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Entry version 155 (13 Nov 2019)
Sequence version 3 (04 Dec 2007)
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Protein

Protein draper

Gene

drpr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).23 Publications
Isoform B: Promotes engulfment of axonal debris by glial cells following axonal injury.1 Publication
Isoform A: Potently inhibits glial cell engulfment of axonal debris produced following axonal injury.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionReceptor
Biological processPhagocytosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-114608 Platelet degranulation
R-DME-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-DME-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-DME-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-DME-8957275 Post-translational protein phosphorylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein draperImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:drpr1 PublicationImported
Synonyms:Megf10
ORF Names:CG2086Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDrosophila melanogaster (Fruit fly)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri7227 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000803 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0027594 drpr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini17 – 800ExtracellularCuratedAdd BLAST784
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei801 – 821HelicalSequence analysisAdd BLAST21
Topological domaini822 – 1031CytoplasmicCuratedAdd BLAST210

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Postsynaptic cell membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

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).13 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi858Y → F: Protein still undergoes tyrosine phosphorylation but fails to rescue the defective phagocytosis caused by a loss of endogenous drpr. 1 Publication1
Mutagenesisi949Y → F: 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. 3 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 16Sequence analysisAdd BLAST16
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500433554817 – 1031Protein draperSequence analysisAdd BLAST1015

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi29 ↔ 88PROSITE-ProRule annotation
Disulfide bondi55 ↔ 62PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi73N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi87 ↔ 98PROSITE-ProRule annotation
Disulfide bondi102 ↔ 111PROSITE-ProRule annotation
Disulfide bondi106 ↔ 117PROSITE-ProRule annotation
Disulfide bondi119 ↔ 128PROSITE-ProRule annotation
Glycosylationi140N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi141 ↔ 153PROSITE-ProRule annotation
Disulfide bondi147 ↔ 160PROSITE-ProRule annotation
Disulfide bondi162 ↔ 171PROSITE-ProRule annotation
Glycosylationi183N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi184 ↔ 196PROSITE-ProRule annotation
Disulfide bondi190 ↔ 203PROSITE-ProRule annotation
Disulfide bondi205 ↔ 214PROSITE-ProRule annotation
Disulfide bondi227 ↔ 239PROSITE-ProRule annotation
Disulfide bondi233 ↔ 246PROSITE-ProRule annotation
Disulfide bondi248 ↔ 257PROSITE-ProRule annotation
Disulfide bondi270 ↔ 282PROSITE-ProRule annotation
Disulfide bondi276 ↔ 289PROSITE-ProRule annotation
Disulfide bondi291 ↔ 300PROSITE-ProRule annotation
Glycosylationi312N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi313 ↔ 325PROSITE-ProRule annotation
Disulfide bondi319 ↔ 332PROSITE-ProRule annotation
Glycosylationi329N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi334 ↔ 343PROSITE-ProRule annotation
Glycosylationi358N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi402 ↔ 414PROSITE-ProRule annotation
Disulfide bondi408 ↔ 421PROSITE-ProRule annotation
Glycosylationi418N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi423 ↔ 432PROSITE-ProRule annotation
Disulfide bondi488 ↔ 500PROSITE-ProRule annotation
Disulfide bondi494 ↔ 507PROSITE-ProRule annotation
Glycosylationi504N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi509 ↔ 518PROSITE-ProRule annotation
Glycosylationi540N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi576 ↔ 588PROSITE-ProRule annotation
Disulfide bondi582 ↔ 595PROSITE-ProRule annotation
Glycosylationi584N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi585N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi597 ↔ 606PROSITE-ProRule annotation
Glycosylationi630N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi664 ↔ 676PROSITE-ProRule annotation
Disulfide bondi670 ↔ 683PROSITE-ProRule annotation
Disulfide bondi685 ↔ 694PROSITE-ProRule annotation
Glycosylationi695N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi795N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).4 Publications
Isoform A: Dephosphorylated by csw which is required for the inhibition of glial cell engulfment of axonal debris produced following axonal injury.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q9W0A0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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).6 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
FBgn0027594 Expressed in 34 organ(s), highest expression level in embryo

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9W0A0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9W0A0 DM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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). 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).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-19640N

Protein interaction database and analysis system

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IntActi
Q9W0A0, 3 interactors

Molecular INTeraction database

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MINTi
Q9W0A0

STRING: functional protein association networks

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STRINGi
7227.FBpp0306204

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9W0A0

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini25 – 100EMIPROSITE-ProRule annotationAdd BLAST76
Domaini99 – 129EGF-like 1PROSITE-ProRule annotationAdd BLAST31
Domaini137 – 172EGF-like 2PROSITE-ProRule annotationAdd BLAST36
Domaini180 – 215EGF-like 3PROSITE-ProRule annotationAdd BLAST36
Domaini223 – 258EGF-like 4PROSITE-ProRule annotationAdd BLAST36
Domaini266 – 301EGF-like 5PROSITE-ProRule annotationAdd BLAST36
Domaini309 – 344EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini398 – 433EGF-like 7PROSITE-ProRule annotationAdd BLAST36
Domaini484 – 519EGF-like 8PROSITE-ProRule annotationAdd BLAST36
Domaini572 – 607EGF-like 9PROSITE-ProRule annotationAdd BLAST36
Domaini660 – 695EGF-like 10PROSITE-ProRule annotationAdd BLAST36

