DRPR_DROME
ID DRPR_DROME Reviewed; 1031 AA.
AC Q9W0A0; M9NEX8; Q1EC80; Q9W0A1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein draper {ECO:0000312|FlyBase:FBgn0027594};
DE Flags: Precursor;
GN Name=drpr {ECO:0000303|PubMed:12765609, ECO:0000312|FlyBase:FBgn0027594};
GN Synonyms=Megf10; ORFNames=CG2086 {ECO:0000312|FlyBase:FBgn0027594};
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|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:ABF85754.1, ECO:0000312|EMBL:ACH92235.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABF85754.1, ECO:0000312|EMBL:ACH92235.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12765609; DOI=10.1016/s0896-6273(03)00289-7;
RA Freeman M.R., Delrow J., Kim J., Johnson E., Doe C.Q.;
RT "Unwrapping glial biology: Gcm target genes regulating glial development,
RT diversification, and function.";
RL Neuron 38:567-580(2003).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15342648; DOI=10.1074/jbc.m408597200;
RA Manaka J., Kuraishi T., Shiratsuchi A., Nakai Y., Higashida H., Henson P.,
RA Nakanishi Y.;
RT "Draper-mediated and phosphatidylserine-independent phagocytosis of
RT apoptotic cells by Drosophila hemocytes/macrophages.";
RL J. Biol. Chem. 279:48466-48476(2004).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CED-6, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY ECDYSONE, AND DISRUPTION PHENOTYPE.
RX PubMed=16772168; DOI=10.1016/j.neuron.2006.04.027;
RA Awasaki T., Tatsumi R., Takahashi K., Arai K., Nakanishi Y., Ueda R.,
RA Ito K.;
RT "Essential role of the apoptotic cell engulfment genes draper and ced-6 in
RT programmed axon pruning during Drosophila metamorphosis.";
RL Neuron 50:855-867(2006).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY INJURY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16772169; DOI=10.1016/j.neuron.2006.04.028;
RA MacDonald J.M., Beach M.G., Porpiglia E., Sheehan A.E., Watts R.J.,
RA Freeman M.R.;
RT "The Drosophila cell corpse engulfment receptor Draper mediates glial
RT clearance of severed axons.";
RL Neuron 50:869-881(2006).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16772170; DOI=10.1016/j.neuron.2006.05.013;
RA Hoopfer E.D., McLaughlin T., Watts R.J., Schuldiner O., O'Leary D.D.,
RA Luo L.;
RT "Wlds protection distinguishes axon degeneration following injury from
RT naturally occurring developmental pruning.";
RL Neuron 50:883-895(2006).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18455990; DOI=10.1016/j.cell.2008.02.052;
RA Kurant E., Axelrod S., Leaman D., Gaul U.;
RT "Six-microns-under acts upstream of Draper in the glial phagocytosis of
RT apoptotic neurons.";
RL Cell 133:498-509(2008).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=18984163; DOI=10.1016/j.cell.2008.08.033;
RA Cuttell L., Vaughan A., Silva E., Escaron C.J., Lavine M., Van Goethem E.,
RA Eid J.P., Quirin M., Franc N.C.;
RT "Undertaker, a Drosophila Junctophilin, links Draper-mediated phagocytosis
RT and calcium homeostasis.";
RL Cell 135:524-534(2008).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SHARK, PHOSPHORYLATION, AND MUTAGENESIS OF
RP TYR-949.
RX PubMed=18432193; DOI=10.1038/nature06901;
RA Ziegenfuss J.S., Biswas R., Avery M.A., Hong K., Sheehan A.E., Yeung Y.G.,
RA Stanley E.R., Freeman M.R.;
RT "Draper-dependent glial phagocytic activity is mediated by Src and Syk
RT family kinase signalling.";
RL Nature 453:935-939(2008).
