LOCUS       NM_001033666            1692 bp    mRNA    linear   ROD 02-JUN-2024
DEFINITION  Rattus norvegicus destrin, actin depolymerizing factor (Dstn),
            mRNA.
ACCESSION   NM_001033666 XM_578171
VERSION     NM_001033666.1
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 1692)
  AUTHORS   Tedeschi,A., Dupraz,S., Curcio,M., Laskowski,C.J., Schaffran,B.,
            Flynn,K.C., Santos,T.E., Stern,S., Hilton,B.J., Larson,M.J.E.,
            Gurniak,C.B., Witke,W. and Bradke,F.
  TITLE     ADF/Cofilin-Mediated Actin Turnover Promotes Axon Regeneration in
            the Adult CNS
  JOURNAL   Neuron 103 (6), 1073-1085 (2019)
   PUBMED   31400829
  REMARK    GeneRIF: Actin depolymerizing factor (ADF)/cofilin controls actin
            turnover to sustain axon regeneration after spinal cord injury
            through its actin-severing activity. This pinpoints ADF/cofilin as
            a key regulator of axon growth competence, irrespective of
            developmental stage.
REFERENCE   2  (bases 1 to 1692)
  AUTHORS   Tahtamouni,L.H., Shaw,A.E., Hasan,M.H., Yasin,S.R. and Bamburg,J.R.
  TITLE     Non-overlapping activities of ADF and cofilin-1 during the
            migration of metastatic breast tumor cells
  JOURNAL   BMC Cell Biol 14, 45 (2013)
   PUBMED   24093776
  REMARK    GeneRIF: Although ADF and cofilin-1 have many redundant functions,
            each of these proteins has functional differences that affect
            F-actin structures, cell adhesion and lamellipodial dynamics, all
            of which are important determinants of cell migration.
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 1692)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   4  (bases 1 to 1692)
  AUTHORS   Hotulainen,P., Paunola,E., Vartiainen,M.K. and Lappalainen,P.
  TITLE     Actin-depolymerizing factor and cofilin-1 play overlapping roles in
            promoting rapid F-actin depolymerization in mammalian nonmuscle
            cells
  JOURNAL   Mol Biol Cell 16 (2), 649-664 (2005)
   PUBMED   15548599
REFERENCE   5  (bases 1 to 1692)
  AUTHORS   Shultz,M.A., Zhang,L., Gu,Y.Z., Baker,G.L., Fannuchi,M.V.,
            Padua,A.M., Gurske,W.A., Morin,D., Penn,S.G., Jovanovich,S.B.,
            Plopper,C.G. and Buckpitt,A.R.
  TITLE     Gene expression analysis in response to lung toxicants: I.
            Sequencing and microarray development
  JOURNAL   Am J Respir Cell Mol Biol 30 (3), 296-310 (2004)
   PUBMED   12947022
REFERENCE   6  (bases 1 to 1692)
  AUTHORS   Yeoh,S., Pope,B., Mannherz,H.G. and Weeds,A.
  TITLE     Determining the differences in actin binding by human ADF and
            cofilin
  JOURNAL   J Mol Biol 315 (4), 911-925 (2002)
   PUBMED   11812157
REFERENCE   7  (bases 1 to 1692)
  AUTHORS   Vartiainen,M.K., Mustonen,T., Mattila,P.K., Ojala,P.J.,
            Thesleff,I., Partanen,J. and Lappalainen,P.
  TITLE     The three mouse actin-depolymerizing factor/cofilins evolved to
            fulfill cell-type-specific requirements for actin dynamics
  JOURNAL   Mol Biol Cell 13 (1), 183-194 (2002)
   PUBMED   11809832
REFERENCE   8  (bases 1 to 1692)
  AUTHORS   Kanamori,T., Suzuki,M. and Titani,K.
  TITLE     Complete amino acid sequences and phosphorylation sites, determined
            by Edman degradation and mass spectrometry, of rat parotid destrin-
            and cofilin-like proteins
  JOURNAL   Arch Oral Biol 43 (12), 955-967 (1998)
   PUBMED   9877327
REFERENCE   9  (bases 1 to 1692)
  AUTHORS   Hawkins,M., Pope,B., Maciver,S.K. and Weeds,A.G.
  TITLE     Human actin depolymerizing factor mediates a pH-sensitive
            destruction of actin filaments
  JOURNAL   Biochemistry 32 (38), 9985-9993 (1993)
   PUBMED   8399167
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from CB785930.1 and
            CF111187.1.
