DBNL_MOUSE
ID DBNL_MOUSE Reviewed; 436 AA.
AC Q62418; Q3TG34; Q3U5X3; Q3U8I5; Q3UZ33; Q5NCI5; Q5NCI6; Q5NCI7; Q80WP1;
AC Q8BH56;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Actin-binding protein 1;
DE AltName: Full=SH3 domain-containing protein 7;
GN Name=Dbnl {ECO:0000312|MGI:MGI:700006};
GN Synonyms=Abp1 {ECO:0000303|PubMed:17476322},
GN Sh3p7 {ECO:0000303|PubMed:9630982};
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] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 79-94 AND
RP 135-144, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-340
RP AND TYR-350, AND PHOSPHORYLATION AT TYR-340 AND TYR-350.
RC TISSUE=Myeloma {ECO:0000269|PubMed:9891087};
RX PubMed=9891087; DOI=10.1128/mcb.19.2.1539;
RA Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J., Wienands J.;
RT "SH3P7 is a cytoskeleton adapter protein and is coupled to signal
RT transduction from lymphocyte antigen receptors.";
RL Mol. Cell. Biol. 19:1539-1546(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAM28340.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH FGD1.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAM28340.1}; TISSUE=Osteoblast;
RX PubMed=12913069; DOI=10.1093/hmg/ddg209;
RA Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B., Gorski J.L.;
RT "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly
RT interacts with cortactin and mAbp1 to modulate cell shape.";
RL Hum. Mol. Genet. 12:1981-1993(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Bone marrow, Corpora quadrigemina, Eye, Head, Kidney,
RC Medulla oblongata, Spleen, and Thymus;
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 [5]
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 [6] {ECO:0000305, ECO:0000312|EMBL:AAH46430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH46430.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH46430.1};
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 [7] {ECO:0000305}
RP INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10637315; DOI=10.1091/mbc.11.1.393;
RA Kessels M.M., Engqvist-Goldstein A.E.Y., Drubin D.G.;
RT "Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase
RT target, with dynamic regions of the cortical actin cytoskeleton in response
RT to Rac1 activation.";
RL Mol. Biol. Cell 11:393-412(2000).
RN [8]
RP FUNCTION, INTERACTION WITH DNM1, ACTIN-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11309416; DOI=10.1083/jcb.153.2.351;
RA Kessels M.M., Engqvist-Goldstein A.E., Drubin D.G., Qualmann B.;
RT "Mammalian Abp1, a signal-responsive F-actin-binding protein, links the
RT actin cytoskeleton to endocytosis via the GTPase dynamin.";
RL J. Cell Biol. 153:351-366(2001).
RN [9]
RP ACTIN-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=16452483; DOI=10.1074/jbc.m510141200;
RA Xu W., Stamnes M.;
RT "The actin-depolymerizing factor homology and charged/helical domains of
RT drebrin and mAbp1 direct membrane binding and localization via distinct
RT interactions with actin.";
RL J. Biol. Chem. 281:11826-11833(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
RX PubMed=17476322; DOI=10.1371/journal.pone.0000400;
RA Pinyol R., Haeckel A., Ritter A., Qualmann B., Kessels M.M.;
RT "Regulation of N-WASP and the Arp2/3 complex by Abp1 controls neuronal
RT morphology.";
RL PLoS ONE 2:E400-E400(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP FUNCTION, AND INTERACTION WITH SHANK2.
RX PubMed=18829961; DOI=10.1523/jneurosci.0336-08.2008;
RA Haeckel A., Ahuja R., Gundelfinger E.D., Qualmann B., Kessels M.M.;
RT "The actin-binding protein Abp1 controls dendritic spine morphology and is
RT important for spine head and synapse formation.";
RL J. Neurosci. 28:10031-10044(2008).
RN [13]
RP INTERACTION WITH ANKRD54.
RX PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
RA Samuels A.L., Klinken S.P., Ingley E.;
RT "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
RT influences erythropoietin-induced differentiation.";
RL Blood 113:3845-3856(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-277 AND SER-280, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [15]
RP FUNCTION, INTERACTION WITH WIPF1, PHOSPHORYLATION AT TYR-340 AND TYR-350,
RP MUTAGENESIS OF TYR-340 AND TYR-350, AND SUBCELLULAR LOCATION.
RX PubMed=22303001; DOI=10.1242/jcs.096529;
RA Boateng L.R., Cortesio C.L., Huttenlocher A.;
RT "Src-mediated phosphorylation of mammalian Abp1 (DBNL) regulates podosome
RT rosette formation in transformed fibroblasts.";
RL J. Cell Sci. 125:1329-1341(2012).
RN [16]
RP FUNCTION, INTERACTION WITH COBL, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23223303; DOI=10.1523/jneurosci.0843-12.2012;
RA Haag N., Schwintzer L., Ahuja R., Koch N., Grimm J., Heuer H., Qualmann B.,
RA Kessels M.M.;
RT "The actin nucleator Cobl is crucial for Purkinje cell development and
RT works in close conjunction with the F-actin binding protein Abp1.";
RL J. Neurosci. 32:17842-17856(2012).