RN [12] {ECO:0000305}
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=19927123; DOI=10.1038/emboj.2009.343;
RA Kuraishi T., Nakagawa Y., Nagaosa K., Hashimoto Y., Ishimoto T., Moki T.,
RA Fujita Y., Nakayama H., Dohmae N., Shiratsuchi A., Yamamoto N., Ueda K.,
RA Yamaguchi M., Awasaki T., Nakanishi Y.;
RT "Pretaporter, a Drosophila protein serving as a ligand for Draper in the
RT phagocytosis of apoptotic cells.";
RL EMBO J. 28:3868-3878(2009).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19890048; DOI=10.4049/jimmunol.0901032;
RA Hashimoto Y., Tabuchi Y., Sakurai K., Kutsuna M., Kurokawa K., Awasaki T.,
RA Sekimizu K., Nakanishi Y., Shiratsuchi A.;
RT "Identification of lipoteichoic acid as a ligand for draper in the
RT phagocytosis of Staphylococcus aureus by Drosophila hemocytes.";
RL J. Immunol. 183:7451-7460(2009).
RN [14] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19707574; DOI=10.1371/journal.pbio.1000184;
RA Fuentes-Medel Y., Logan M.A., Ashley J., Ataman B., Budnik V.,
RA Freeman M.R.;
RT "Glia and muscle sculpt neuromuscular arbors by engulfing destabilized
RT synaptic boutons and shed presynaptic debris.";
RL PLoS Biol. 7:E1000184-E1000184(2009).
RN [15] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20577216; DOI=10.1038/nature09127;
RA McPhee C.K., Logan M.A., Freeman M.R., Baehrecke E.H.;
RT "Activation of autophagy during cell death requires the engulfment receptor
RT Draper.";
RL Nature 465:1093-1096(2010).
RN [16] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22992958; DOI=10.1242/dev.082776;
RA Etchegaray J.I., Timmons A.K., Klein A.P., Pritchett T.L., Welch E.,
RA Meehan T.L., Li C., McCall K.;
RT "Draper acts through the JNK pathway to control synchronous engulfment of
RT dying germline cells by follicular epithelial cells.";
RL Development 139:4029-4039(2012).
RN [17] {ECO:0000305}
RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-858 AND TYR-949.
RX PubMed=23337816;
RA Fujita Y., Nagaosa K., Shiratsuchi A., Nakanishi Y.;
RT "Role of NPxY motif in Draper-mediated apoptotic cell clearance in
RT Drosophila.";
RL Drug Discov. Ther. 6:291-297(2012).
RN [18] {ECO:0000305}
RP FUNCTION (ISOFORMS A AND B), INTERACTION WITH CSW, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DOMAIN, AND DEPHOSPHORYLATION.
RX PubMed=22426252; DOI=10.1038/nn.3066;
RA Logan M.A., Hackett R., Doherty J., Sheehan A., Speese S.D., Freeman M.R.;
RT "Negative regulation of glial engulfment activity by Draper terminates
RT glial responses to axon injury.";
RL Nat. Neurosci. 15:722-730(2012).
RN [19] {ECO:0000305}
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=23420848; DOI=10.1093/jb/mvt014;
RA Tung T.T., Nagaosa K., Fujita Y., Kita A., Mori H., Okada R., Nonaka S.,
RA Nakanishi Y.;
RT "Phosphatidylserine recognition and induction of apoptotic cell clearance
RT by Drosophila engulfment receptor Draper.";
RL J. Biochem. 153:483-491(2013).
RN [20] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25111228; DOI=10.1016/j.ajpath.2014.06.018;
RA Draper I., Mahoney L.J., Mitsuhashi S., Pacak C.A., Salomon R.N.,
RA Kang P.B.;
RT "Silencing of drpr leads to muscle and brain degeneration in adult
RT Drosophila.";
RL Am. J. Pathol. 184:2653-2661(2014).
RN [21] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24412417; DOI=10.1016/j.neuron.2013.11.021;
RA Han C., Song Y., Xiao H., Wang D., Franc N.C., Jan L.Y., Jan Y.N.;
RT "Epidermal cells are the primary phagocytes in the fragmentation and
RT clearance of degenerating dendrites in Drosophila.";
RL Neuron 81:544-560(2014).
RN [22] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-949.
