NWK_DROME
ID NWK_DROME Reviewed; 1075 AA.
AC X2JAU8; M9NE66; M9NF56; M9NFQ1; Q9VSU8; X2J8V0; X2JC77; X2JCQ1; X2JGF9;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Protein nervous wreck {ECO:0000303|PubMed:14980202, ECO:0000303|PubMed:18701694, ECO:0000303|PubMed:21464232};
DE Short=Nwk {ECO:0000303|PubMed:21464232};
GN Name=nwk {ECO:0000312|FlyBase:FBgn0263456};
GN ORFNames=CG43479 {ECO:0000312|FlyBase:FBgn0263456};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AHN58019.1, ECO:0000312|Proteomes:UP000000803}
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASP, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14980202; DOI=10.1016/s0896-6273(04)00016-9;
RA Coyle I.P., Koh Y.H., Lee W.C., Slind J., Fergestad T., Littleton J.T.,
RA Ganetzky B.;
RT "Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates
RT synaptic growth in Drosophila.";
RL Neuron 41:521-534(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP WASP; DAP160 AND SHI.
RX PubMed=18701694; DOI=10.1523/jneurosci.2304-08.2008;
RA Rodal A.A., Motola-Barnes R.N., Littleton J.T.;
RT "Nervous wreck and Cdc42 cooperate to regulate endocytic actin assembly
RT during synaptic growth.";
RL J. Neurosci. 28:8316-8325(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH DAP160 AND SHI.
RX PubMed=18498733; DOI=10.1016/j.neuron.2008.03.007;
RA O'Connor-Giles K.M., Ho L.L., Ganetzky B.;
RT "Nervous wreck interacts with thickveins and the endocytic machinery to
RT attenuate retrograde BMP signaling during synaptic growth.";
RL Neuron 58:507-518(2008).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SNX16, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21464232; DOI=10.1083/jcb.201009052;
RA Rodal A.A., Blunk A.D., Akbergenova Y., Jorquera R.A., Buhl L.K.,
RA Littleton J.T.;
RT "A presynaptic endosomal trafficking pathway controls synaptic growth
RT signaling.";
RL J. Cell Biol. 193:201-217(2011).
RN [7]
RP FUNCTION, DOMAIN, LIPID-BINDING, SUBUNIT, AND STRUCTURE BY ELECTRON
RP MICROSCOPY (20 ANGSTROMS) OF 1-428.
RX PubMed=23761074; DOI=10.1091/mbc.e13-05-0271;
RA Becalska A.N., Kelley C.F., Berciu C., Stanishneva-Konovalova T.B., Fu X.,
RA Wang S., Sokolova O.S., Nicastro D., Rodal A.A.;
RT "Formation of membrane ridges and scallops by the F-BAR protein Nervous
RT Wreck.";
RL Mol. Biol. Cell 24:2406-2418(2013).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP DAP160, LIPID-BINDING, DOMAIN, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLU-676.
RX PubMed=26686642; DOI=10.1016/j.celrep.2015.11.044;
RA Kelley C.F., Messelaar E.M., Eskin T.L., Wang S., Song K., Vishnia K.,
RA Becalska A.N., Shupliakov O., Hagan M.F., Danino D., Sokolova O.S.,
RA Nicastro D., Rodal A.A.;
RT "Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and
RT Autoregulation.";
RL Cell Rep. 13:2597-2609(2015).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SH3PX1.
RX PubMed=26567222; DOI=10.1242/jcs.178699;
RA Ukken F.P., Bruckner J.J., Weir K.L., Hope S.J., Sison S.L.,
RA Birschbach R.M., Hicks L., Taylor K.L., Dent E.W., Gonsalvez G.B.,
RA O'Connor-Giles K.M.;
RT "BAR-SH3 sorting nexins are conserved interacting proteins of Nervous wreck
RT that organize synapses and promote neurotransmission.";
RL J. Cell Sci. 129:166-177(2016).
RN [10]
RP FUNCTION, SUBUNIT, INTERACTION WITH WASP, LIPID-BINDING, DOMAIN, AND
RP STRUCTURE BY ELECTRON MICROSCOPY (20 ANGSTROMS).
RX PubMed=27601635; DOI=10.1073/pnas.1524412113;
RA Stanishneva-Konovalova T.B., Kelley C.F., Eskin T.L., Messelaar E.M.,
RA Wasserman S.A., Sokolova O.S., Rodal A.A.;
RT "Coordinated autoinhibition of F-BAR domain membrane binding and WASp
RT activation by Nervous Wreck.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E5552-E5561(2016).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, IDENTIFICATION IN A
RP COMPLEX WITH SYN AND SYT1, AND TISSUE SPECIFICITY.
