LOCUS NP_001028838 165 aa linear ROD 31-AUG-2026
DEFINITION destrin [Rattus norvegicus].
ACCESSION NP_001028838 XP_578171
VERSION NP_001028838.1
DBSOURCE REFSEQ: accession 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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 (residues 1 to 165)
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 XP_578171.1.
##Evidence-Data-START##
Transcript exon combination :: CF111187.1, EV774158.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMD01647510, SAMD01647522
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on single protein-coding transcript
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..165
/organism="Rattus norvegicus"
/db_xref="taxon:10116"
/chromosome="3"
/map="3q41"
Protein 1..165
/product="destrin"
/note="ADF; actin-depolymerizing factor"
/calculated_mol_wt=18403
Site 2
/site_type="acetylation"
/note="N-acetylalanine.
/evidence=ECO:0000269|PubMed:9877327, ECO:0000269|Ref.4;
propagated from UniProtKB/Swiss-Prot (Q7M0E3.3)"
Region 3..152
/region_name="ADF_cofilin_like"
/note="Cofilin, Destrin, and related actin depolymerizing
factors; cd11286"
/db_xref="CDD:200442"
Site 3..4
/site_type="other"
/note="putative G-actin interface [polypeptide binding]"
/db_xref="CDD:200442"
Site 3
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:9877327,
ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (Q7M0E3.3)"
Site 19
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:P60981; propagated from
UniProtKB/Swiss-Prot (Q7M0E3.3)"
Region 30..34
/region_name="Nuclear localization signal.
/evidence=ECO:0000255"
/note="propagated from UniProtKB/Swiss-Prot (Q7M0E3.3)"
Site order(96,98,112,139,142)
/site_type="other"
/note="putative F-actin interface [polypeptide binding]"
/db_xref="CDD:200442"
CDS 1..165
/gene="Dstn"
/coded_by="NM_001033666.1:122..619"
/db_xref="GeneID:502674"
/db_xref="RGD:1588366"
ORIGIN
1 masgvqvade vcrifydmkv rkcstpeeik krkkavifcl sadkkcivve egkeilvgdv
61 gvtitdpfkh fvgmlpekdc ryalydasfe tkesrkeelm fflwapeqap lkskmiyass
121 kdaikkkfpg ikheyqangp edlnrtsiae klggslivaf egspv
//