RX PubMed=26028435; DOI=10.1016/j.cub.2015.04.037;
RA Evans I.R., Rodrigues F.S., Armitage E.L., Wood W.;
RT "Draper/CED-1 mediates an ancient damage response to control inflammatory
RT blood cell migration in vivo.";
RL Curr. Biol. 25:1606-1612(2015).
RN [23] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=27212238; DOI=10.1016/j.cell.2016.04.049;
RA Weavers H., Evans I.R., Martin P., Wood W.;
RT "Corpse engulfment generates a molecular memory that primes the macrophage
RT inflammatory response.";
RL Cell 165:1658-1671(2016).
RN [24] {ECO:0000305}
RP FUNCTION.
RX PubMed=27498858; DOI=10.1016/j.celrep.2016.07.022;
RA Musashe D.T., Purice M.D., Speese S.D., Doherty J., Logan M.A.;
RT "Insulin-like signaling promotes glial phagocytic clearance of degenerating
RT axons through regulation of Draper.";
RL Cell Rep. 16:1838-1850(2016).
RN [25] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27347682; DOI=10.1371/journal.pone.0158217;
RA Meehan T.L., Joudi T.F., Timmons A.K., Taylor J.D., Habib C.S.,
RA Peterson J.S., Emmanuel S., Franc N.C., McCall K.;
RT "Components of the engulfment machinery have distinct roles in corpse
RT processing.";
RL PLoS ONE 11:E0158217-E0158217(2016).
RN [26]
RP FUNCTION.
RX PubMed=30802937; DOI=10.1002/1873-3468.13348;
RA Draper I., Saha M., Stonebreaker H., Salomon R.N., Matin B., Kang P.B.;
RT "The impact of Megf10/Drpr gain-of-function on muscle development in
RT Drosophila.";
RL FEBS Lett. 593:680-696(2019).
RN [27]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX DOI=10.1093/hmg/ddz064;
RA Saha M., Rizzo S.A., Ramanathan M., Hightower R.M., Santostefano K.E.,
RA Terada N., Finkel R.S., Berg J.S., Chahin N., Pacak C.A., Wagner R.E.,
RA Alexander M.S., Draper I., Kang P.B.;
RT "Selective serotonin reuptake inhibitors ameliorate MEGF10 myopathy.";
RL Hum. Mol. Genet. 2019:0-0(2019).
CC -!- FUNCTION: Receptor which is involved in the phagocytosis of a variety
CC of cells including apoptotic cells, severed and pruned axons,
CC degenerating dendrites, salivary gland cells, germline cells and
CC bacteria (PubMed:15342648, PubMed:16772168, PubMed:16772169,
CC PubMed:18984163, PubMed:20577216, PubMed:22992958, PubMed:24412417).
CC Binds to the ligand prtp which relocates from the endoplasmic reticulum
CC to the cell surface during apoptosis (PubMed:19927123,
CC PubMed:23337816). Ligand-binding may promote tyrosine phosphorylation
CC mediated by Src42a, interaction with shark and subsequent activation of
CC phagocytosis (PubMed:18432193). Also binds to the membrane phospholipid
CC phosphatidylserine which is exposed on the surface of apoptotic cells
CC (PubMed:23420848). Required for the phagocytosis of apoptotic cells by
CC macrophages (PubMed:15342648). Also required for the phagocytosis of
CC apoptotic neurons by glial cells in the embryonic nervous system
CC (PubMed:12765609). Acts downstream of NimC4/simu in the glial
CC phagocytosis of apoptotic neurons (PubMed:18455990). Plays a role in
CC the glial engulfment of larval axons as part of programmed axon pruning
CC during metamorphosis (PubMed:16772168, PubMed:16772170). Also mediates
CC glial cell clearance of severed axons following axonal injury
CC (PubMed:16772169, PubMed:27498858). Required for the engulfment of
CC degenerating dendrites by epidermal cells (PubMed:24412417). Required
CC in the ovary for the engulfment and subsequent processing of dying
CC germline cells by follicular epithelial cells through activation of the
CC JNK/bsk pathway (PubMed:22992958, PubMed:27347682). Plays a role in
CC neuromuscular junction development by mediating the clearance of
CC presynaptic debris and immature boutons which are shed by growing
CC synapses (PubMed:19707574). Required for larval salivary gland cell
CC death which occurs following a rise in steroid levels after puparium
CC formation (PubMed:20577216). Also involved in bacterial phagocytosis
CC (PubMed:18984163). Required for hemocyte phagocytosis of the Gram-
CC positive bacterium S.aureus (PubMed:19890048). Lipoteichoic acid,
CC synthesized by the S.aureus lipoteichoic acid synthase ltaS, acts as a
CC ligand for drpr in this process (PubMed:19890048). Together with Src42a
CC and shark, promotes the migration of macrophages to sites of wounding
CC as part of a signaling cascade where Scr42a detects production of
CC hydrogen peroxide at wound sites which triggers phosphorylation of drpr
CC and subsequent recruitment and activation of shark (PubMed:26028435).
