DREB_MOUSE
ID DREB_MOUSE Reviewed; 706 AA.
AC Q9QXS6; A2CG16; Q3V234; Q922X1; Q9QXS5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Drebrin;
DE AltName: Full=Developmentally-regulated brain protein;
GN Name=Dbn1; Synonyms=Drba;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND E2), AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=10633083; DOI=10.1242/jcs.113.2.325;
RA Keon B.H., Jedrzejewski P.T., Paul D.L., Goodenough D.A.;
RT "Isoform specific expression of the neuronal F-actin binding protein,
RT drebrin, in specialized cells of stomach and kidney epithelia.";
RL J. Cell Sci. 113:325-336(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A2).
RC STRAIN=ICR;
RX PubMed=11991718; DOI=10.1006/geno.2002.6764;
RA Jin M., Tanaka S., Sekino Y., Ren Y., Yamazaki H., Kawai-Hirai R.,
RA Kojima N., Shirao T.;
RT "A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal mapping,
RT genomic structure, expression, and functional characterization.";
RL Genomics 79:686-692(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-683 (ISOFORM A).
RC STRAIN=C57BL/6 X CBA;
RA Shirao T., Kawai-Hirai R.;
RT "Mouse genome for drebrin.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-10; 43-71; 140-147; 150-165; 178-185; 272-291 AND
RP 376-402, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-383; SER-385;
RP SER-393; THR-394 AND SER-658, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH RUFY3, AND SUBCELLULAR LOCATION.
RX PubMed=24720729; DOI=10.1111/jnc.12740;
RA Wei Z., Sun M., Liu X., Zhang J., Jin Y.;
RT "Rufy3, a protein specifically expressed in neurons, interacts with actin-
RT bundling protein Fascin to control the growth of axons.";
RL J. Neurochem. 130:678-692(2014).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25865831; DOI=10.1111/jnc.13119;
RA Jung G., Kim E.J., Cicvaric A., Sase S., Groeger M., Hoeger H.,
RA Sialana F.J., Berger J., Monje F.J., Lubec G.;
RT "Drebrin depletion alters neurotransmitter receptor levels in protein
RT complexes, dendritic spine morphogenesis and memory-related synaptic
RT plasticity in the mouse hippocampus.";
RL J. Neurochem. 134:327-339(2015).
CC -!- FUNCTION: Actin cytoskeleton-organizing protein that plays a role in
CC the formation of cell projections (By similarity). Required for actin
CC polymerization at immunological synapses (IS) and for the recruitment
CC of the chemokine receptor CXCR4 to IS (By similarity). Plays a role in
CC dendritic spine morphogenesis and organization, including the
CC localization of the dopamine receptor DRD1 to the dendritic spines
CC (PubMed:25865831). Involved in memory-related synaptic plasticity in
CC the hippocampus (PubMed:25865831). {ECO:0000250|UniProtKB:Q16643,
CC ECO:0000269|PubMed:25865831}.
CC -!- SUBUNIT: Interacts with RUFY3 (PubMed:24720729). Interacts with CXCR4;
CC this interaction is enhanced by antigenic stimulation (By similarity).
CC Interacts (via ADF-H domain) with ZMYND8 (via PHD-type Zinc finger,
CC Bromo and PWWP domains); the interaction leads to sequestering of
CC ZMYND8 in the cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:Q16643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16643}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q16643}. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:Q16643}. Cell junction
CC {ECO:0000250|UniProtKB:Q16643}. Cell projection
CC {ECO:0000269|PubMed:24720729}. Cell projection, growth cone
CC {ECO:0000269|PubMed:24720729}. Note=In the absence of antigen, evenly
CC distributed throughout subcortical regions of the T-cell membrane and
CC cytoplasm. In the presence of antigen, distributes to the immunological
CC synapse forming at the T-cell-APC contact area, where it localizes at
CC the peripheral and distal supramolecular activation clusters (SMAC) (By
CC similarity). Colocalized with RUFY3 and F-actin at the transitional
CC domain of the axonal growth cone (PubMed:24720729).