            
            On Sep 22, 2005 this sequence version replaced XM_578171.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF111187.1, EV774158.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-133               CB785930.1         234-366
            134-1692            CF111187.1         94-1652
FEATURES             Location/Qualifiers
     source          1..1692
                     /organism="Rattus norvegicus"
                     /mol_type="mRNA"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q41"
     gene            1..1692
                     /gene="Dstn"
                     /note="destrin, actin depolymerizing factor"
                     /db_xref="GeneID:502674"
                     /db_xref="RGD:1588366"
     exon            1..124
                     /gene="Dstn"
                     /inference="alignment:Splign:2.1.0"
     CDS             122..619
                     /gene="Dstn"
                     /note="ADF; actin-depolymerizing factor"
                     /codon_start=1
                     /product="destrin"
                     /protein_id="NP_001028838.1"
                     /db_xref="GeneID:502674"
                     /db_xref="RGD:1588366"
                     /translation="MASGVQVADEVCRIFYDMKVRKCSTPEEIKKRKKAVIFCLSADK
                     KCIVVEEGKEILVGDVGVTITDPFKHFVGMLPEKDCRYALYDASFETKESRKEELMFF
                     LWAPEQAPLKSKMIYASSKDAIKKKFPGIKHEYQANGPEDLNRTSIAEKLGGSLIVAF
                     EGSPV"
     exon            125..432
                     /gene="Dstn"
                     /inference="alignment:Splign:2.1.0"
     exon            433..509
                     /gene="Dstn"
                     /inference="alignment:Splign:2.1.0"
     exon            510..1692
                     /gene="Dstn"
                     /inference="alignment:Splign:2.1.0"
ORIGIN      
        1 gcccttaata agctcgagct gccgcgtccg ccctgcgctt cctctcctgc ttttgctacc
       61 gcgaggaaga aggtgcacag actttccgcc aggttcctag ctctcctccc gatccgcgaa
      121 catggcctca ggagttcaag ttgcagatga agtatgtcgt attttctacg acatgaaagt
      181 tcggaaatgc tccacacctg aagaaatcaa gaaaagaaag aaggctgtca ttttttgtct
      241 cagtgcagac aaaaagtgca tagtcgttga agaaggcaaa gagatcttgg ttggagatgt
      301 cggcgttacc ataactgatc ctttcaagca ttttgtggga atgcttcctg aaaaagattg
      361 tcgctacgct ttgtatgatg ccagctttga aaccaaggag tccagaaaag aagagctcat
      421 gttcttcttg tgggcaccag aacaagcacc tctgaaaagt aaaatgatct atgcaagctc
      481 gaaggacgcc atcaagaaga aatttccagg tataaagcac gagtatcaag caaatgggcc
      541 agaagacctc aatcggacta gtattgctga aaagctaggt ggctccttaa ttgtagcgtt
      601 cgaaggatcc cctgtgtaga ttatcagtca gtgccacgaa ttgaaagctt ccatatttaa
      661 cactatcctt tcactatata agtaaagcaa atatattagg ccaggatctc actgagggga
      721 atttgtcttg tcatctttta gagtaaacta aaaattttat agtgtctgca aatactaccc
      781 tacataaatc tagcctctaa agtttcattg gtgtggaatt aaattcttat tggccaaatg
      841 cctattttca tgaagtgact tgtaaagatt ttgttaagct caggattttt aataacacag
      901 ttcacaaaac agtacaaggc aatgtgaggg gaactactaa tctttgctaa cctcagcagt
      961 tactttgttt cttttgttta gaaaagtgat tgtaatctgt gtatcatttt gacccaaatt
     1021 ctctattttt ccttgactta aacagaataa tgagatataa ttttctttat actgtgtaca
     1081 acacctaatc tatactaaca gcaataagac taagccaggc agtcttaatt ctatcagatg
     1141 tgtcatgaga ctgtttcaga ctcgcgtctg cttaaagttc acgctcatct tgcaaagcgc
     1201 cagagcaccg tgctggagtg cagtcagtgc cctgtacctg ccgcaagagg ctcgctgggc
     1261 tgggagatgg cgtagagcaa ctttctgtct tagaaatcat ggtgatcctc aggagaatgc
     1321 tccgtgtctt gtaacaacta attacattgc aaattagggc ttcattgtaa tctactttat
     1381 taatgaaaaa tgacaaggca gtgtactgat aagccaaggt gctttcgatc tgtaatctct
     1441 tcttcaaaac tgctgtgtct ggtacagtag actggaaaga gtgttgatta tgtttcctct
     1501 ggggcctggt agggtgcaaa tgcctagagc agtttaccag ctgtgtgtga gacagaagca
     1561 gtaccatgga tgacacaggg gactgcccaa caacacttgg aaatgatggt taccatcaca
     1621 ggcatgacac tgaacactgt agaggtgcac agtcagttga acttagtagc agtgctggct
     1681 ttatgtaata aa
//