CC Also required for macrophage priming which occurs following
CC phagocytosis of apoptotic cells and ensures that macrophages develop a
CC form of molecular memory that allows them to later mount an
CC inflammatory response to tissue damage and bacterial infection
CC (PubMed:27212238). Is also an essential factor in the regulation of
CC muscle development and myogenesis, and as a consequence is required for
CC normal locomotion (PubMed:12765609, PubMed:25111228, Ref.27). Likely to
CC control the balance between skeletal muscle satellite cells
CC proliferation and differentiation through regulation of the notch
CC signaling pathway (PubMed:25111228, PubMed:30802937, Ref.27).
CC {ECO:0000269|PubMed:12765609, ECO:0000269|PubMed:15342648,
CC ECO:0000269|PubMed:16772168, ECO:0000269|PubMed:16772169,
CC ECO:0000269|PubMed:16772170, ECO:0000269|PubMed:18432193,
CC ECO:0000269|PubMed:18455990, ECO:0000269|PubMed:18984163,
CC ECO:0000269|PubMed:19707574, ECO:0000269|PubMed:19890048,
CC ECO:0000269|PubMed:19927123, ECO:0000269|PubMed:20577216,
CC ECO:0000269|PubMed:22992958, ECO:0000269|PubMed:23337816,
CC ECO:0000269|PubMed:23420848, ECO:0000269|PubMed:24412417,
CC ECO:0000269|PubMed:25111228, ECO:0000269|PubMed:26028435,
CC ECO:0000269|PubMed:27212238, ECO:0000269|PubMed:27347682,
CC ECO:0000269|PubMed:27498858, ECO:0000269|PubMed:30802937,
CC ECO:0000269|Ref.27}.
CC -!- FUNCTION: [Isoform B]: Promotes engulfment of axonal debris by glial
CC cells following axonal injury. {ECO:0000269|PubMed:22426252}.
CC -!- FUNCTION: [Isoform A]: Potently inhibits glial cell engulfment of
CC axonal debris produced following axonal injury.
CC {ECO:0000269|PubMed:22426252}.
CC -!- SUBUNIT: Interacts (via the cytoplasmic domain) with shark; this is
CC required for the recruitment of drpr and glial cells to severed axons
CC and for the phagocytosis of axonal debris by glial cells following axon
CC injury (PubMed:18432193). Interacts with ced-6 (PubMed:16772168).
CC {ECO:0000269|PubMed:16772168, ECO:0000269|PubMed:18432193}.
CC -!- SUBUNIT: [Isoform A]: Interacts with csw; this results in
CC dephosphorylation of drpr isoform A which is required for the
CC inhibition of glial cell engulfment of axonal debris produced following
CC axonal injury (PubMed:22426252). {ECO:0000269|PubMed:22426252}.
