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 24-JAN-2024, entry version 189. 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}, Sh3p7 GN {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, RC Pancreas, 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}. 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; 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; 32. DR DIP; DIP-39835N; -. DR IntAct; Q62418; 7. DR MINT; Q62418; -. DR STRING; 10090.ENSMUSP00000020769; -. DR GlyGen; Q62418; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q62418; -. DR PhosphoSitePlus; Q62418; -. DR SwissPalm; Q62418; -. DR EPD; Q62418; -. DR jPOST; Q62418; -. DR MaxQB; Q62418; -. DR PaxDb; 10090-ENSMUSP00000020769; -. DR PeptideAtlas; Q62418; -. DR ProteomicsDB; 279155; -. [Q62418-1] DR ProteomicsDB; 279156; -. [Q62418-2] DR ProteomicsDB; 279157; -. [Q62418-3] DR Pumba; Q62418; -. DR Antibodypedia; 13203; 295 antibodies from 35 providers. DR DNASU; 13169; -. DR Ensembl; ENSMUST00000020769.14; ENSMUSP00000020769.8; ENSMUSG00000020476.15. [Q62418-1] DR Ensembl; ENSMUST00000102928.5; ENSMUSP00000099992.5; ENSMUSG00000020476.15. [Q62418-2] DR Ensembl; ENSMUST00000109845.8; ENSMUSP00000105471.2; ENSMUSG00000020476.15. [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 AGR; MGI:700006; -. 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; FKEPRGA; -. DR OrthoDB; 101008at2759; -. DR PhylomeDB; Q62418; -. DR TreeFam; TF318935; -. DR BioGRID-ORCS; 13169; 3 hits in 78 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 261 other cell types or tissues. 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:0098978; C:glutamatergic synapse; ISO:MGI. 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:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central. DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central. DR GO; GO:0098793; C:presynapse; ISO:MGI. 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:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; ISO:MGI. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0006897; P:endocytosis; 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; ISO:MGI. DR GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI. DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central. DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB. DR CDD; cd11281; ADF_drebrin_like; 1. DR CDD; cd11960; SH3_Abp1_eu; 1. DR Gene3D; 3.40.20.10; Severin; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR002108; ADF-H. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR035717; Drebrin-like_SH3. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1. DR PANTHER; PTHR10829:SF12; DREBRIN-LIKE PROTEIN; 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; SSF55753; Actin depolymerizing proteins; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51263; ADF_H; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q62418; MM. 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 //