DBNL_DROME
ID DBNL_DROME Reviewed; 531 AA.
AC Q9VU84; Q8MRS9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Drebrin-like protein;
DE AltName: Full=Actin binding protein 1;
GN Name=Abp1; ORFNames=CG10083;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP IDENTIFICATION.
RX PubMed=10908588; DOI=10.1083/jcb.150.2.f63;
RA Goldstein L.S., Gunawardena S.;
RT "Flying through the Drosophila cytoskeletal genome.";
RL J. Cell Biol. 150:F63-F68(2000).
RN [5]
RP FUNCTION.
RX PubMed=12975351; DOI=10.1083/jcb.200303023;
RA Rogers S.L., Wiedemann U., Stuurman N., Vale R.D.;
RT "Molecular requirements for actin-based lamella formation in Drosophila S2
RT cells.";
RL J. Cell Biol. 162:1079-1088(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Actin-binding adapter protein. Binds to F-actin but is not
CC involved in actin polymerization, capping or bundling. Does not bind G-
CC actin (By similarity). Does not seem to be involved in actin-based
CC lamella protrusion during cell migration. {ECO:0000250,
CC ECO:0000269|PubMed:12975351}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49805.1; -; Genomic_DNA.
DR EMBL; AY119287; AAM51147.1; -; mRNA.
DR EMBL; BT021389; AAX33537.1; -; mRNA.
DR RefSeq; NP_648657.1; NM_140400.2.
DR AlphaFoldDB; Q9VU84; -.
DR SMR; Q9VU84; -.
DR BioGRID; 64863; 5.
DR IntAct; Q9VU84; 3.
DR STRING; 7227.FBpp0075561; -.
DR iPTMnet; Q9VU84; -.
DR PaxDb; Q9VU84; -.
DR PRIDE; Q9VU84; -.
DR EnsemblMetazoa; FBtr0075819; FBpp0075561; FBgn0036372.
DR GeneID; 39520; -.
DR KEGG; dme:Dmel_CG10083; -.
DR UCSC; CG10083-RA; d. melanogaster.
DR CTD; 39520; -.
DR FlyBase; FBgn0036372; Abp1.
DR VEuPathDB; VectorBase:FBgn0036372; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000168710; -.
DR HOGENOM; CLU_013085_0_1_1; -.
DR InParanoid; Q9VU84; -.
DR OMA; TNIDMVD; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; Q9VU84; -.
DR Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-DME-6794361; Neurexins and neuroligins.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 39520; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39520; -.
DR PRO; PR:Q9VU84; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036372; Expressed in cleaving embryo and 23 other tissues.
DR Genevisible; Q9VU84; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IDA:FlyBase.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0061176; C:type Ib terminal bouton; IDA:FlyBase.
DR GO; GO:0061177; C:type Is terminal bouton; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IC:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:FlyBase.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:FlyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
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:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0072553; P:terminal button organization; IMP:FlyBase.
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; IPR035717; Drebrin-like_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
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 Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..531
FT /note="Drebrin-like protein"
FT /id="PRO_0000270188"
FT DOMAIN 2..133
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT DOMAIN 472..531
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 191..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 177..220
FT /evidence="ECO:0000255"
FT COMPBIAS 286..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
SQ SEQUENCE 531 AA; 58729 MW; A1CAAFA251F151C7 CRC64;
MAVSFEKNRA QIVAAWKDVL DDKSDTNWSL FGYEGQTNEL KVVATGDGGV DELNEDLNSG
KIMYAFVRIE DPKTGLNKYL LINWQGEGAP VLRKGTCANH IRDVSNLLSG AHLTINARNE
DDIDLDRLLK KLSTVSSAYS FKEPRGAMEE QKAPVGTNYT RVIPTKELNA SVMQDFWKKE
EAEEKLRQEA EKESKRLELQ KLEQEQRSRE EKEHKEREKL VISTTKLQPA HVPIKTSPQP
LSPEKTAPGF ANNLTDAERM RQARNQEARE LIGSRVGAAK AMFTKHTSEG QLQSKLNTQP
PAKPARNSIA QRINVFNQNQ PQDAPVPSPP RAASPAKPLP VEAPEPVVPA PAIAPAAPVA
AEVVSTIAEV EESQPVDDLP LAHESEQFST IKRSPHSKSN SLQSQSPDET TSSNETDTAV
SQEQEEEVRT KVSVTVQQSQ SVKSSGMSTL ERNALTDLVN EDDFICQETL GDLGQRARAL
YDYQAADETE ITFDPGDVIT HIDQIDEGWW QGLGPDGTYG LFPANYVEII N
