00940000154700; -.
DR   InParanoid; A0A287CS17; -.
DR   OMA; KPNVRNN; -.
DR   OrthoDB; 197898at2759; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0034709; C:methylosome; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0044020; F:histone H4R3 methyltransferase activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0008327; F:methyl-CpG binding; IEA:Ensembl.
DR   GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IEA:Ensembl.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:Ensembl.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:Ensembl.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:Ensembl.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; IEA:Ensembl.
DR   GO; GO:0008380; P:RNA splicing; IEA:Ensembl.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11006; PROTEIN ARGININE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11006:SF54; PROTEIN ARGININE N-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01015};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01015}.
FT   DOMAIN          92..189
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13649"
SQ   SEQUENCE   371 AA;  42462 MW;  544349801B0E1396 CRC64;
     MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF
     GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS
     SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLYA
     RDKWLAPDGL IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV
     DPKQLVTNAC LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG
     FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC
     ELSCSTDYRM R
//
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