EIGER_DROME
ID EIGER_DROME Reviewed; 415 AA.
AC Q8MUJ1; Q8IGD3; Q8MRW2; Q8MY88;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein eiger {ECO:0000303|PubMed:12176339};
DE Contains:
DE RecName: Full=Protein eiger, membrane form {ECO:0000305};
DE Contains:
DE RecName: Full=Protein eiger, soluble form {ECO:0000303|PubMed:12894227};
GN Name=egr {ECO:0000312|FlyBase:FBgn0033483};
GN Synonyms=Darth {ECO:0000303|PubMed:12894227};
GN ORFNames=CG12919 {ECO:0000312|FlyBase:FBgn0033483};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAM76710.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=12176339; DOI=10.1016/s0960-9822(02)00954-5;
RA Moreno E., Yan M., Basler K.;
RT "Evolution of TNF signaling mechanisms: JNK-dependent apoptosis triggered
RT by Eiger, the Drosophila homolog of the TNF superfamily.";
RL Curr. Biol. 12:1263-1268(2002).
RN [2] {ECO:0000312|EMBL:BAC00950.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12065414; DOI=10.1093/emboj/cdf306;
RA Igaki T., Kanda H., Yamamoto-Goto Y., Kanuka H., Kuranaga E., Aigaki T.,
RA Miura M.;
RT "Eiger, a TNF superfamily ligand that triggers the Drosophila JNK
RT pathway.";
RL EMBO J. 21:3009-3018(2002).
RN [3] {ECO:0000312|EMBL:AAM66763.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 146-150,
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, GLYCOSYLATION, CLEAVAGE, AND INDUCTION.
RX PubMed=12894227; DOI=10.1038/sj.onc.1206715;
RA Kauppila S., Maaty W.S., Chen P., Tomar R.S., Eby M.T., Chapo J., Chew S.,
RA Rathore N., Zachariah S., Sinha S.K., Abrams J.M., Chaudhary P.M.;
RT "Eiger and its receptor, Wengen, comprise a TNF-like system in
RT Drosophila.";
RL Oncogene 22:4860-4867(2003).
RN [4] {ECO:0000312|EMBL:AAO15310.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Inohara N., Nunez G.;
RT "DT1, a Drosophila tumor necrosis factor family member.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5] {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 [6] {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 [7] {ECO:0000312|EMBL:AAM51093.1, ECO:0000312|EMBL:AAN71595.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 99-415 (ISOFORM 1).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM51093.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM51093.1}, and
RC Head {ECO:0000312|EMBL:AAN71595.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8] {ECO:0000312|EMBL:AAX33519.1, ECO:0000312|EMBL:ACO06073.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAN71595.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=17356067; DOI=10.1242/jcs.03420;
RA Bidla G., Dushay M.S., Theopold U.;
RT "Crystal cell rupture after injury in Drosophila requires the JNK pathway,
RT small GTPases and the TNF homolog Eiger.";
RL J. Cell Sci. 120:1209-1215(2007).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17381241; DOI=10.1371/journal.ppat.0030041;
RA Schneider D.S., Ayres J.S., Brandt S.M., Costa A., Dionne M.S.,
RA Gordon M.D., Mabery E.M., Moule M.G., Pham L.N., Shirasu-Hiza M.M.;
RT "Drosophila eiger mutants are sensitive to extracellular pathogens.";
RL PLoS Pathog. 3:E41-E41(2007).
RN [11] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19375319; DOI=10.1016/j.cub.2009.03.062;
RA Babcock D.T., Landry C., Galko M.J.;
RT "Cytokine signaling mediates UV-induced nociceptive sensitization in
RT Drosophila larvae.";
RL Curr. Biol. 19:799-806(2009).
RN [12] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19289090; DOI=10.1016/j.devcel.2009.01.002;
RA Igaki T., Pastor-Pareja J.C., Aonuma H., Miura M., Xu T.;
RT "Intrinsic tumor suppression and epithelial maintenance by endocytic
RT activation of Eiger/TNF signaling in Drosophila.";
RL Dev. Cell 16:458-465(2009).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=19019992; DOI=10.1242/dev.023366;
RA Kato K., Awasaki T., Ito K.;
RT "Neuronal programmed cell death induces glial cell division in the adult
RT Drosophila brain.";
RL Development 136:51-59(2009).
RN [14] {ECO:0000305}
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20505310; DOI=10.1159/000315050;
RA Mabery E.M., Schneider D.S.;
RT "The Drosophila TNF ortholog eiger is required in the fat body for a robust
RT immune response.";
RL J. Innate Immun. 2:371-378(2010).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=24066226; DOI=10.7554/elife.01004;
RA Perez-Garijo A., Fuchs Y., Steller H.;
RT "Apoptotic cells can induce non-autonomous apoptosis through the TNF
RT pathway.";
RL Elife 2:E01004-E01004(2013).
RN [16] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25754009; DOI=10.1016/j.febslet.2015.02.032;
RA Shklover J., Levy-Adam F., Kurant E.;
RT "The role of Drosophila TNF Eiger in developmental and damage-induced
RT neuronal apoptosis.";
RL FEBS Lett. 589:871-879(2015).