RX PubMed=29568072; DOI=10.1038/emm.2017.303;
RA Hur J.H., Lee S.H., Kim A.Y., Koh Y.H.;
RT "Regulation of synaptic architecture and synaptic vesicle pools by Nervous
RT wreck at Drosophila Type 1b glutamatergic synapses.";
RL Exp. Mol. Med. 50:E462-E462(2018).
CC -!- FUNCTION: Adapter protein that provides a link between vesicular
CC membrane traffic and the actin assembly machinery. Acts together with
CC Cdc42 to stimulate actin nucleation mediated by WASp and the ARP2/3
CC complex (PubMed:18701694, PubMed:27601635). Binds to membranes enriched
CC in phosphatidylinositol 4,5-bisphosphate and causes local membrane
CC deformation (PubMed:23761074, PubMed:26686642). Required for normal
CC structure and function of synapses at the neuromuscular junction
CC (PubMed:18701694, PubMed:14980202, PubMed:18498733, PubMed:21464232,
CC PubMed:26686642, PubMed:26567222, PubMed:27601635, PubMed:29568072).
CC Plays a role in synaptic vesicle trafficking (PubMed:29568072).
CC Required for the release of a normal number of synaptic vesicles per
CC action potential (PubMed:26567222). {ECO:0000269|PubMed:14980202,
CC ECO:0000269|PubMed:18498733, ECO:0000269|PubMed:18701694,
CC ECO:0000269|PubMed:21464232, ECO:0000269|PubMed:23761074,
CC ECO:0000269|PubMed:26567222, ECO:0000269|PubMed:26686642,
CC ECO:0000269|PubMed:27601635, ECO:0000269|PubMed:29568072}.
CC -!- SUBUNIT: Homodimer (Probable) (PubMed:27601635). Interacts (via SH3
CC domain 1) with WASp (PubMed:14980202, PubMed:18701694,
CC PubMed:27601635). Interacts (via SH3 domain 1) with shi/dynamin
CC (PubMed:18701694, PubMed:18498733). Interacts (via SH3 domain 2) with
CC Dap160 (PubMed:18701694, PubMed:18498733, PubMed:26686642). Interacts
CC (via F-BAR domain) with SH3PX1 (PubMed:26567222). Interacts (via SH3
CC domain 2) with Snx16 (PubMed:21464232). Identified in a complex with
CC Syn and Syt1 (PubMed:29568072). {ECO:0000269|PubMed:14980202,
CC ECO:0000269|PubMed:18498733, ECO:0000269|PubMed:18701694,
CC ECO:0000269|PubMed:21464232, ECO:0000269|PubMed:26567222,
CC ECO:0000269|PubMed:26686642, ECO:0000269|PubMed:27601635,
CC ECO:0000269|PubMed:29568072, ECO:0000305|PubMed:23761074}.
CC -!- INTERACTION:
CC X2JAU8; Q9VAT0: WASp; NbExp=3; IntAct=EBI-167691, EBI-132019;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:14980202,
CC ECO:0000269|PubMed:21464232, ECO:0000269|PubMed:26686642,
CC ECO:0000269|PubMed:29568072}. Synapse {ECO:0000269|PubMed:29568072}.
CC Cell projection, axon {ECO:0000269|PubMed:14980202,
CC ECO:0000269|PubMed:18701694, ECO:0000269|PubMed:26567222,
CC ECO:0000269|PubMed:26686642, ECO:0000269|PubMed:27601635}. Presynaptic
CC cell membrane {ECO:0000269|PubMed:26567222}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:29568072}.
CC Recycling endosome {ECO:0000269|PubMed:21464232}. Note=Detected at
CC presynaptic axon terminals at the neuromuscular junction
CC (PubMed:14980202, PubMed:18701694, PubMed:21464232, PubMed:26686642,
CC PubMed:26567222, PubMed:27601635, PubMed:29568072). Colocalizes with
CC Cdc42 and Rab11 (PubMed:18701694, PubMed:21464232).
