Q9W0A0 · DRPR_DROME
- ProteinProtein draper
- Genedrpr
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1031 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor which is involved in the phagocytosis of a variety of cells including apoptotic cells, severed and pruned axons, degenerating dendrites, salivary gland cells, germline cells and bacteria (PubMed:15342648, PubMed:16772168, PubMed:16772169, PubMed:18984163, PubMed:20577216, PubMed:22992958, PubMed:24412417).
Binds to the ligand prtp which relocates from the endoplasmic reticulum to the cell surface during apoptosis (PubMed:19927123, PubMed:23337816).
Ligand-binding may promote tyrosine phosphorylation mediated by Src42a, interaction with shark and subsequent activation of phagocytosis (PubMed:18432193).
Also binds to the membrane phospholipid phosphatidylserine which is exposed on the surface of apoptotic cells (PubMed:23420848).
Required for the phagocytosis of apoptotic cells by macrophages (PubMed:15342648).
Also required for the phagocytosis of apoptotic neurons by glial cells in the embryonic nervous system (PubMed:12765609).
Acts downstream of NimC4/simu in the glial phagocytosis of apoptotic neurons (PubMed:18455990).
Plays a role in the glial engulfment of larval axons as part of programmed axon pruning during metamorphosis (PubMed:16772168, PubMed:16772170).
Also mediates glial cell clearance of severed axons following axonal injury (PubMed:16772169, PubMed:27498858).
Required for the engulfment of degenerating dendrites by epidermal cells (PubMed:24412417).
Required in the ovary for the engulfment and subsequent processing of dying germline cells by follicular epithelial cells through activation of the JNK/bsk pathway (PubMed:22992958, PubMed:27347682).
Plays a role in neuromuscular junction development by mediating the clearance of presynaptic debris and immature boutons which are shed by growing synapses (PubMed:19707574).
Required for larval salivary gland cell death which occurs following a rise in steroid levels after puparium formation (PubMed:20577216).
Also involved in bacterial phagocytosis (PubMed:18984163).
Required for hemocyte phagocytosis of the Gram-positive bacterium S.aureus (PubMed:19890048).
Lipoteichoic acid, synthesized by the S.aureus lipoteichoic acid synthase ltaS, acts as a ligand for drpr in this process (PubMed:19890048).
Together with Src42a and shark, promotes the migration of macrophages to sites of wounding as part of a signaling cascade where Scr42a detects production of hydrogen peroxide at wound sites which triggers phosphorylation of drpr and subsequent recruitment and activation of shark (PubMed:26028435).
Also required for macrophage priming which occurs following phagocytosis of apoptotic cells and ensures that macrophages develop a form of molecular memory that allows them to later mount an inflammatory response to tissue damage and bacterial infection (PubMed:27212238).
Is also an essential factor in the regulation of muscle development and myogenesis, and as a consequence is required for normal locomotion (PubMed:12765609, PubMed:25111228, Ref.27). Likely to control the balance between skeletal muscle satellite cells proliferation and differentiation through regulation of the notch signaling pathway (PubMed:25111228, PubMed:30802937, Ref.27).
Binds to the ligand prtp which relocates from the endoplasmic reticulum to the cell surface during apoptosis (PubMed:19927123, PubMed:23337816).
Ligand-binding may promote tyrosine phosphorylation mediated by Src42a, interaction with shark and subsequent activation of phagocytosis (PubMed:18432193).
Also binds to the membrane phospholipid phosphatidylserine which is exposed on the surface of apoptotic cells (PubMed:23420848).
Required for the phagocytosis of apoptotic cells by macrophages (PubMed:15342648).
Also required for the phagocytosis of apoptotic neurons by glial cells in the embryonic nervous system (PubMed:12765609).
Acts downstream of NimC4/simu in the glial phagocytosis of apoptotic neurons (PubMed:18455990).
Plays a role in the glial engulfment of larval axons as part of programmed axon pruning during metamorphosis (PubMed:16772168, PubMed:16772170).