CC -!- INTERACTION:
CC Q9W0A0; Q9VYV3: prtp; NbExp=3; IntAct=EBI-107028, EBI-125861;
CC Q9W0A0; Q24145: Shark; NbExp=3; IntAct=EBI-107028, EBI-3403861;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12765609,
CC ECO:0000269|PubMed:18455990, ECO:0000269|PubMed:22992958}; Single-pass
CC type I membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:16772169}. Cytoplasm {ECO:0000269|PubMed:22992958}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:19707574,
CC ECO:0000269|PubMed:22992958}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:27212238}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:27347682}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:27347682}. Note=In olfactory receptor neurons,
CC expressed at low levels along the axon but is up-regulated at severed
CC axons following injury (PubMed:16772169). In follicle cells, detected
CC at the cell membrane and in punctate speckles within the cytoplasm
CC (PubMed:22992958). Also detected in follicle cells on the phagocytic
CC cup and on newly internalized phagosomes (PubMed:27347682). In stage 13
CC macrophages, localizes to punctae around engulfed cell corpses but by
CC stage 15, relocates to the cell cortex (PubMed:27212238).
CC {ECO:0000269|PubMed:16772169, ECO:0000269|PubMed:22992958,
CC ECO:0000269|PubMed:27212238, ECO:0000269|PubMed:27347682}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B {ECO:0000312|FlyBase:FBgn0027594}; Synonyms=Draper-I
CC {ECO:0000303|PubMed:22426252};
CC IsoId=Q9W0A0-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0027594}; Synonyms=Draper-II
CC {ECO:0000303|PubMed:22426252};
CC IsoId=Q9W0A0-2; Sequence=VSP_058652, VSP_058653;
CC Name=C {ECO:0000312|FlyBase:FBgn0027594}; Synonyms=Draper-III
CC {ECO:0000303|PubMed:22426252};
CC IsoId=Q9W0A0-3; Sequence=VSP_058652, VSP_060222, VSP_060223;
CC -!- TISSUE SPECIFICITY: Expressed in adult head (at protein level)
CC (PubMed:22426252). Expressed in glia, macrophages and ectoderm (at
CC protein level) (PubMed:18455990). Detected in glia around the mushroom
CC body dorsal lobe and in glial processes infiltrating the medial lobe
CC (at protein level) (PubMed:16772168). Expressed in adult brain glia
CC including antennal lobe glia (at protein level) (PubMed:16772169).
CC Expressed in the larval fat body (at protein level) (PubMed:20577216).
CC Expressed in the ovary (at protein level) (PubMed:22992958). Isoform B:
CC Predominant isoform in adult glia (PubMed:22426252).
CC {ECO:0000269|PubMed:16772168, ECO:0000269|PubMed:16772169,
CC ECO:0000269|PubMed:18455990, ECO:0000269|PubMed:20577216,
CC ECO:0000269|PubMed:22426252, ECO:0000269|PubMed:22992958}.
CC -!- DEVELOPMENTAL STAGE: In glial cells around the mushroom body dorsal
CC lobe, expression is weak in wandering larvae and pupae at 12 hours
CC after puparium formation (APF) and is elevated in pupae at 6 hours APF
CC (PubMed:16772168). In naive stage 11 macrophages, expressed at low
CC levels with increased levels seen following apoptotic cell corpse
CC uptake and a further increase observed by stage 15 (PubMed:27212238).
CC Isoform A: Selectively expressed in adults (PubMed:22426252).
CC {ECO:0000269|PubMed:16772168, ECO:0000269|PubMed:22426252,
CC ECO:0000269|PubMed:27212238}.
CC -!- INDUCTION: By axon injury which results in up-regulation on severed
CC axons with levels reaching a peak between 12 and 24 hours after injury
CC (at protein level) (PubMed:16772169). By ecdysone (PubMed:16772168).
CC {ECO:0000269|PubMed:16772168, ECO:0000269|PubMed:16772169}.
CC -!- DOMAIN: Isoform B: The intracellular domain is required for glial
CC engulfment activity. Isoform A: The intracellular domain contains an
CC 11-residue insertion compared to isoform B and is incapable of
CC promoting glial engulfment. {ECO:0000269|PubMed:22426252}.
CC -!- PTM: Phosphorylated on tyrosine residues (PubMed:18432193,
CC PubMed:19927123, PubMed:23337816, PubMed:23420848). Phosphorylation is
CC induced by binding to prtp (PubMed:19927123). It is also induced by
CC binding to the membrane phospholipid phosphatidylserine
CC (PubMed:23420848). Phosphorylation may be mediated directly or
CC indirectly by Src42a and is required for interaction with shark
CC (PubMed:18432193). {ECO:0000269|PubMed:18432193,
CC ECO:0000269|PubMed:19927123, ECO:0000269|PubMed:23337816,
CC ECO:0000269|PubMed:23420848}.