CC -!- FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby
CC plays a role in receptor-mediated endocytosis. Plays a role in the
CC reorganization of the actin cytoskeleton, formation of cell
CC projections, such as neurites, in neuron morphogenesis and synapse
CC formation via its interaction with WASL and COBL. Does not bind G-actin
CC and promote actin polymerization by itself. Required for the formation
CC of organized podosome rosettes. May act as a common effector of antigen
CC receptor-signaling pathways in leukocytes. Acts as a key component of
CC the immunological synapse that regulates T-cell activation by bridging
CC TCRs and the actin cytoskeleton to gene activation and endocytic
CC processes. {ECO:0000269|PubMed:11309416, ECO:0000269|PubMed:17476322,
CC ECO:0000269|PubMed:18829961, ECO:0000269|PubMed:22303001,
CC ECO:0000269|PubMed:23223303}.
CC -!- SUBUNIT: Interacts with SHANK3, SYN1 and PRAM1 (By similarity).
CC Interacts with SHANK2. Interacts with FGD1, DNM1 and MAP4K1. Interacts
CC with ANKRD54. Interacts with COBL. Interacts with WASL and WIPF1.
CC {ECO:0000250, ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:11309416,
CC ECO:0000269|PubMed:12913069, ECO:0000269|PubMed:17476322,
CC ECO:0000269|PubMed:18829961, ECO:0000269|PubMed:19064729,
CC ECO:0000269|PubMed:22303001, ECO:0000269|PubMed:23223303}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:17476322,
CC ECO:0000269|PubMed:9891087}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:12913069}. Cell
CC projection, ruffle {ECO:0000269|PubMed:12913069}. Cytoplasm, cell
CC cortex {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:11309416,
CC ECO:0000269|PubMed:23223303}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JHL4}. Synapse {ECO:0000269|PubMed:11309416}.
CC Perikaryon {ECO:0000269|PubMed:11309416}. Cell projection, neuron
CC projection {ECO:0000269|PubMed:11309416}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9JHL4}; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000305|PubMed:11309416}; Peripheral membrane protein; Cytoplasmic
CC side. Golgi apparatus membrane {ECO:0000269|PubMed:16452483};
CC Peripheral membrane protein; Cytoplasmic side. Cell projection,
CC podosome {ECO:0000269|PubMed:22303001}. Early endosome
CC {ECO:0000250|UniProtKB:Q9UJU6}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9JHL4}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9JHL4}. Note=Associates with lamellipodial
CC actin and membrane ruffles. Colocalizes with actin and cortactin at
CC podosome dots and podosome rosettes. {ECO:0000250|UniProtKB:Q9JHL4,
CC ECO:0000269|PubMed:12913069, ECO:0000269|PubMed:17476322,
CC ECO:0000269|PubMed:22303001}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:12913069};
CC IsoId=Q62418-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9891087};
CC IsoId=Q62418-2; Sequence=VSP_050790;
CC Name=3 {ECO:0000305};
CC IsoId=Q62418-3; Sequence=VSP_050789;
CC -!- TISSUE SPECIFICITY: Detected in hippocampus neurons and in the Purkinje
CC cell layer in cerebellum (at protein level). Predominantly expressed in
CC brain, thymus and spleen. Also found in testis, heart and lung. Little
CC or no expression detected in ovary or muscle.
CC {ECO:0000269|PubMed:10637315, ECO:0000269|PubMed:23223303,
CC ECO:0000269|PubMed:9891087}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression is high during early
CC development but drops during later development.
CC {ECO:0000269|PubMed:10637315}.
CC -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3 and
CC PRAM1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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DR EMBL; U58884; AAC52640.1; -; mRNA.
DR EMBL; AY098595; AAM28340.1; -; mRNA.
DR EMBL; AK046073; BAC32592.1; -; mRNA.
DR EMBL; AK053796; BAC35528.1; -; mRNA.
DR EMBL; AK078082; BAC37118.1; -; mRNA.
DR EMBL; AK134136; BAE22028.1; -; mRNA.
DR EMBL; AK134487; BAE22160.1; -; mRNA.
DR EMBL; AK140752; BAE24466.1; -; mRNA.
DR EMBL; AK142818; BAE25201.1; -; mRNA.
DR EMBL; AK146920; BAE27532.1; -; mRNA.
DR EMBL; AK151096; BAE30108.1; -; mRNA.
DR EMBL; AK152204; BAE31033.1; -; mRNA.
DR EMBL; AK153389; BAE31953.1; -; mRNA.
DR EMBL; AK159984; BAE35535.1; -; mRNA.
DR EMBL; AK168898; BAE40714.1; -; mRNA.
DR EMBL; AK172471; BAE43024.1; -; mRNA.
DR EMBL; AL627069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046430; AAH46430.1; -; mRNA.
DR CCDS; CCDS24403.1; -. [Q62418-2]
DR CCDS; CCDS48746.1; -. [Q62418-1]
DR CCDS; CCDS48747.1; -. [Q62418-3]
DR RefSeq; NP_001139780.1; NM_001146308.1. [Q62418-1]
DR RefSeq; NP_001139781.1; NM_001146309.1. [Q62418-3]
DR RefSeq; NP_038838.1; NM_013810.3. [Q62418-2]
DR AlphaFoldDB; Q62418; -.