Also mediates glial cell clearance of severed axons following axonal injury (PubMed:16772169, PubMed:27498858).
Required for the engulfment of degenerating dendrites by epidermal cells (PubMed:24412417).
Required in the ovary for the engulfment and subsequent processing of dying germline cells by follicular epithelial cells through activation of the JNK/bsk pathway (PubMed:22992958, PubMed:27347682).
Plays a role in neuromuscular junction development by mediating the clearance of presynaptic debris and immature boutons which are shed by growing synapses (PubMed:19707574).
Required for larval salivary gland cell death which occurs following a rise in steroid levels after puparium formation (PubMed:20577216).
Also involved in bacterial phagocytosis (PubMed:18984163).
Required for hemocyte phagocytosis of the Gram-positive bacterium S.aureus (PubMed:19890048).
Lipoteichoic acid, synthesized by the S.aureus lipoteichoic acid synthase ltaS, acts as a ligand for drpr in this process (PubMed:19890048).
Together with Src42a and shark, promotes the migration of macrophages to sites of wounding as part of a signaling cascade where Scr42a detects production of hydrogen peroxide at wound sites which triggers phosphorylation of drpr and subsequent recruitment and activation of shark (PubMed:26028435).
Also required for macrophage priming which occurs following phagocytosis of apoptotic cells and ensures that macrophages develop a form of molecular memory that allows them to later mount an inflammatory response to tissue damage and bacterial infection (PubMed:27212238).
Is also an essential factor in the regulation of muscle development and myogenesis, and as a consequence is required for normal locomotion (PubMed:12765609, PubMed:25111228, Ref.27). Likely to control the balance between skeletal muscle satellite cells proliferation and differentiation through regulation of the notch signaling pathway (PubMed:25111228, PubMed:30802937, Ref.27).
Isoform B
Promotes engulfment of axonal debris by glial cells following axonal injury.
Isoform A
Potently inhibits glial cell engulfment of axonal debris produced following axonal injury.
GO annotations
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameProtein draper
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9W0A0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: In olfactory receptor neurons, expressed at low levels along the axon but is up-regulated at severed axons following injury (PubMed:16772169).
In follicle cells, detected at the cell membrane and in punctate speckles within the cytoplasm (PubMed:22992958).
Also detected in follicle cells on the phagocytic cup and on newly internalized phagosomes (PubMed:27347682).
In stage 13 macrophages, localizes to punctae around engulfed cell corpses but by stage 15, relocates to the cell cortex (PubMed:27212238).
In follicle cells, detected at the cell membrane and in punctate speckles within the cytoplasm (PubMed:22992958).
Also detected in follicle cells on the phagocytic cup and on newly internalized phagosomes (PubMed:27347682).
