LOCUS       NM_024363               1201 bp    mRNA    linear   ROD 10-FEB-2025
DEFINITION  Rattus norvegicus protein arginine methyltransferase 1 (Prmt1),
            mRNA.
ACCESSION   NM_024363
VERSION     NM_024363.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (bases 1 to 1201)
  AUTHORS   Shen,Q., Xiao,Y., Cheng,B., Sun,Z., Hu,Y., Yang,H. and Luo,Y.
  TITLE     PRMT1 promotes extracellular matrix degradation and apoptosis of
            chondrocytes in temporomandibular joint osteoarthritis via the
            AKT/FOXO1 signaling pathway
  JOURNAL   Int J Biochem Cell Biol 141, 106112 (2021)
   PUBMED   34715362
  REMARK    GeneRIF: PRMT1 promotes extracellular matrix degradation and
            apoptosis of chondrocytes in temporomandibular joint osteoarthritis
            via the AKT/FOXO1 signaling pathway.
REFERENCE   2  (bases 1 to 1201)
  AUTHORS   Price,O.M., Thakur,A., Ortolano,A., Towne,A., Velez,C., Acevedo,O.
            and Hevel,J.M.
  TITLE     Naturally occurring cancer-associated mutations disrupt
            oligomerization and activity of protein arginine methyltransferase
            1 (PRMT1)
  JOURNAL   J Biol Chem 297 (5), 101336 (2021)
   PUBMED   34688662
  REMARK    GeneRIF: Naturally occurring cancer-associated mutations disrupt
            oligomerization and activity of protein arginine methyltransferase
            1 (PRMT1).
REFERENCE   3  (bases 1 to 1201)
  AUTHORS   Ma,J., Wu,Y. and He,Y.
  TITLE     Silencing circRNA LRP6 down-regulates PRMT1 to improve the
            streptozocin-induced pancreatic beta-cell injury and insulin
            secretion by sponging miR-9-5p
  JOURNAL   J Bioenerg Biomembr 53 (3), 333-342 (2021)
   PUBMED   33826088
  REMARK    GeneRIF: Silencing circRNA LRP6 down-regulates PRMT1 to improve the
            streptozocin-induced pancreatic beta-cell injury and insulin
            secretion by sponging miR-9-5p.
REFERENCE   4  (bases 1 to 1201)
  AUTHORS   Zhu,Y., Yu,C. and Zhuang,S.
  TITLE     Protein arginine methyltransferase 1 mediates renal fibroblast
            activation and fibrogenesis through activation of Smad3 signaling
  JOURNAL   Am J Physiol Renal Physiol 318 (2), F375-F387 (2020)
   PUBMED   31813251
  REMARK    GeneRIF: PRMT1 may mediate renal fibroblast activation and renal
            fibrosis development through activation of the TGF-beta/Smad3
            signaling pathway.
REFERENCE   5  (bases 1 to 1201)
  AUTHORS   Jeong,M.H., Jeong,H.J., Ahn,B.Y., Pyun,J.H., Kwon,I., Cho,H. and
            Kang,J.S.
  TITLE     PRMT1 suppresses ATF4-mediated endoplasmic reticulum response in
            cardiomyocytes
  JOURNAL   Cell Death Dis 10 (12), 903 (2019)
   PUBMED   31787756
  REMARK    GeneRIF: PRMT1 suppresses ATF4-mediated endoplasmic reticulum
            response in cardiomyocytes.
            Erratum:[Cell Death Dis. 2020 Mar 23;11(3):203. doi:
            10.1038/s41419-020-2373-8.. PMID: 32251281]
            Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1201)
  AUTHORS   Pawlak,M.R., Scherer,C.A., Chen,J., Roshon,M.J. and Ruley,H.E.
  TITLE     Arginine N-methyltransferase 1 is required for early
            postimplantation mouse development, but cells deficient in the
            enzyme are viable
  JOURNAL   Mol Cell Biol 20 (13), 4859-4869 (2000)
   PUBMED   10848611
REFERENCE   7  (bases 1 to 1201)
  AUTHORS   Tang,J., Kao,P.N. and Herschman,H.R.
  TITLE     Protein-arginine methyltransferase I, the predominant
            protein-arginine methyltransferase in cells, interacts with and is
            regulated by interleukin enhancer-binding factor 3
  JOURNAL   J Biol Chem 275 (26), 19866-19876 (2000)
   PUBMED   10749851
REFERENCE   8  (bases 1 to 1201)
  AUTHORS   Tang,J., Gary,J.D., Clarke,S. and Herschman,H.R.