DR SMR; Q62418; -.
DR BioGRID; 199059; 29.
DR DIP; DIP-39835N; -.
DR IntAct; Q62418; 7.
DR MINT; Q62418; -.
DR STRING; 10090.ENSMUSP00000020769; -.
DR iPTMnet; Q62418; -.
DR PhosphoSitePlus; Q62418; -.
DR SwissPalm; Q62418; -.
DR EPD; Q62418; -.
DR jPOST; Q62418; -.
DR MaxQB; Q62418; -.
DR PaxDb; Q62418; -.
DR PeptideAtlas; Q62418; -.
DR PRIDE; Q62418; -.
DR ProteomicsDB; 279155; -. [Q62418-1]
DR ProteomicsDB; 279156; -. [Q62418-2]
DR ProteomicsDB; 279157; -. [Q62418-3]
DR Antibodypedia; 13203; 276 antibodies from 35 providers.
DR DNASU; 13169; -.
DR Ensembl; ENSMUST00000020769; ENSMUSP00000020769; ENSMUSG00000020476. [Q62418-1]
DR Ensembl; ENSMUST00000102928; ENSMUSP00000099992; ENSMUSG00000020476. [Q62418-2]
DR Ensembl; ENSMUST00000109845; ENSMUSP00000105471; ENSMUSG00000020476. [Q62418-3]
DR GeneID; 13169; -.
DR KEGG; mmu:13169; -.
DR UCSC; uc007hxb.2; mouse. [Q62418-2]
DR UCSC; uc007hxc.2; mouse. [Q62418-3]
DR UCSC; uc007hxd.2; mouse. [Q62418-1]
DR CTD; 28988; -.
DR MGI; MGI:700006; Dbnl.
DR VEuPathDB; HostDB:ENSMUSG00000020476; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000156732; -.
DR HOGENOM; CLU_013085_0_1_1; -.
DR InParanoid; Q62418; -.
DR OMA; TNIDMVD; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; Q62418; -.
DR TreeFam; TF318935; -.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13169; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dbnl; mouse.
DR PRO; PR:Q62418; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q62418; protein.
DR Bgee; ENSMUSG00000020476; Expressed in ileal epithelium and 257 other tissues.
DR Genevisible; Q62418; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IBA:GO_Central.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IBA:GO_Central.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; IEA:InterPro.
DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR CDD; cd11960; SH3_Abp1_eu; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR029923; Dbnl.
DR InterPro; IPR035717; Drebrin-like_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829:SF12; PTHR10829:SF12; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00102; ADF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51263; ADF_H; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Adaptive immunity; Alternative splicing;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; Endocytosis;
KW Endosome; Golgi apparatus; Immunity; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse; Transport.
FT CHAIN 1..436
FT /note="Drebrin-like protein"
FT /id="PRO_0000079794"
FT DOMAIN 2..133
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 377..436
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 185..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..233
FT /evidence="ECO:0000255"
FT COMPBIAS 185..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 367..368
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 296
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJU6"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22303001,
FT ECO:0000269|PubMed:9891087"
FT MOD_RES 350
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22303001,
FT ECO:0000269|PubMed:9891087"
FT VAR_SEQ 235..238
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_050789"
FT VAR_SEQ 236..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9630982, ECO:0000303|PubMed:9891087"
FT /id="VSP_050790"
FT MUTAGEN 340
FT /note="Y->F: Reduces phosphorylation. Abolishes
FT phosphorylation; when associated with F-350."
FT /evidence="ECO:0000269|PubMed:22303001,
FT ECO:0000269|PubMed:9891087"
FT MUTAGEN 350
FT /note="Y->F: Reduces phosphorylation. Impairs podosome
FT rosette formation. Abolishes phosphorylation; when
FT associated with F-340."
FT /evidence="ECO:0000269|PubMed:22303001,
FT ECO:0000269|PubMed:9891087"
FT CONFLICT 30
FT /note="L -> F (in Ref. 4; BAE40714)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="V -> D (in Ref. 4; BAE31953)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> V (in Ref. 4; BAE30108/BAE31033)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="S -> C (in Ref. 4; BAE22028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 48700 MW; 85AEF9781C698A3F CRC64;
MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EELVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH VSTMANFLKG AHVTINARAE
EDVEPECIME KVAKASGANY SFHKESTSFQ DVGPQAPVGS VYQKTNAISE IKRVGKDNFW
AKAEKEEENR RLEEKRRAEE ERQRLEEERR ERELQEAARR EQRYQEQHRS AGAPSPSSRT
GEPEQEAVSR TRQEWESAGQ QAPHPREIFK QKERAMSTTS VTSSQPGKLR SPFLQKQLTQ
PETSYGREPT APVSRPAAGV CEEPAPSTLS SAQTEEEPTY EVPPEQDTLY EEPPLVQQQG
AGSEHIDNYM QSQGFSGQGL CARALYDYQA ADDTEISFDP ENLITGIEVI DEGWWRGYGP
DGHFGMFPAN YVELIE