In stage 13 macrophages, localizes to punctae around engulfed cell corpses but by stage 15, relocates to the cell cortex (PubMed:27212238).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 17-800 | Extracellular | ||||
Sequence: QADLKDLDGPNICKRRELYNVDVVYTELQSFQERGSTWCVTFPPRCSTYRIKHRVVNKTKTIAKNRIVRDCCDGYIASAGECVPHCSEPCQHGRCISPEKCKCDHGYGGPACDINCPPGWYGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCADICPEGFFGANCSEKCRCENGGKCHHVSGECQCAPGFTGPLCDMRCPDGKHGAQCQQDCPCQNDGKCQPETGACMCNPGWTGDVCANKCPVGSYGPGCQESCECYKGAPCHHITGQCECPPGYRGERCFDECQLNTYGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCAERICEANKYGLDCNRTCECDMEHTDLCHPETGNCQCSIGWSSAQCTRPCTFLRYGPNCELTCNCKNGAKCSPVNGTCLCAPGWRGPTCEESCEPGTFGQDCALRCDCQNGAKCEPETGQCLCTAGWKNIKCDRPCDLNHFGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCERKCDTGKFGHDCAQKCQCDFNNSLACDATNGRCVCKQDWGGVHCETNCRSGYYGENCDKVCRCLNNSSCDPDSGNCICSAGWTGADCAEPCPPGFYGMECKERCPEILHGNKSCDHITGEILCRTGYIGLTCEHPCPAGLYGPGCKLKCNCEHGGECNHVTGQCQCLPGWTGSNCNESCPTDTYGQGCAQRCRCVHHKVCRKADGMCICETGWSGTRCDEVCPEGFYGEHCMNTCACPSANFQCHAAHGCVCRSGYTGDNCDELIASQRIADQSENSSRAS | ||||||
Transmembrane | 801-821 | Helical | ||||
Sequence: VALTLVLMTLFACIIFAVFIY | ||||||
Topological domain | 822-1031 | Cytoplasmic | ||||
Sequence: YRRRVSNLKTEIAHVHYTHDTNPPSWPPNHNFDNPVYGMQAETRLLPNNMRSKMNNFDQRSTMSTDYGDDCNASGRVGSYSINYNHDLLTKNLNADRTNPIVYNESLKEEHVYDEIKHKEGYKDPDEYDHLDYSRPSTSQKPHYHRMNDAMLNINQDEEKPSNVKNMTVLLNKPLPPTEPEPQHECFDNTNTNLDNVSTASPSSSPKFLK |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryos show no defects in early central nervous system (CNS) development but display defective CNS cell corpse engulfment (PubMed:12765609).
Increased number and volume of apoptotic particles in the nerve cord (PubMed:18455990).
Suppression of glial engulfment of larval axons which results in defective axon pruning with most larval axons remaining in the mushroom body dorsal lobe at 18 hours after puparium formation in contrast to the wild-type where most of the larval axons are pruned by this time (PubMed:16772168, PubMed:16772170).
Failure of glia to respond to axon injury, resulting in severed axons not being cleared from the CNS (PubMed:16772169).
Impaired clearance of degenerating dendrites (PubMed:24412417).
Highly abnormal neuromuscular junctions characterized by reduced synaptic growth, the accumulation of presynaptic debris and pruned ghost boutons, and reduced larval mobility (PubMed:19707574).
Significant defects in germ cell engulfment by follicle cells (PubMed:22992958).
Defective larval salivary gland death with persistance of salivary gland material in 98% of mutants 24 hours after puparium formation (PubMed:20577216).
Reduced hemocyte phagocytosis of S.aureus following infection with infected flies dying earlier than controls (PubMed:19890048).
Following wounding, impaired migration of macrophages to wound sites (PubMed:26028435).
Reduced lifespan (PubMed:25111228, Ref.27). Reduced climbing performance and impaired motor function with mutants displaying abnormal positioning of the legs and a rapid age-dependent decline in locomotor activity from 3 days to 7-10 days of adult life (PubMed:25111228).
In 30-40 day old flies, pathological changes in thoracic skeletal muscle, such as loss of striation, variability in fiber size and vacuolization, that mainly affect the tergal depressor of the trochanter.(PubMed:25111228) Marked degeneration and vacuolization of the nervous system including brain and thoracic ventral ganglia, and degeneration of the retina and optic ganglia (PubMed:25111228).
RNAi-mediated knockdown results in greatly reduced phagocytosis of apoptotic cells (PubMed:15342648).
RNAi-mediated knockdown in neurons does not affect clearance of axon fragments resulting from developmental axon pruning but RNAi-mediated knockdown in glial cells results in defective clearance of axon fragments (PubMed:16772170).
RNAi-mediated knockdown in the mesoderm or in adult precursor muscle cells results in impaired locomotor activity which is not seen following RNAi-mediated knockdown in neurons or glia (PubMed:25111228).
Increased number and volume of apoptotic particles in the nerve cord (PubMed:18455990).