RN [17] {ECO:0000305}
RP FUNCTION.
RX PubMed=25874673; DOI=10.1038/nature14298;
RA Andersen D.S., Colombani J., Palmerini V., Chakrabandhu K., Boone E.,
RA Roethlisberger M., Toggweiler J., Basler K., Mapelli M., Hueber A.O.,
RA Leopold P.;
RT "The Drosophila TNF receptor Grindelwald couples loss of cell polarity and
RT neoplastic growth.";
RL Nature 522:482-486(2015).
CC -!- FUNCTION: Cytokine which acts as a ligand for wgn (PubMed:12894227).
CC Also acts as a ligand for grnd (PubMed:25874673). Induces apoptosis by
CC triggering JNK signaling (PubMed:12176339, PubMed:12065414,
CC PubMed:12894227). Required for JNK-dependent non-autonomous apoptosis
CC through release from apoptotic cells and activation of apoptosis in
CC neighboring cells (PubMed:24066226). Required for JNK-independent
CC damage-induced apoptosis in the embryonic central nervous system
CC through regulation of the pro-apoptotic gene hid (PubMed:25754009).
CC Involved in the innate immune response to extracellular pathogens
CC (PubMed:17381241). Plays a role in the melanization immune response
CC through its involvement in the rupture of crystal cells and subsequent
CC release of prophenoloxidase (PubMed:17356067). Following UV-induced
CC epidermal damage, released from apoptotic epidermal cells, binds to the
CC wgn receptor on nociceptive sensory neurons and plays a role in
CC development of thermal allodynia, a responsiveness to subthreshold
CC thermal stimuli which are not normally perceived as noxious
CC (PubMed:19375319). Involved in glial cell division induced by neuronal
CC programmed cell death and injury (PubMed:19019992). Has tumor
CC suppressor activity and eliminates oncogenic cells from epithelia,
CC thereby maintaining epithelial integrity (PubMed:19289090).
CC {ECO:0000269|PubMed:12065414, ECO:0000269|PubMed:12176339,
CC ECO:0000269|PubMed:12894227, ECO:0000269|PubMed:17356067,
CC ECO:0000269|PubMed:17381241, ECO:0000269|PubMed:19019992,
CC ECO:0000269|PubMed:19289090, ECO:0000269|PubMed:19375319,
CC ECO:0000269|PubMed:24066226, ECO:0000269|PubMed:25754009,
CC ECO:0000269|PubMed:25874673}.
CC -!- INTERACTION:
CC Q8MUJ1; Q9VJ83: grnd; NbExp=4; IntAct=EBI-108054, EBI-164007;
CC Q8MUJ1; Q9VWS4: wgn; NbExp=3; IntAct=EBI-108054, EBI-161953;
CC -!- SUBCELLULAR LOCATION: [Protein eiger, membrane form]: Cell membrane
CC {ECO:0000269|PubMed:12065414, ECO:0000269|PubMed:19289090,
CC ECO:0000269|PubMed:25754009}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Protein eiger, soluble form]: Secreted
CC {ECO:0000269|PubMed:12894227}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Eiger-L {ECO:0000303|PubMed:12894227};
CC IsoId=Q8MUJ1-1; Sequence=Displayed;
CC Name=2; Synonyms=Eiger-S {ECO:0000303|PubMed:12894227};
CC IsoId=Q8MUJ1-2; Sequence=VSP_058011;
CC -!- TISSUE SPECIFICITY: During embryogenesis, highly expressed in glial
CC cells and neurons (at protein level) (PubMed:25754009). Highly
CC localized to the dorsal surface of pregastrulating embryos
CC (PubMed:12894227). During gastrulation, expression occurs in the
CC epidermal layer of the embryo and is most prominent at the surface of
CC dorsal folds that will later form the amnioserosa (PubMed:12894227). At
CC germ band extended stages, prominent in the neurogenic region adjacent
CC to the mesodermal segments of the embryo (PubMed:12894227). In later-
CC staged embryos at stages 15/16, detected in subsets of cells within the
CC condensing nerve cord (PubMed:12894227). After embryonic stage 10,
CC predominantly detected in the nervous system (PubMed:12065414). In the
CC third instar larva, strongly expressed in the brain hemispheres and at
CC the morphogenetic furrow in the eye disk (PubMed:12065414). Also
CC expressed at significant levels in many cells posterior to the furrow
CC and in the proliferating cells at the furrow (PubMed:12065414). In the
CC adult, expressed in the fat body (PubMed:20505310).
CC {ECO:0000269|PubMed:12065414, ECO:0000269|PubMed:12894227,
CC ECO:0000269|PubMed:20505310, ECO:0000269|PubMed:25754009}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 and isoform 2 are expressed throughout
CC development and in the adult. Isoform 1 predominates at each stage by
CC about 5 to 10-fold. {ECO:0000269|PubMed:12894227}.
CC -!- INDUCTION: By gamma-radiation (PubMed:12894227). By bacterial infection
CC (PubMed:20505310). {ECO:0000269|PubMed:12894227,
CC ECO:0000269|PubMed:20505310}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12894227}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000269|PubMed:12894227}.