CC {ECO:0000250|UniProtKB:Q16643, ECO:0000269|PubMed:24720729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=A;
CC IsoId=Q9QXS6-1; Sequence=Displayed;
CC Name=A2;
CC IsoId=Q9QXS6-2; Sequence=VSP_004199, VSP_004200;
CC Name=E2;
CC IsoId=Q9QXS6-3; Sequence=VSP_004198;
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus, with expression in
CC the pyramidal cells of CA1, CA2 and CA3 and in the granule cells of the
CC dentate gyrus (at protein level) (PubMed:25865831). Highly expressed in
CC brain, also present in stomach and to a lesser degree in kidney, colon,
CC and urinary bladder (PubMed:10633083). The E2 isoform is specifically
CC expressed in adult stomach, kidney, and cultured cells
CC (PubMed:10633083). {ECO:0000269|PubMed:10633083,
CC ECO:0000269|PubMed:25865831}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian frequency
CC (PubMed:25865831). Mutant mice exhibit significant reduction of
CC dendritic spine numbers, altered dendritic spine morphology with a
CC reduction in the number of mushroom, thin and stubby types of dendritic
CC spines, decreased protein levels of the neurotransmitter receptors
CC DRD1, DRD2, HTR1A and 5HT7R and reduced numbers of DRD1 receptors on
CC dendritic spines (PubMed:25865831). Inhibited memory-related high-
CC frequency-induced synaptic strengthening (PubMed:25865831).
CC {ECO:0000269|PubMed:25865831}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF187147; AAF25189.1; -; mRNA.
DR EMBL; AF187148; AAF25190.1; -; mRNA.
DR EMBL; AB064321; BAB86904.1; -; mRNA.
DR EMBL; AK132060; BAE20965.1; -; mRNA.
DR EMBL; CT009762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006714; AAH06714.1; -; mRNA.
DR EMBL; AB028740; BAB87811.1; -; Genomic_DNA.
DR CCDS; CCDS36677.1; -. [Q9QXS6-3]
DR CCDS; CCDS49274.1; -. [Q9QXS6-1]
DR RefSeq; NP_001170842.1; NM_001177371.1. [Q9QXS6-1]
DR RefSeq; NP_001170843.1; NM_001177372.1.
DR RefSeq; NP_062787.2; NM_019813.4. [Q9QXS6-3]
DR AlphaFoldDB; Q9QXS6; -.
DR SMR; Q9QXS6; -.
DR BioGRID; 207900; 30.
DR IntAct; Q9QXS6; 20.
DR MINT; Q9QXS6; -.
DR STRING; 10090.ENSMUSP00000021950; -.
DR iPTMnet; Q9QXS6; -.
DR PhosphoSitePlus; Q9QXS6; -.
DR SwissPalm; Q9QXS6; -.
DR jPOST; Q9QXS6; -.
DR MaxQB; Q9QXS6; -.
DR PaxDb; Q9QXS6; -.
DR PeptideAtlas; Q9QXS6; -.
DR PRIDE; Q9QXS6; -.
DR ProteomicsDB; 277496; -. [Q9QXS6-1]
DR ProteomicsDB; 277497; -. [Q9QXS6-2]
DR ProteomicsDB; 277498; -. [Q9QXS6-3]
DR Antibodypedia; 3641; 343 antibodies from 37 providers.
DR DNASU; 56320; -.
DR Ensembl; ENSMUST00000021950; ENSMUSP00000021950; ENSMUSG00000034675. [Q9QXS6-1]
DR Ensembl; ENSMUST00000109923; ENSMUSP00000105549; ENSMUSG00000034675. [Q9QXS6-3]
DR GeneID; 56320; -.
DR KEGG; mmu:56320; -.
DR UCSC; uc007qrc.2; mouse. [Q9QXS6-1]
DR CTD; 1627; -.
DR MGI; MGI:1931838; Dbn1.