Suppression of glial engulfment of larval axons which results in defective axon pruning with most larval axons remaining in the mushroom body dorsal lobe at 18 hours after puparium formation in contrast to the wild-type where most of the larval axons are pruned by this time (PubMed:16772168, PubMed:16772170).
Failure of glia to respond to axon injury, resulting in severed axons not being cleared from the CNS (PubMed:16772169).
Impaired clearance of degenerating dendrites (PubMed:24412417).
Highly abnormal neuromuscular junctions characterized by reduced synaptic growth, the accumulation of presynaptic debris and pruned ghost boutons, and reduced larval mobility (PubMed:19707574).
Significant defects in germ cell engulfment by follicle cells (PubMed:22992958).
Defective larval salivary gland death with persistance of salivary gland material in 98% of mutants 24 hours after puparium formation (PubMed:20577216).
Reduced hemocyte phagocytosis of S.aureus following infection with infected flies dying earlier than controls (PubMed:19890048).
Following wounding, impaired migration of macrophages to wound sites (PubMed:26028435).
Reduced lifespan (PubMed:25111228, Ref.27). Reduced climbing performance and impaired motor function with mutants displaying abnormal positioning of the legs and a rapid age-dependent decline in locomotor activity from 3 days to 7-10 days of adult life (PubMed:25111228).
In 30-40 day old flies, pathological changes in thoracic skeletal muscle, such as loss of striation, variability in fiber size and vacuolization, that mainly affect the tergal depressor of the trochanter.(PubMed:25111228) Marked degeneration and vacuolization of the nervous system including brain and thoracic ventral ganglia, and degeneration of the retina and optic ganglia (PubMed:25111228).
RNAi-mediated knockdown results in greatly reduced phagocytosis of apoptotic cells (PubMed:15342648).
RNAi-mediated knockdown in neurons does not affect clearance of axon fragments resulting from developmental axon pruning but RNAi-mediated knockdown in glial cells results in defective clearance of axon fragments (PubMed:16772170).
RNAi-mediated knockdown in the mesoderm or in adult precursor muscle cells results in impaired locomotor activity which is not seen following RNAi-mediated knockdown in neurons or glia (PubMed:25111228).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 858 | Protein still undergoes tyrosine phosphorylation but fails to rescue the defective phagocytosis caused by a loss of endogenous drpr. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 949 | Markedly reduced interaction with shark. In contrast to the wild-type, does not rescue the ability of macrophages to migrate to a wound when expressed in drpr mutants. Protein still undergoes tyrosine phosphorylation and rescues the defective phagocytosis caused by a loss of endogenous drpr. | ||||
Sequence: Y → F |
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MLPVILIACLAQLVLA | ||||||
Chain | PRO_5004335548 | 17-1031 | Protein draper | |||
Sequence: QADLKDLDGPNICKRRELYNVDVVYTELQSFQERGSTWCVTFPPRCSTYRIKHRVVNKTKTIAKNRIVRDCCDGYIASAGECVPHCSEPCQHGRCISPEKCKCDHGYGGPACDINCPPGWYGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCADICPEGFFGANCSEKCRCENGGKCHHVSGECQCAPGFTGPLCDMRCPDGKHGAQCQQDCPCQNDGKCQPETGACMCNPGWTGDVCANKCPVGSYGPGCQESCECYKGAPCHHITGQCECPPGYRGERCFDECQLNTYGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCAERICEANKYGLDCNRTCECDMEHTDLCHPETGNCQCSIGWSSAQCTRPCTFLRYGPNCELTCNCKNGAKCSPVNGTCLCAPGWRGPTCEESCEPGTFGQDCALRCDCQNGAKCEPETGQCLCTAGWKNIKCDRPCDLNHFGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCERKCDTGKFGHDCAQKCQCDFNNSLACDATNGRCVCKQDWGGVHCETNCRSGYYGENCDKVCRCLNNSSCDPDSGNCICSAGWTGADCAEPCPPGFYGMECKERCPEILHGNKSCDHITGEILCRTGYIGLTCEHPCPAGLYGPGCKLKCNCEHGGECNHVTGQCQCLPGWTGSNCNESCPTDTYGQGCAQRCRCVHHKVCRKADGMCICETGWSGTRCDEVCPEGFYGEHCMNTCACPSANFQCHAAHGCVCRSGYTGDNCDELIASQRIADQSENSSRASVALTLVLMTLFACIIFAVFIYYRRRVSNLKTEIAHVHYTHDTNPPSWPPNHNFDNPVYGMQAETRLLPNNMRSKMNNFDQRSTMSTDYGDDCNASGRVGSYSINYNHDLLTKNLNADRTNPIVYNESLKEEHVYDEIKHKEGYKDPDEYDHLDYSRPSTSQKPHYHRMNDAMLNINQDEEKPSNVKNMTVLLNKPLPPTEPEPQHECFDNTNTNLDNVSTASPSSSPKFLK | ||||||