CC {ECO:0000269|PubMed:14980202, ECO:0000269|PubMed:18701694,
CC ECO:0000269|PubMed:21464232, ECO:0000269|PubMed:26567222,
CC ECO:0000269|PubMed:26686642, ECO:0000269|PubMed:27601635,
CC ECO:0000269|PubMed:29568072}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=I;
CC IsoId=X2JAU8-1; Sequence=Displayed;
CC Name=2; Synonyms=D, G;
CC IsoId=X2JAU8-2; Sequence=VSP_060059;
CC Name=3; Synonyms=H;
CC IsoId=X2JAU8-3; Sequence=VSP_060051, VSP_060055, VSP_060058;
CC Name=4; Synonyms=L;
CC IsoId=X2JAU8-4; Sequence=VSP_060051, VSP_060058;
CC Name=5; Synonyms=K;
CC IsoId=X2JAU8-5; Sequence=VSP_060052, VSP_060059;
CC Name=6; Synonyms=J;
CC IsoId=X2JAU8-6; Sequence=VSP_060052;
CC Name=7; Synonyms=B;
CC IsoId=X2JAU8-7; Sequence=VSP_060051, VSP_060056, VSP_060058,
CC VSP_060059;
CC Name=8; Synonyms=C;
CC IsoId=X2JAU8-8; Sequence=VSP_060053;
CC Name=9; Synonyms=F;
CC IsoId=X2JAU8-9; Sequence=VSP_060054, VSP_060057;
CC -!- TISSUE SPECIFICITY: Detected in larval body wall muscle
CC (PubMed:29568072). Detected at the neuromuscular junction, on
CC motoneuron axons and axon terminals, at synaptic boutons in the
CC periactive zone surrounding the synapse (at protein level)
CC (PubMed:14980202, PubMed:29568072). Detected on motoneuron axons and
CC axon terminals, at synaptic boutons in the periactive zone surrounding
CC the synapse (PubMed:26686642). {ECO:0000269|PubMed:14980202,
CC ECO:0000269|PubMed:26686642, ECO:0000269|PubMed:29568072}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryonic brain, ventral nerve cord
CC and sensory neurons, but not in muscle. {ECO:0000269|PubMed:14980202}.
CC -!- DOMAIN: In the autoinhibited state, the SH3 domains are bound to the
CC concave surface of the F-BAR domain and prevent promiscuous membrane
CC binding. {ECO:0000269|PubMed:26567222, ECO:0000269|PubMed:26686642}.
CC -!- DOMAIN: Upon heterologous expression, the isolated F-BAR domain is
CC localized at the cell membrane, and causes the formation of cellular
CC protrusions (PubMed:23761074, PubMed:26686642). Contrary to F-BAR
CC domains from other proteins, causes membrane flattening on giant
CC unilamellar vesicles (in vitro) (PubMed:23761074, PubMed:26686642).
CC Binds to membranes enriched in phosphatidylserine and
CC phosphatidylinositides, such as phosphatidylinositol 3-phosphate,
CC phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-
CC bisphosphate (PubMed:23761074, PubMed:26686642, PubMed:27601635).
CC {ECO:0000269|PubMed:23761074, ECO:0000269|PubMed:26686642,
CC ECO:0000269|PubMed:27601635}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in adults at room
CC temperature, but flies rapidly loose coordination and become paralyzed
CC within three minutes at 38 degrees Celsius (PubMed:14980202). Larvae
CC display overgrowth of neuromuscular junctions, with increased numbers
CC of synaptic boutons and increased frequency and complexity of axon
CC branching (PubMed:14980202, PubMed:18701694, PubMed:18498733,
CC PubMed:21464232, PubMed:26686642, PubMed:29568072). The synaptic area
CC and the number of reserve and readily releasable synaptic vesicles are
CC decreased (PubMed:29568072). {ECO:0000269|PubMed:14980202,
CC ECO:0000269|PubMed:18498733, ECO:0000269|PubMed:18701694,
CC ECO:0000269|PubMed:21464232, ECO:0000269|PubMed:26686642,
CC ECO:0000269|PubMed:29568072}.
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DR EMBL; AE014296; AFH04360.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04361.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04362.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04363.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50313.4; -; Genomic_DNA.
DR EMBL; AE014296; AHN58018.1; -; Genomic_DNA.
DR EMBL; AE014296; AHN58019.1; -; Genomic_DNA.
DR EMBL; AE014296; AHN58020.1; -; Genomic_DNA.
DR EMBL; AE014296; AHN58021.1; -; Genomic_DNA.
DR EMBL; AE014296; AHN58022.1; -; Genomic_DNA.