CC -!- PTM: [Isoform A]: Dephosphorylated by csw which is required for the
CC inhibition of glial cell engulfment of axonal debris produced following
CC axonal injury. {ECO:0000269|PubMed:22426252}.
CC -!- DISRUPTION PHENOTYPE: Embryos show no defects in early central nervous
CC system (CNS) development but display defective CNS cell corpse
CC engulfment (PubMed:12765609). Increased number and volume of apoptotic
CC particles in the nerve cord (PubMed:18455990). Suppression of glial
CC engulfment of larval axons which results in defective axon pruning with
CC most larval axons remaining in the mushroom body dorsal lobe at 18
CC hours after puparium formation in contrast to the wild-type where most
CC of the larval axons are pruned by this time (PubMed:16772168,
CC PubMed:16772170). Failure of glia to respond to axon injury, resulting
CC in severed axons not being cleared from the CNS (PubMed:16772169).
CC Impaired clearance of degenerating dendrites (PubMed:24412417). Highly
CC abnormal neuromuscular junctions characterized by reduced synaptic
CC growth, the accumulation of presynaptic debris and pruned ghost
CC boutons, and reduced larval mobility (PubMed:19707574). Significant
CC defects in germ cell engulfment by follicle cells (PubMed:22992958).
CC Defective larval salivary gland death with persistance of salivary
CC gland material in 98% of mutants 24 hours after puparium formation
CC (PubMed:20577216). Reduced hemocyte phagocytosis of S.aureus following
CC infection with infected flies dying earlier than controls
CC (PubMed:19890048). Following wounding, impaired migration of
CC macrophages to wound sites (PubMed:26028435). Reduced
CC lifespan.(PubMed:25111228,Ref.27) Reduced climbing performance and
CC impaired motor function with mutants displaying abnormal positioning of
CC the legs and a rapid age-dependent decline in locomotor activity from 3
CC days to 7-10 days of adult life (PubMed:25111228). In 30-40 day old
CC flies, pathological changes in thoracic skeletal muscle, such as loss
CC of striation, variability in fiber size and vacuolization, that mainly
CC affect the tergal depressor of the trochanter.(PubMed:25111228) Marked
CC degeneration and vacuolization of the nervous system including brain
CC and thoracic ventral ganglia, and degeneration of the retina and optic
CC ganglia (PubMed:25111228). RNAi-mediated knockdown results in greatly
CC reduced phagocytosis of apoptotic cells (PubMed:15342648). RNAi-
CC mediated knockdown in neurons does not affect clearance of axon
CC fragments resulting from developmental axon pruning but RNAi-mediated
CC knockdown in glial cells results in defective clearance of axon
CC fragments (PubMed:16772170). RNAi-mediated knockdown in the mesoderm or
CC in adult precursor muscle cells results in impaired locomotor activity
CC which is not seen following RNAi-mediated knockdown in neurons or glia
CC (PubMed:25111228). {ECO:0000269|PubMed:12765609,
CC ECO:0000269|PubMed:15342648, ECO:0000269|PubMed:16772168,
CC ECO:0000269|PubMed:16772169, ECO:0000269|PubMed:16772170,
CC ECO:0000269|PubMed:18455990, ECO:0000269|PubMed:19707574,
CC ECO:0000269|PubMed:19890048, ECO:0000269|PubMed:20577216,
CC ECO:0000269|PubMed:22992958, ECO:0000269|PubMed:24412417,
CC ECO:0000269|PubMed:25111228, ECO:0000269|PubMed:26028435}.
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; AE014296; AAF47552.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47553.3; -; Genomic_DNA.
DR EMBL; AE014296; AFH04220.1; -; Genomic_DNA.
DR EMBL; BT025854; ABF85754.1; -; mRNA.
DR EMBL; BT044170; ACH92235.1; -; mRNA.