CC -!- DISRUPTION PHENOTYPE: Reduced resistance to extracellular pathogens
CC (PubMed:17381241). Complete absence of thermal allodynia in mutant
CC larvae exposed to UV radiation (PubMed:19375319). RNAi-mediated
CC knockdown in the adult fat body results in increased survival following
CC S.typhimurium infection, increased levels of diptericin and reduced
CC feeding rate (PubMed:20505310). {ECO:0000269|PubMed:17381241,
CC ECO:0000269|PubMed:19375319, ECO:0000269|PubMed:20505310}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM51093.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF521176; AAM76710.1; -; mRNA.
DR EMBL; AB073865; BAC00950.1; -; mRNA.
DR EMBL; AY115551; AAM66763.1; -; mRNA.
DR EMBL; AF149799; AAO15310.1; -; mRNA.
DR EMBL; AE013599; AAF58848.2; -; Genomic_DNA.
DR EMBL; AE013599; AAS64883.1; -; Genomic_DNA.
DR EMBL; AY119233; AAM51093.1; ALT_FRAME; mRNA.
DR EMBL; BT001838; AAN71595.1; -; mRNA.
DR EMBL; BT021371; AAX33519.1; -; mRNA.
DR EMBL; BT072996; ACO06073.1; -; mRNA.
DR RefSeq; NP_724878.2; NM_165735.4. [Q8MUJ1-1]
DR RefSeq; NP_995791.1; NM_206069.3. [Q8MUJ1-2]
DR PDB; 6ZT0; X-ray; 2.02 A; A=273-415.
DR PDBsum; 6ZT0; -.
DR AlphaFoldDB; Q8MUJ1; -.
DR SMR; Q8MUJ1; -.
DR IntAct; Q8MUJ1; 5.
DR STRING; 7227.FBpp0087493; -.
DR GlyGen; Q8MUJ1; 3 sites.
DR PaxDb; Q8MUJ1; -.
DR DNASU; 36054; -.
DR EnsemblMetazoa; FBtr0088405; FBpp0087493; FBgn0033483. [Q8MUJ1-1]
DR EnsemblMetazoa; FBtr0088406; FBpp0087494; FBgn0033483. [Q8MUJ1-2]
DR GeneID; 36054; -.
DR KEGG; dme:Dmel_CG12919; -.
DR UCSC; CG12919-RA; d. melanogaster. [Q8MUJ1-1]
DR UCSC; CG12919-RB; d. melanogaster.
DR CTD; 36054; -.
DR FlyBase; FBgn0033483; egr.
DR VEuPathDB; VectorBase:FBgn0033483; -.
DR eggNOG; ENOG502QUAV; Eukaryota.
DR HOGENOM; CLU_662723_0_0_1; -.
DR InParanoid; Q8MUJ1; -.
DR OMA; LVYAQIH; -.
DR PhylomeDB; Q8MUJ1; -.
DR Reactome; R-DME-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR BioGRID-ORCS; 36054; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36054; -.
DR PRO; PR:Q8MUJ1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033483; Expressed in adult Malpighian tubule (Drosophila) and 43 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IDA:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:FlyBase.
DR GO; GO:0014009; P:glial cell proliferation; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:1900074; P:negative regulation of neuromuscular synaptic transmission; IGI:FlyBase.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:FlyBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:FlyBase.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:FlyBase.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0002347; P:response to tumor cell; IMP:FlyBase.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:FlyBase.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS00251; TNF_1; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane; Coiled coil;
KW Cytokine; Direct protein sequencing; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Protein eiger, membrane form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435108"
FT CHAIN 146..415
FT /note="Protein eiger, soluble form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000435109"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 111..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..233
FT /evidence="ECO:0000255"
FT COMPBIAS 115..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 145..146
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:12894227"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 265..270
FT /note="Missing (in isoform 2)"
FT /id="VSP_058011"
FT CONFLICT 101
FT /note="E -> A (in Ref. 7; AAM51093)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="S -> R (in Ref. 7; AAN71595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 46918 MW; E087A26DE222D2BF CRC64;
MTAETLKPFI TPTSANDDGF PAKATSTATA QRRTRQLIPL VLGFIGLGLV VAILALTIWQ
TTRVSHLDKE LKSLKRVVDN LQQRLGINYL DEFDEFQKEY ENALIDYPKK VDGLTDEEDD
DDGDGLDSIA DDEDDDVSYS SVDDVGADYE DYTDMLNKLN NAHTGTTPTS ETTAEGEGET
DSASSASNDD NVFDDFTSYN AHKKKQERKS RSIADVRNEE QNIQGNHTEL QEKSSNEATS
KESPAPLHHR RRMHSRHRHL LVRKGESLLS ARSEDSRPAA HFHLSSRRRH QGSMGYHGDM
YIGNDNERNS YQGHFQTRDG VLTVTNTGLY YVYAQICYNN SHDQNGFIVF QGDTPFLQCL
NTVPTNMPHK VHTCHTSGLI HLERNERIHL KDIHNDRNAV LREGNNRSYF GIFKV