Disulfide bond | 29↔88 | |||||
Sequence: CKRRELYNVDVVYTELQSFQERGSTWCVTFPPRCSTYRIKHRVVNKTKTIAKNRIVRDCC | ||||||
Disulfide bond | 55↔62 | |||||
Sequence: CVTFPPRC | ||||||
Glycosylation | 73 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 87↔98 | |||||
Sequence: CCDGYIASAGEC | ||||||
Disulfide bond | 102↔111 | |||||
Sequence: CSEPCQHGRC | ||||||
Disulfide bond | 106↔117 | |||||
Sequence: CQHGRCISPEKC | ||||||
Disulfide bond | 119↔128 | |||||
Sequence: CDHGYGGPAC | ||||||
Glycosylation | 140 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 141↔153 | |||||
Sequence: CSMQCDCLNNAVC | ||||||
Disulfide bond | 147↔160 | |||||
Sequence: CLNNAVCEPFSGDC | ||||||
Disulfide bond | 162↔171 | |||||
Sequence: CAKGYTGARC | ||||||
Glycosylation | 183 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 184↔196 | |||||
Sequence: CSEKCRCENGGKC | ||||||
Disulfide bond | 190↔203 | |||||
Sequence: CENGGKCHHVSGEC | ||||||
Disulfide bond | 205↔214 | |||||
Sequence: CAPGFTGPLC | ||||||
Disulfide bond | 227↔239 | |||||
Sequence: CQQDCPCQNDGKC | ||||||
Disulfide bond | 233↔246 | |||||
Sequence: CQNDGKCQPETGAC | ||||||
Disulfide bond | 248↔257 | |||||
Sequence: CNPGWTGDVC | ||||||
Disulfide bond | 270↔282 | |||||
Sequence: CQESCECYKGAPC | ||||||
Disulfide bond | 276↔289 | |||||
Sequence: CYKGAPCHHITGQC | ||||||
Disulfide bond | 291↔300 | |||||
Sequence: CPPGYRGERC | ||||||
Glycosylation | 312 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 313↔325 | |||||
Sequence: CSMTCDCANDAMC | ||||||
Disulfide bond | 319↔332 | |||||
Sequence: CANDAMCDRANGTC | ||||||
Glycosylation | 329 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 334↔343 | |||||
Sequence: CNPGWTGAKC | ||||||
Glycosylation | 358 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 402↔414 | |||||
Sequence: CELTCNCKNGAKC | ||||||
Disulfide bond | 408↔421 | |||||
Sequence: CKNGAKCSPVNGTC | ||||||
Glycosylation | 418 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 423↔432 | |||||
Sequence: CAPGWRGPTC | ||||||
Disulfide bond | 488↔500 | |||||
Sequence: CAKVCDCHNNAAC | ||||||
Disulfide bond | 494↔507 | |||||
Sequence: CHNNAACNPQNGSC | ||||||
Glycosylation | 504 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 509↔518 | |||||
Sequence: CAAGWTGERC | ||||||
Glycosylation | 540 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 576↔588 | |||||
Sequence: CDKVCRCLNNSSC | ||||||
Disulfide bond | 582↔595 | |||||
Sequence: CLNNSSCDPDSGNC | ||||||
Glycosylation | 584 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 585 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 597↔606 | |||||
Sequence: CSAGWTGADC | ||||||
Glycosylation | 630 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 664↔676 | |||||
Sequence: CKLKCNCEHGGEC | ||||||
Disulfide bond | 670↔683 | |||||
Sequence: CEHGGECNHVTGQC | ||||||
Disulfide bond | 685↔694 | |||||
Sequence: CLPGWTGSNC | ||||||
Glycosylation | 695 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 795 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Phosphorylated on tyrosine residues (PubMed:18432193, PubMed:19927123, PubMed:23337816, PubMed:23420848).