DR RefSeq; NP_001246549.1; NM_001259620.2. [Q9W0A0-3]
DR RefSeq; NP_477450.1; NM_058102.3. [Q9W0A0-2]
DR RefSeq; NP_728660.2; NM_167911.3. [Q9W0A0-1]
DR AlphaFoldDB; Q9W0A0; -.
DR SMR; Q9W0A0; -.
DR DIP; DIP-19640N; -.
DR IntAct; Q9W0A0; 3.
DR MINT; Q9W0A0; -.
DR STRING; 7227.FBpp0306204; -.
DR GlyGen; Q9W0A0; 14 sites.
DR PRIDE; Q9W0A0; -.
DR DNASU; 38218; -.
DR EnsemblMetazoa; FBtr0072798; FBpp0072680; FBgn0027594. [Q9W0A0-2]
DR EnsemblMetazoa; FBtr0072799; FBpp0072681; FBgn0027594. [Q9W0A0-1]
DR EnsemblMetazoa; FBtr0309845; FBpp0301579; FBgn0027594. [Q9W0A0-3]
DR GeneID; 38218; -.
DR KEGG; dme:Dmel_CG2086; -.
DR UCSC; CG2086-RA; d. melanogaster.
DR UCSC; CG2086-RB; d. melanogaster. [Q9W0A0-1]
DR CTD; 38218; -.
DR FlyBase; FBgn0027594; drpr.
DR VEuPathDB; VectorBase:FBgn0027594; -.
DR eggNOG; KOG0200; Eukaryota.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000167451; -.
DR InParanoid; Q9W0A0; -.
DR PhylomeDB; Q9W0A0; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-DME-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 38218; 0 hits in 3 CRISPR screens.
DR ChiTaRS; drpr; fly.
DR GenomeRNAi; 38218; -.
DR PRO; PR:Q9W0A0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0027594; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9W0A0; baseline and differential.
DR Genevisible; Q9W0A0; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IMP:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; NAS:FlyBase.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IMP:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:FlyBase.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:FlyBase.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:FlyBase.
DR GO; GO:0071588; P:hydrogen peroxide mediated signaling pathway; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase.
DR GO; GO:0106016; P:positive regulation of inflammatory response to wounding; IGI:FlyBase.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:FlyBase.
DR GO; GO:1904396; P:regulation of neuromuscular junction development; IMP:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; IMP:UniProtKB.
DR GO; GO:0035071; P:salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF00053; Laminin_EGF; 3.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00180; EGF_Lam; 12.
DR PROSITE; PS00022; EGF_1; 13.
DR PROSITE; PS01186; EGF_2; 14.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Phagocytosis; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1031
FT /note="Protein draper"
FT /evidence="ECO:0000255"
FT /id="PRO_5004335548"
FT TOPO_DOM 17..800
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..1031
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 25..100
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 99..129
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 137..172
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 180..215
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 223..258
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 266..301
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 309..344
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 398..433
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 484..519
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 572..607
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 660..695
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 940..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 29..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 55..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 87..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 102..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 106..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 141..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 147..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 162..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 184..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 190..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 205..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 227..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 233..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 248..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 270..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 276..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 291..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 313..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 319..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 334..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 402..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 408..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 423..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 488..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 494..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 509..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 576..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 597..606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 664..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 670..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 685..694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 131..579
FT /note="NCPPGWYGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCADICPEGFFGA
FT NCSEKCRCENGGKCHHVSGECQCAPGFTGPLCDMRCPDGKHGAQCQQDCPCQNDGKCQP
FT ETGACMCNPGWTGDVCANKCPVGSYGPGCQESCECYKGAPCHHITGQCECPPGYRGERC
FT FDECQLNTYGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCAERICEANKYGLDCNR
FT TCECDMEHTDLCHPETGNCQCSIGWSSAQCTRPCTFLRYGPNCELTCNCKNGAKCSPVN
FT GTCLCAPGWRGPTCEESCEPGTFGQDCALRCDCQNGAKCEPETGQCLCTAGWKNIKCDR
FT PCDLNHFGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCERKCDTGKFGHDCAQKCQ
FT CDFNNSLACDATNGRCVCKQDWGGVHCETNCRSGYYGENCDKV -> I (in
FT isoform A and isoform C)"
FT /id="VSP_058652"
FT VAR_SEQ 946
FT /note="P -> PVKIYSKILFPE (in isoform A)"
FT /id="VSP_058653"
FT VAR_SEQ 947..976
FT /note="DEYDHLDYSRPSTSQKPHYHRMNDAMLNIN -> GMSLDFYTGRLSNFTINY
FT VLYICTHYGMNQ (in isoform C)"
FT /id="VSP_060222"
FT VAR_SEQ 977..1031
FT /note="Missing (in isoform C)"
FT /id="VSP_060223"
FT MUTAGEN 858
FT /note="Y->F: Protein still undergoes tyrosine
FT phosphorylation but fails to rescue the defective
FT phagocytosis caused by a loss of endogenous drpr."