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MEGF family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0200 Eukaryota
KOG1218 Eukaryota
ENOG410XQWV LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000167451

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9W0A0

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9W0A0

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR011489 EMI_domain
IPR002049 Laminin_EGF

Pfam protein domain database

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Pfami
View protein in Pfam
PF12661 hEGF, 3 hits
PF00053 Laminin_EGF, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00181 EGF, 14 hits
SM00180 EGF_Lam, 12 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00022 EGF_1, 13 hits
PS01186 EGF_2, 14 hits
PS50026 EGF_3, 10 hits
PS51041 EMI, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform BImported (identifier: Q9W0A0-1) [UniParc]FASTAAdd to basket
Also known as: Draper-I1 Publication

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLPVILIACL AQLVLAQADL KDLDGPNICK RRELYNVDVV YTELQSFQER
60 70 80 90 100
GSTWCVTFPP RCSTYRIKHR VVNKTKTIAK NRIVRDCCDG YIASAGECVP
110 120 130 140 150
HCSEPCQHGR CISPEKCKCD HGYGGPACDI NCPPGWYGRN CSMQCDCLNN
160 170 180 190 200
AVCEPFSGDC ECAKGYTGAR CADICPEGFF GANCSEKCRC ENGGKCHHVS
210 220 230 240 250
GECQCAPGFT GPLCDMRCPD GKHGAQCQQD CPCQNDGKCQ PETGACMCNP
260 270 280 290 300
GWTGDVCANK CPVGSYGPGC QESCECYKGA PCHHITGQCE CPPGYRGERC
310 320 330 340 350
FDECQLNTYG FNCSMTCDCA NDAMCDRANG TCICNPGWTG AKCAERICEA
360 370 380 390 400
NKYGLDCNRT CECDMEHTDL CHPETGNCQC SIGWSSAQCT RPCTFLRYGP
410 420 430 440 450
NCELTCNCKN GAKCSPVNGT CLCAPGWRGP TCEESCEPGT FGQDCALRCD
460 470 480 490 500
CQNGAKCEPE TGQCLCTAGW KNIKCDRPCD LNHFGQDCAK VCDCHNNAAC
510 520 530 540 550
NPQNGSCTCA AGWTGERCER KCDTGKFGHD CAQKCQCDFN NSLACDATNG
560 570 580 590 600
RCVCKQDWGG VHCETNCRSG YYGENCDKVC RCLNNSSCDP DSGNCICSAG
610 620 630 640 650
WTGADCAEPC PPGFYGMECK ERCPEILHGN KSCDHITGEI LCRTGYIGLT
660 670 680 690 700
CEHPCPAGLY GPGCKLKCNC EHGGECNHVT GQCQCLPGWT GSNCNESCPT
710 720 730 740 750
DTYGQGCAQR CRCVHHKVCR KADGMCICET GWSGTRCDEV CPEGFYGEHC
760 770 780 790 800
MNTCACPSAN FQCHAAHGCV CRSGYTGDNC DELIASQRIA DQSENSSRAS
810 820 830 840 850
VALTLVLMTL FACIIFAVFI YYRRRVSNLK TEIAHVHYTH DTNPPSWPPN
860 870 880 890 900
HNFDNPVYGM QAETRLLPNN MRSKMNNFDQ RSTMSTDYGD DCNASGRVGS
910 920 930 940 950
YSINYNHDLL TKNLNADRTN PIVYNESLKE EHVYDEIKHK EGYKDPDEYD
960 970 980 990 1000
HLDYSRPSTS QKPHYHRMND AMLNINQDEE KPSNVKNMTV LLNKPLPPTE
1010 1020 1030
PEPQHECFDN TNTNLDNVST ASPSSSPKFL K
Length:1,031
Mass (Da):113,015
Last modified:December 4, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA6A0104917D060A9
GO
Isoform AImported (identifier: Q9W0A0-2) [UniParc]FASTAAdd to basket
Also known as: Draper-II1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     131-579: NCPPGWYGRN...GYYGENCDKV → I
     946-946: P → PVKIYSKILFPE

Show »
Length:594
Mass (Da):66,213
Checksum:i8E1B5963F654579A
GO
Isoform CImported (identifier: Q9W0A0-3) [UniParc]FASTAAdd to basket
Also known as: Draper-III1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     131-579: NCPPGWYGRN...GYYGENCDKV → I
     947-976: DEYDHLDYSRPSTSQKPHYHRMNDAMLNIN → GMSLDFYTGRLSNFTINYVLYICTHYGMNQ
     977-1031: Missing.