Phosphorylation is induced by binding to prtp (PubMed:19927123).
It is also induced by binding to the membrane phospholipid phosphatidylserine (PubMed:23420848).
Phosphorylation may be mediated directly or indirectly by Src42a and is required for interaction with shark (PubMed:18432193).
Phosphorylation is induced by binding to prtp (PubMed:19927123).
It is also induced by binding to the membrane phospholipid phosphatidylserine (PubMed:23420848).
Phosphorylation may be mediated directly or indirectly by Src42a and is required for interaction with shark (PubMed:18432193).
Isoform A
Dephosphorylated by csw which is required for the inhibition of glial cell engulfment of axonal debris produced following axonal injury.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in adult head (at protein level) (PubMed:22426252).
Expressed in glia, macrophages and ectoderm (at protein level) (PubMed:18455990).
Detected in glia around the mushroom body dorsal lobe and in glial processes infiltrating the medial lobe (at protein level) (PubMed:16772168).
Expressed in adult brain glia including antennal lobe glia (at protein level) (PubMed:16772169).
Expressed in the larval fat body (at protein level) (PubMed:20577216).
Expressed in the ovary (at protein level) (PubMed:22992958).
Isoform B: Predominant isoform in adult glia (PubMed:22426252).
Expressed in glia, macrophages and ectoderm (at protein level) (PubMed:18455990).
Detected in glia around the mushroom body dorsal lobe and in glial processes infiltrating the medial lobe (at protein level) (PubMed:16772168).
Expressed in adult brain glia including antennal lobe glia (at protein level) (PubMed:16772169).
Expressed in the larval fat body (at protein level) (PubMed:20577216).
Expressed in the ovary (at protein level) (PubMed:22992958).
Isoform B: Predominant isoform in adult glia (PubMed:22426252).
Induction
By axon injury which results in up-regulation on severed axons with levels reaching a peak between 12 and 24 hours after injury (at protein level) (PubMed:16772169).
By ecdysone (PubMed:16772168).
By detection of apoptotic cells (PubMed:34860835).
By ecdysone (PubMed:16772168).
By detection of apoptotic cells (PubMed:34860835).
Developmental stage
In glial cells around the mushroom body dorsal lobe, expression is weak in wandering larvae and pupae at 12 hours after puparium formation (APF) and is elevated in pupae at 6 hours APF (PubMed:16772168).
In naive stage 11 macrophages, expressed at low levels with increased levels seen following apoptotic cell corpse uptake and a further increase observed by stage 15 (PubMed:27212238).
Isoform A: Selectively expressed in adults (PubMed:22426252).
In naive stage 11 macrophages, expressed at low levels with increased levels seen following apoptotic cell corpse uptake and a further increase observed by stage 15 (PubMed:27212238).
Isoform A: Selectively expressed in adults (PubMed:22426252).
Gene expression databases
Interaction
Subunit
Interacts (via the cytoplasmic domain) with shark; this is required for the recruitment of drpr and glial cells to severed axons and for the phagocytosis of axonal debris by glial cells following axon injury (PubMed:18432193).