FT /evidence="ECO:0000269|PubMed:23337816"
FT MUTAGEN 949
FT /note="Y->F: Markedly reduced interaction with shark. In
FT contrast to the wild-type, does not rescue the ability of
FT macrophages to migrate to a wound when expressed in drpr
FT mutants. Protein still undergoes tyrosine phosphorylation
FT and rescues the defective phagocytosis caused by a loss of
FT endogenous drpr."
FT /evidence="ECO:0000269|PubMed:18432193,
FT ECO:0000269|PubMed:23337816, ECO:0000269|PubMed:26028435"
FT CONFLICT 577
FT /note="D -> Y (in Ref. 3; ABF85754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1031 AA; 113015 MW; A6A0104917D060A9 CRC64;
MLPVILIACL AQLVLAQADL KDLDGPNICK RRELYNVDVV YTELQSFQER GSTWCVTFPP
RCSTYRIKHR VVNKTKTIAK NRIVRDCCDG YIASAGECVP HCSEPCQHGR CISPEKCKCD
HGYGGPACDI NCPPGWYGRN CSMQCDCLNN AVCEPFSGDC ECAKGYTGAR CADICPEGFF
GANCSEKCRC ENGGKCHHVS GECQCAPGFT GPLCDMRCPD GKHGAQCQQD CPCQNDGKCQ
PETGACMCNP GWTGDVCANK CPVGSYGPGC QESCECYKGA PCHHITGQCE CPPGYRGERC
FDECQLNTYG FNCSMTCDCA NDAMCDRANG TCICNPGWTG AKCAERICEA NKYGLDCNRT
CECDMEHTDL CHPETGNCQC SIGWSSAQCT RPCTFLRYGP NCELTCNCKN GAKCSPVNGT
CLCAPGWRGP TCEESCEPGT FGQDCALRCD CQNGAKCEPE TGQCLCTAGW KNIKCDRPCD
LNHFGQDCAK VCDCHNNAAC NPQNGSCTCA AGWTGERCER KCDTGKFGHD CAQKCQCDFN
NSLACDATNG RCVCKQDWGG VHCETNCRSG YYGENCDKVC RCLNNSSCDP DSGNCICSAG
WTGADCAEPC PPGFYGMECK ERCPEILHGN KSCDHITGEI LCRTGYIGLT CEHPCPAGLY
GPGCKLKCNC EHGGECNHVT GQCQCLPGWT GSNCNESCPT DTYGQGCAQR CRCVHHKVCR
KADGMCICET GWSGTRCDEV CPEGFYGEHC MNTCACPSAN FQCHAAHGCV CRSGYTGDNC
DELIASQRIA DQSENSSRAS VALTLVLMTL FACIIFAVFI YYRRRVSNLK TEIAHVHYTH
DTNPPSWPPN HNFDNPVYGM QAETRLLPNN MRSKMNNFDQ RSTMSTDYGD DCNASGRVGS
YSINYNHDLL TKNLNADRTN PIVYNESLKE EHVYDEIKHK EGYKDPDEYD HLDYSRPSTS
QKPHYHRMND AMLNINQDEE KPSNVKNMTV LLNKPLPPTE PEPQHECFDN TNTNLDNVST
ASPSSSPKFL K