  TITLE     PRMT 3, a type I protein arginine N-methyltransferase that differs
            from PRMT1 in its oligomerization, subcellular localization,
            substrate specificity, and regulation
  JOURNAL   J Biol Chem 273 (27), 16935-16945 (1998)
   PUBMED   9642256
REFERENCE   9  (bases 1 to 1201)
  AUTHORS   Lin,W.J., Gary,J.D., Yang,M.C., Clarke,S. and Herschman,H.R.
  TITLE     The mammalian immediate-early TIS21 protein and the
            leukemia-associated BTG1 protein interact with a protein-arginine
            N-methyltransferase
  JOURNAL   J Biol Chem 271 (25), 15034-15044 (1996)
   PUBMED   8663146
REFERENCE   10 (bases 1 to 1201)
  AUTHORS   Gary,J.D., Lin,W.J., Yang,M.C., Herschman,H.R. and Clarke,S.
  TITLE     The predominant protein-arginine methyltransferase from
            Saccharomyces cerevisiae
  JOURNAL   J Biol Chem 271 (21), 12585-12594 (1996)
   PUBMED   8647869
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U60882.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U60882.1, FQ219843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760396, SAMN06621351
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1201
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q22"
     gene            1..1201
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /note="protein arginine methyltransferase 1"
                     /db_xref="GeneID:60421"
                     /db_xref="RGD:62020"
     exon            1..38
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     CDS             3..1064
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /EC_number="2.1.1.319"
                     /function="methylates (mono and asymmetric dimethylation)
                     the guanidino nitrogens of arginyl residues present in a
                     glycine and arginine-rich domain; (e.g. can methylate
                     recombinant hnRNPA1 as well as crude histones)"
                     /note="histone-arginine N-methyltransferase PRMT1;
                     heterogeneous nuclear ribonucleoproteins
                     methyltransferase-like 2"
                     /codon_start=1
                     /product="protein arginine N-methyltransferase 1"
                     /protein_id="NP_077339.1"
                     /db_xref="GeneID:60421"
                     /db_xref="RGD:62020"
                     /translation="MAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGI
                     HEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS
                     SISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVL
                     HARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPL
                     VDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTR
                     CHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTID
                     LDFKGQLCELSCSTDYRMR"
     exon            39..140
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            141..296
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            297..360
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            361..503
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            504..591
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            592..707
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            708..858
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            859..980
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     exon            981..1201
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /inference="alignment:Splign:2.1.0"
     polyA_site      1201
                     /gene="Prmt1"
                     /gene_synonym="Hrmt1l2"
                     /note="109 A nucleotides"
ORIGIN      
        1 agatggcggc agccgaggcc gcgaactgca tcatggaggt ttcctgtggc caagcagaaa
       61 gtagtgagaa gcccaatgct gaggacatga catccaaaga ctactacttt gactcctatg
      121 cccactttgg catccacgag gagatgctaa aggatgaggt gcgaaccctc acgtaccgca
      181 actccatgtt tcacaatcgg catctcttca aagacaaggt ggtgctggat gtgggctcgg
      241 gcactggcat cctctgcatg ttcgctgcca aggcaggggc ccgcaaggtc attgggatcg
      301 agtgctccag tatctctgat tatgctgtga agattgtcaa agccaataag ttagaccacg
      361 tggtgaccat catcaagggc aaggtggagg aggtggagct gcctgtggag aaggtggaca
      421 tcatcatcag cgagtggatg ggttattgcc tcttctatga gtccatgctc aacactgtgc
      481 tgcacgctcg tgacaagtgg ctggcacctg atggcctcat cttcccagac cgagccaccc
      541 tgtatgtgac agccattgag gaccgacagt ataaagacta caagatccac tggtgggaga
      601 atgtatatgg ctttgatatg tcctgcatta aagacgtggc catcaaggag cccctggtgg
      661 acgtggtgga cccaaagcag ctggtcacca acgcctgcct cataaaggag gtggacatct
      721 acacagtcaa ggtggaggac ctgaccttca cctccccgtt ttgtctgcaa gtgaagagga
      781 atgactatgt gcatgcacta gtggcctact tcaacatcga gttcacccga tgccacaaga
      841 ggaccggctt ctctaccagt cctgagtctc catacacaca ttggaagcag actgtgttct
      901 acatggagga ctacctaaca gtgaagaccg gcgaggagat ttttggcact attggaatga
      961 ggcccaacgc caaaaacaat cgtgacttgg actttaccat cgacctggac ttcaagggtc
     1021 agctgtgtga gctctcttgt tccaccgact accggatgcg ctgaggaggt gccaggctgg
     1081 ccctcctgca aaagggggct caggggctgg gcttggggga tgggagggta catcgtggca
     1141 gtgtttttca taacttatgt ttttatatgg ttgcgtttat gccaataaat cctcagctga
     1201 c
//