Interacts with ced-6 (PubMed:16772168).
Interacts with ced-6 (PubMed:16772168).
Isoform A
Interacts with csw; this results in dephosphorylation of drpr isoform A which is required for the inhibition of glial cell engulfment of axonal debris produced following axonal injury (PubMed:22426252).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9W0A0 | prtp Q9VYV3 | 3 | EBI-107028, EBI-125861 | |
BINARY | Q9W0A0 | Shark Q24145 | 3 | EBI-107028, EBI-3403861 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-100 | EMI | ||||
Sequence: GPNICKRRELYNVDVVYTELQSFQERGSTWCVTFPPRCSTYRIKHRVVNKTKTIAKNRIVRDCCDGYIASAGECVP | ||||||
Domain | 99-129 | EGF-like 1 | ||||
Sequence: VPHCSEPCQHGRCISPEKCKCDHGYGGPACD | ||||||
Domain | 137-172 | EGF-like 2 | ||||
Sequence: YGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCA | ||||||
Domain | 180-215 | EGF-like 3 | ||||
Sequence: FGANCSEKCRCENGGKCHHVSGECQCAPGFTGPLCD | ||||||
Domain | 223-258 | EGF-like 4 | ||||
Sequence: HGAQCQQDCPCQNDGKCQPETGACMCNPGWTGDVCA | ||||||
Domain | 266-301 | EGF-like 5 | ||||
Sequence: YGPGCQESCECYKGAPCHHITGQCECPPGYRGERCF | ||||||
Domain | 309-344 | EGF-like 6 | ||||
Sequence: YGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCA | ||||||
Domain | 398-433 | EGF-like 7 | ||||
Sequence: YGPNCELTCNCKNGAKCSPVNGTCLCAPGWRGPTCE | ||||||
Domain | 484-519 | EGF-like 8 | ||||
Sequence: FGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCE | ||||||
Domain | 572-607 | EGF-like 9 | ||||
Sequence: YGENCDKVCRCLNNSSCDPDSGNCICSAGWTGADCA | ||||||
Domain | 660-695 | EGF-like 10 | ||||
Sequence: YGPGCKLKCNCEHGGECNHVTGQCQCLPGWTGSNCN | ||||||
Compositional bias | 940-957 | Basic and acidic residues | ||||
Sequence: KEGYKDPDEYDHLDYSRP | ||||||
Region | 940-964 | Disordered | ||||
Sequence: KEGYKDPDEYDHLDYSRPSTSQKPH | ||||||
Region | 988-1031 | Disordered | ||||
Sequence: MTVLLNKPLPPTEPEPQHECFDNTNTNLDNVSTASPSSSPKFLK | ||||||
Compositional bias | 1005-1031 | Polar residues | ||||
Sequence: HECFDNTNTNLDNVSTASPSSSPKFLK |
Domain
Isoform B: The intracellular domain is required for glial engulfment activity. Isoform A: The intracellular domain contains an 11-residue insertion compared to isoform B and is incapable of promoting glial engulfment.