DR RefSeq; NP_001246689.1; NM_001259760.2. [X2JAU8-7]
DR RefSeq; NP_001246690.1; NM_001259761.2. [X2JAU8-8]
DR RefSeq; NP_001246691.1; NM_001259762.2. [X2JAU8-2]
DR RefSeq; NP_001246692.1; NM_001259763.2. [X2JAU8-9]
DR RefSeq; NP_001286993.1; NM_001300064.1. [X2JAU8-3]
DR RefSeq; NP_001286994.1; NM_001300065.1. [X2JAU8-1]
DR RefSeq; NP_001286995.1; NM_001300066.1. [X2JAU8-6]
DR RefSeq; NP_001286996.1; NM_001300067.1. [X2JAU8-5]
DR RefSeq; NP_001286997.1; NM_001300068.1. [X2JAU8-4]
DR RefSeq; NP_648290.3; NM_140033.3. [X2JAU8-2]
DR AlphaFoldDB; X2JAU8; -.
DR SMR; X2JAU8; -.
DR IntAct; X2JAU8; 1.
DR STRING; 7227.FBpp0301205; -.
DR EnsemblMetazoa; FBtr0309276; FBpp0301203; FBgn0263456. [X2JAU8-7]
DR EnsemblMetazoa; FBtr0309277; FBpp0301204; FBgn0263456. [X2JAU8-8]
DR EnsemblMetazoa; FBtr0309278; FBpp0301205; FBgn0263456. [X2JAU8-2]
DR EnsemblMetazoa; FBtr0309280; FBpp0301207; FBgn0263456. [X2JAU8-9]
DR EnsemblMetazoa; FBtr0331857; FBpp0304241; FBgn0263456. [X2JAU8-2]
DR EnsemblMetazoa; FBtr0344238; FBpp0310642; FBgn0263456. [X2JAU8-3]
DR EnsemblMetazoa; FBtr0344239; FBpp0310643; FBgn0263456. [X2JAU8-1]
DR EnsemblMetazoa; FBtr0344240; FBpp0310644; FBgn0263456. [X2JAU8-6]
DR EnsemblMetazoa; FBtr0344241; FBpp0310645; FBgn0263456. [X2JAU8-5]
DR EnsemblMetazoa; FBtr0344242; FBpp0310646; FBgn0263456. [X2JAU8-4]
DR GeneID; 39052; -.
DR KEGG; dme:Dmel_CG43479; -.
DR UCSC; CG4684-RA; d. melanogaster.
DR CTD; 39052; -.
DR FlyBase; FBgn0263456; nwk.
DR VEuPathDB; VectorBase:FBgn0263456; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00510000046732; -.
DR HOGENOM; CLU_013546_0_0_1; -.
DR OMA; YADGWWE; -.
DR OrthoDB; 348563at2759; -.
DR SignaLink; X2JAU8; -.
DR BioGRID-ORCS; 39052; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39052; -.
DR PRO; PR:X2JAU8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0263456; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; X2JAU8; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISM:FlyBase.
DR GO; GO:0061024; P:membrane organization; IMP:GO_Central.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; IGI:FlyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IDA:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR CDD; cd11761; SH3_FCHSD_1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035460; FCHSD_SH3_1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Endosome; Lipid-binding; Membrane; Reference proteome; Repeat; SH3 domain;
KW Synapse.