Show »
Length:528
Mass (Da):58,676
Checksum:i3282B9AF939D5232
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M9PGU6M9PGU6_DROME
Draper, isoform E
drpr BcDNA:GH03529, CG18172, CT41022, CT6730, Dmel\CG2086
1,042Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M9PDW5M9PDW5_DROME
Draper, isoform D
drpr BcDNA:GH03529, CG18172, CT41022, CT6730, Dmel\CG2086
613Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M9PBI3M9PBI3_DROME
Draper, isoform F
drpr BcDNA:GH03529, CG18172, CT41022, CT6730, Dmel\CG2086
976Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti577D → Y in ABF85754 (Ref. 3) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058652131 – 579NCPPG…NCDKV → I in isoform A and isoform C. Add BLAST449
Alternative sequenceiVSP_058653946P → PVKIYSKILFPE in isoform A. 1
Alternative sequenceiVSP_060222947 – 976DEYDH…MLNIN → GMSLDFYTGRLSNFTINYVL YICTHYGMNQ in isoform C. Add BLAST30
Alternative sequenceiVSP_060223977 – 1031Missing in isoform C. Add BLAST55

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AE014296 Genomic DNA Translation: AAF47552.1
AE014296 Genomic DNA Translation: AAF47553.3
AE014296 Genomic DNA Translation: AFH04220.1
BT025854 mRNA Translation: ABF85754.1
BT044170 mRNA Translation: ACH92235.1

NCBI Reference Sequences

More...
RefSeqi
NP_001246549.1, NM_001259620.2 [Q9W0A0-3]
NP_477450.1, NM_058102.3 [Q9W0A0-2]
NP_728660.2, NM_167911.3 [Q9W0A0-1]

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0072798; FBpp0072680; FBgn0027594 [Q9W0A0-2]
FBtr0072799; FBpp0072681; FBgn0027594 [Q9W0A0-1]
FBtr0309845; FBpp0301579; FBgn0027594 [Q9W0A0-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
38218

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG2086

UCSC genome browser

More...
UCSCi
CG2086-RA d. melanogaster
CG2086-RB d. melanogaster [Q9W0A0-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA Translation: AAF47552.1
AE014296 Genomic DNA Translation: AAF47553.3
AE014296 Genomic DNA Translation: AFH04220.1
BT025854 mRNA Translation: ABF85754.1
BT044170 mRNA Translation: ACH92235.1
RefSeqiNP_001246549.1, NM_001259620.2 [Q9W0A0-3]
NP_477450.1, NM_058102.3 [Q9W0A0-2]
NP_728660.2, NM_167911.3 [Q9W0A0-1]

3D structure databases

SMRiQ9W0A0
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-19640N
IntActiQ9W0A0, 3 interactors
MINTiQ9W0A0
STRINGi7227.FBpp0306204

Proteomic databases

PRIDEiQ9W0A0

Genome annotation databases

EnsemblMetazoaiFBtr0072798; FBpp0072680; FBgn0027594 [Q9W0A0-2]
FBtr0072799; FBpp0072681; FBgn0027594 [Q9W0A0-1]
FBtr0309845; FBpp0301579; FBgn0027594 [Q9W0A0-3]
GeneIDi38218
KEGGidme:Dmel_CG2086
UCSCiCG2086-RA d. melanogaster
CG2086-RB d. melanogaster [Q9W0A0-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
38218
FlyBaseiFBgn0027594 drpr

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
KOG1218 Eukaryota
ENOG410XQWV LUCA
GeneTreeiENSGT00940000167451
InParanoidiQ9W0A0
PhylomeDBiQ9W0A0

Enzyme and pathway databases

ReactomeiR-DME-114608 Platelet degranulation
R-DME-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-DME-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-DME-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-DME-8957275 Post-translational protein phosphorylation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
drpr fly

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
38218

Protein Ontology

More...
PROi
PR:Q9W0A0

Gene expression databases

BgeeiFBgn0027594 Expressed in 34 organ(s), highest expression level in embryo
ExpressionAtlasiQ9W0A0 baseline and differential
GenevisibleiQ9W0A0 DM

Family and domain databases

InterProiView protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR011489 EMI_domain
IPR002049 Laminin_EGF
PfamiView protein in Pfam
PF12661 hEGF, 3 hits
PF00053 Laminin_EGF, 3 hits
SMARTiView protein in SMART
SM00181 EGF, 14 hits
SM00180 EGF_Lam, 12 hits
PROSITEiView protein in PROSITE
PS00022 EGF_1, 13 hits
PS01186 EGF_2, 14 hits
PS50026 EGF_3, 10 hits
PS51041 EMI, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDRPR_DROME
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9W0A0
Secondary accession number(s): M9NEX8, Q1EC80, Q9W0A1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 30, 2016
Last sequence update: December 4, 2007
Last modified: November 13, 2019
This is version 155 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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