Sequence similarities
Belongs to the MEGF family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
Q9W0A0-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameB
- SynonymsDraper-I
- Length1,031
- Mass (Da)113,015
- Last updated2007-12-04 v3
- ChecksumA6A0104917D060A9
Q9W0A0-2
- NameA
- SynonymsDraper-II
- Differences from canonical
- 131-579: NCPPGWYGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCADICPEGFFGANCSEKCRCENGGKCHHVSGECQCAPGFTGPLCDMRCPDGKHGAQCQQDCPCQNDGKCQPETGACMCNPGWTGDVCANKCPVGSYGPGCQESCECYKGAPCHHITGQCECPPGYRGERCFDECQLNTYGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCAERICEANKYGLDCNRTCECDMEHTDLCHPETGNCQCSIGWSSAQCTRPCTFLRYGPNCELTCNCKNGAKCSPVNGTCLCAPGWRGPTCEESCEPGTFGQDCALRCDCQNGAKCEPETGQCLCTAGWKNIKCDRPCDLNHFGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCERKCDTGKFGHDCAQKCQCDFNNSLACDATNGRCVCKQDWGGVHCETNCRSGYYGENCDKV → I
- 946-946: P → PVKIYSKILFPE
Q9W0A0-3
- NameC
- SynonymsDraper-III
- Differences from canonical
- 131-579: NCPPGWYGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCADICPEGFFGANCSEKCRCENGGKCHHVSGECQCAPGFTGPLCDMRCPDGKHGAQCQQDCPCQNDGKCQPETGACMCNPGWTGDVCANKCPVGSYGPGCQESCECYKGAPCHHITGQCECPPGYRGERCFDECQLNTYGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCAERICEANKYGLDCNRTCECDMEHTDLCHPETGNCQCSIGWSSAQCTRPCTFLRYGPNCELTCNCKNGAKCSPVNGTCLCAPGWRGPTCEESCEPGTFGQDCALRCDCQNGAKCEPETGQCLCTAGWKNIKCDRPCDLNHFGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCERKCDTGKFGHDCAQKCQCDFNNSLACDATNGRCVCKQDWGGVHCETNCRSGYYGENCDKV → I
- 947-976: DEYDHLDYSRPSTSQKPHYHRMNDAMLNIN → GMSLDFYTGRLSNFTINYVLYICTHYGMNQ
- 977-1031: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_058652 | 131-579 | in isoform A and isoform C | |||
Sequence: NCPPGWYGRNCSMQCDCLNNAVCEPFSGDCECAKGYTGARCADICPEGFFGANCSEKCRCENGGKCHHVSGECQCAPGFTGPLCDMRCPDGKHGAQCQQDCPCQNDGKCQPETGACMCNPGWTGDVCANKCPVGSYGPGCQESCECYKGAPCHHITGQCECPPGYRGERCFDECQLNTYGFNCSMTCDCANDAMCDRANGTCICNPGWTGAKCAERICEANKYGLDCNRTCECDMEHTDLCHPETGNCQCSIGWSSAQCTRPCTFLRYGPNCELTCNCKNGAKCSPVNGTCLCAPGWRGPTCEESCEPGTFGQDCALRCDCQNGAKCEPETGQCLCTAGWKNIKCDRPCDLNHFGQDCAKVCDCHNNAACNPQNGSCTCAAGWTGERCERKCDTGKFGHDCAQKCQCDFNNSLACDATNGRCVCKQDWGGVHCETNCRSGYYGENCDKV → I | ||||||
Sequence conflict | 577 | in Ref. 3; ABF85754 | ||||
Sequence: D → Y | ||||||
Compositional bias | 940-957 | Basic and acidic residues | ||||
Sequence: KEGYKDPDEYDHLDYSRP | ||||||
Alternative sequence | VSP_058653 | 946 | in isoform A | |||
Sequence: P → PVKIYSKILFPE | ||||||
Alternative sequence | VSP_060222 | 947-976 | in isoform C | |||
Sequence: DEYDHLDYSRPSTSQKPHYHRMNDAMLNIN → GMSLDFYTGRLSNFTINYVLYICTHYGMNQ | ||||||
Alternative sequence | VSP_060223 | 977-1031 | in isoform C | |||
Sequence: Missing | ||||||
Compositional bias | 1005-1031 | Polar residues | ||||
Sequence: HECFDNTNTNLDNVSTASPSSSPKFLK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014296 EMBL· GenBank· DDBJ | AAF47552.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF47553.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AFH04220.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT025854 EMBL· GenBank· DDBJ | ABF85754.1 EMBL· GenBank· DDBJ | mRNA | ||
BT044170 EMBL· GenBank· DDBJ | ACH92235.1 EMBL· GenBank· DDBJ | mRNA |