FT CHAIN 1..1075
FT /note="Protein nervous wreck"
FT /id="PRO_0000446275"
FT DOMAIN 11..289
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 542..603
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 658..721
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 361..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 611..633
FT /note="Missing (in isoform 3, isoform 4 and isoform 7)"
FT /id="VSP_060051"
FT VAR_SEQ 774..792
FT /note="Missing (in isoform 5 and isoform 6)"
FT /id="VSP_060052"
FT VAR_SEQ 793..1074
FT /note="VLIQEPGMEDDLSDDGQPPPSLPPPQLAKAGGSAPGSGSKVEKGAAAGGANT
FT LNLGMAQIIVTAATPMVEDGADKSFPPVGESDAQPVEPVSKEQPAEVAKKPDIAPKPLA
FT KVAPQSAPAKEGNAGVRPVVSITLTEYPSCDAEDQQSFSEGTDSASVADVPVLQDAEDP
FT FNEKAKGESGDGSGFEANFEANFDANFDDAFAGIGGGGGGGGGGGEQSNELDINGEAAG
FT EAIVSGSAAGDEDIEAPKQVVGGRASIPEELDSNQLAHYHEHEIYYVDYSHGQ -> GK
FT CHILALSTGLLFPLSISLFKLYPYRF (in isoform 8)"
FT /id="VSP_060053"
FT VAR_SEQ 793..885
FT /note="VLIQEPGMEDDLSDDGQPPPSLPPPQLAKAGGSAPGSGSKVEKGAAAGGANT
FT LNLGMAQIIVTAATPMVEDGADKSFPPVGESDAQPVEPVSK -> GQNQSQTTAKKGNL
FT MNMLFYLNYLIPETFPDSVILSVGKSISTPLFESMSNPPLNYCSTFKMRFSSWYIEKNI
FT QYIFSIRFLSTCLQLFPKDI (in isoform 9)"
FT /id="VSP_060054"
FT VAR_SEQ 848..872
FT /note="Missing (in isoform 3)"
FT /id="VSP_060055"
FT VAR_SEQ 848..871
FT /note="Missing (in isoform 7)"
FT /id="VSP_060056"
FT VAR_SEQ 886..1075
FT /note="Missing (in isoform 9)"
FT /id="VSP_060057"
FT VAR_SEQ 915..935
FT /note="Missing (in isoform 3, isoform 4 and isoform 7)"
FT /id="VSP_060058"
FT VAR_SEQ 1059..1075
FT /note="HYHEHEIYYVDYSHGQL -> RLQNLKESNA (in isoform 2,
FT isoform 5 and isoform 7)"
FT /id="VSP_060059"
FT MUTAGEN 676
FT /note="E->R: Decreased interaction with F-BAR domain. No
FT effect on interaction with Dap160."
FT /evidence="ECO:0000269|PubMed:26686642"
SQ SEQUENCE 1075 AA; 117255 MW; A3AC3F8BE5A890FC CRC64;
MQPPPRKGNY VKFLKNLHTE QVAKLQLKNQ HECDLLEDIR QFTIKRSAVE KSYSESLLKI
SSQYLNKKIP NIPDIKMEGM EERWNMWSVW RTVLEENEKL ARARLAAIEV FQQQIADEAK
VLRDYKLAIA KRSLAGIVNV QKELHLSVGD VDKTKKSYFD EEHCAHDVRD KARDIEEKLK
KKKGSFFQSI TSLQKNSARV TSRKELLEEK SSGARNDYVL SLAAANAHQN RYFTVDLQTT
MTTMENYVFE RVAEYLMLMG RTELLTCSAT QNSFGKIRDQ AQQLTREYNL QCCYLFYPVL
KQHIQYDFEA CDNDPVRKVT AEHESAAETL TKEAKNLAGR VVKENASIRE NAKKLALCQS
LRDSGQRTDP NDPNGPDLDT KIEEFRDQIR RSETEKTKAE ACLQCLRDGG INVDEWVQEA
ENMGVQELTR SASSISMRTD ASGQGENPSS DSFYDSDKEE TQAAAQTKPK QEQQLSRDRT
FSDSEDEPEV RPSAAAASSA AAASSSMMAS SAGGWDDPTE VNWGAGEEED DKDEPIVPEP
KEAIFKCTAL YSYTAQNPDE LTIVENEQLE VVGEGDGDGW LRARNYRGEE GYVPHNYLDI
DQETAGSAFN GTSGNQLRSQ ISFSSVDYTV DNEDQTVDSM QSPDQVSVIM APQKRVKSDV
EWCIALYDYD ATAEDELTFE EGDKIKIITK TAHGVDDGWW EGELDGKFGN FPSLVVEECD
EMGEPLSEGG DESPPPTAAP TFALPPAPAL PPEYAHELEL ELTEDMFGSQ DTADEDSGYI
PNGAAAPSIP PPVLIQEPGM EDDLSDDGQP PPSLPPPQLA KAGGSAPGSG SKVEKGAAAG
GANTLNLGMA QIIVTAATPM VEDGADKSFP PVGESDAQPV EPVSKEQPAE VAKKPDIAPK
PLAKVAPQSA PAKEGNAGVR PVVSITLTEY PSCDAEDQQS FSEGTDSASV ADVPVLQDAE
DPFNEKAKGE SGDGSGFEAN FEANFDANFD DAFAGIGGGG GGGGGGGEQS NELDINGEAA
GEAIVSGSAA GDEDIEAPKQ VVGGRASIPE ELDSNQLAHY HEHEIYYVDY SHGQL