DR VEuPathDB; HostDB:ENSMUSG00000034675; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000159431; -.
DR HOGENOM; CLU_013085_3_0_1; -.
DR InParanoid; Q9QXS6; -.
DR OMA; FAQSDEC; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; Q9QXS6; -.
DR TreeFam; TF318935; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 56320; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dbn1; mouse.
DR PRO; PR:Q9QXS6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QXS6; protein.
DR Bgee; ENSMUSG00000034675; Expressed in cortical plate and 234 other tissues.
DR ExpressionAtlas; Q9QXS6; baseline and differential.
DR Genevisible; Q9QXS6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0032279; C:asymmetric synapse; ISO:MGI.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0044308; C:axonal spine; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:1902737; C:dendritic filopodium; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0005921; C:gap junction; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0044309; C:neuron spine; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0140661; F:cytoskeletal motor inhibitor activity; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0010643; P:cell communication by chemical coupling; IMP:MGI.
DR GO; GO:0010644; P:cell communication by electrical coupling; IMP:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISS:UniProtKB.
DR GO; GO:0048699; P:generation of neurons; IEP:DFLAT.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:MGI.
DR GO; GO:0098828; P:modulation of inhibitory postsynaptic potential; ISO:MGI.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; ISO:MGI.
DR GO; GO:1904113; P:negative regulation of muscle filament sliding; ISO:MGI.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEP:DFLAT.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0060134; P:prepulse inhibition; ISO:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI.
DR GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; ISO:MGI.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR028438; Drebrin.
DR PANTHER; PTHR10829:SF1; PTHR10829:SF1; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Developmental protein; Differentiation;
KW Direct protein sequencing; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..706
FT /note="Drebrin"
FT /id="PRO_0000080009"
FT DOMAIN 3..134
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 209..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07266"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 322..367
FT /note="Missing (in isoform E2)"
FT /evidence="ECO:0000303|PubMed:10633083,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_004198"
FT VAR_SEQ 368
FT /note="S -> R (in isoform A2)"
FT /evidence="ECO:0000303|PubMed:11991718"
FT /id="VSP_004199"
FT VAR_SEQ 369..706
FT /note="Missing (in isoform A2)"
FT /evidence="ECO:0000303|PubMed:11991718"
FT /id="VSP_004200"
FT CONFLICT 79
FT /note="K -> T (in Ref. 1; AAF25189/AAF25190 and 2;
FT BAB86904)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="Q -> QQ (in Ref. 3; BAE20965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 77287 MW; 39E542D2BB859346 CRC64;
MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG LQELSGHFEN
QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS HVAKVAEFFQ GVDVIVNASS
VEDIDAGAIG QRLSNGLARL SSPVLHRLRL REDENAEPVG TTYQKTDAAV EMKRINREQF
WEQAKKEEEL RKEEERKKAL DARLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ
SLEAEEAKRR LKEQSIFGDQ RDEEEESQMK KSESEVEEAA AIIAQRPDNP REFFRQQERV
ASASGGSCDA PAPAPFNHRP GRPYCPFIKA SDSGPSSSSS SSSSPPRTPF PYITCHRTPN
LSSSLPCSHL DSHRRMAPTP IPTRSPSDSS TASTPIAEQI ERALDEVTSS QPPPPPPPPP
PTQEAQETTP SLDEELSKEA KVTAAPEVWA GCAAEPPQAQ EPPLLQSSPL EDSMCTESPE
QAALAAPAEP AASVTSVADV HAADTIETTT ATTDTTIANN VTPAAASLID LWPGNGEEAS
TLQAEPRVPT PPSGAEASLA EVPLLNEAAQ EPLPPVGEGC ANLLNFDELP EPPATFCDPE
EEVGETLAAS QVLTMPSALE EVDQVLEQEL EPEPHLLTNG ETTQKEGTQA SEGYFSQSQE
EEFAQSEEPC AKVPPPVFYN KPPEIDITCW DADPVPEEEE GFEGGD
