FADD_DROME
ID FADD_DROME Reviewed; 239 AA.
AC Q9V3B4; A4V9R5; A4V9R6; A4V9R7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Fas-associated death domain protein;
DE AltName: Full=Death domain-containing adapter protein BG4;
DE AltName: Full=FAS-associating death domain-containing protein;
DE Short=dFADD;
GN Name=Fadd; Synonyms=BG4; ORFNames=CG12297;
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG22535.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DREDD, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10934188; DOI=10.1074/jbc.c000341200;
RA Hu S., Yang X.;
RT "dFADD, a novel death domain-containing adapter protein for the Drosophila
RT caspase DREDD.";
RL J. Biol. Chem. 275:30761-30764(2000).
RN [2] {ECO:0000312|EMBL:AAF44325.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou L., Steller H.;
RT "BG4_a potential Drosophila homologue of FAS-associating death-domain
RT containing protein (FADD).";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAF55950.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF55950.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-201, AND VARIANTS MET-71; PRO-87;
RP PRO-135; THR-143 AND GLN-149.
RC STRAIN=G02, G125, G130, and G140;
RX PubMed=17465907; DOI=10.1111/j.1420-9101.2007.01305.x;
RA Jiggins F.M., Kim K.W.;
RT "A screen for immunity genes evolving under positive selection in
RT Drosophila.";
RL J. Evol. Biol. 20:965-970(2007).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH IMD.
RX PubMed=12433364; DOI=10.1016/s1074-7613(02)00454-5;
RA Naitza S., Rosse C., Kappler C., Georgel P., Belvin M., Gubb D.,
RA Camonis J., Hoffmann J.A., Reichhart J.-M.;
RT "The Drosophila immune defense against Gram-negative infection requires the
RT death protein dFADD.";
RL Immunity 17:575-581(2002).
RN [7]
RP INTERACTION WITH DREDD.
RX PubMed=22549468; DOI=10.1038/emboj.2012.121;
RA Meinander A., Runchel C., Tenev T., Chen L., Kim C.H., Ribeiro P.S.,
RA Broemer M., Leulier F., Zvelebil M., Silverman N., Meier P.;
RT "Ubiquitylation of the initiator caspase DREDD is required for innate
RT immune signalling.";
RL EMBO J. 31:2770-2783(2012).
CC -!- FUNCTION: Component of the IMD signaling pathway and is required for
CC the host defense against Gram-negative bacteria. Interacts with Dredd,
CC promotes cleavage of Dredd and is necessary and sufficient for
CC enhancing Dredd-induced apoptosis. {ECO:0000269|PubMed:10934188,
CC ECO:0000269|PubMed:12433364}.
CC -!- SUBUNIT: Interacts (via N-terminus) with Dredd; likely to bind Dredd
CC simultaneously with Diap2 to form a trimeric complex (PubMed:10934188,
CC PubMed:22549468). Interacts with imd (PubMed:12433364).
CC {ECO:0000269|PubMed:10934188, ECO:0000269|PubMed:12433364,
CC ECO:0000269|PubMed:22549468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10934188}.
CC -!- DEVELOPMENTAL STAGE: Expressed between 3-12 hours of embryonic
CC development. {ECO:0000269|PubMed:10934188}.
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DR EMBL; AF295103; AAG22535.1; -; mRNA.
DR EMBL; AF222005; AAF44325.1; -; mRNA.
DR EMBL; AE014297; AAF55950.1; -; Genomic_DNA.
DR EMBL; AM412815; CAL85438.1; -; Genomic_DNA.
DR EMBL; AM412816; CAL85439.1; -; Genomic_DNA.
DR EMBL; AM412817; CAL85440.1; -; Genomic_DNA.
DR EMBL; AM412818; CAL85441.1; -; Genomic_DNA.
DR RefSeq; NP_651006.1; NM_142749.3.
DR AlphaFoldDB; Q9V3B4; -.
DR BioGRID; 67555; 103.
DR DIP; DIP-18912N; -.
DR IntAct; Q9V3B4; 6.
DR MINT; Q9V3B4; -.
DR STRING; 7227.FBpp0083574; -.
DR PaxDb; Q9V3B4; -.
DR DNASU; 42594; -.
DR EnsemblMetazoa; FBtr0084176; FBpp0083574; FBgn0038928.
DR GeneID; 42594; -.
DR KEGG; dme:Dmel_CG12297; -.
DR UCSC; CG12297-RA; d. melanogaster.
DR CTD; 8772; -.
DR FlyBase; FBgn0038928; Fadd.
DR VEuPathDB; VectorBase:FBgn0038928; -.
DR eggNOG; ENOG502SE91; Eukaryota.
DR HOGENOM; CLU_093594_0_0_1; -.
DR InParanoid; Q9V3B4; -.
DR OMA; LIEEDDC; -.
DR OrthoDB; 1619689at2759; -.
DR PhylomeDB; Q9V3B4; -.
DR Reactome; R-DME-214397; Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
DR SignaLink; Q9V3B4; -.
DR BioGRID-ORCS; 42594; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42594; -.
DR PRO; PR:Q9V3B4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038928; Expressed in cleaving embryo and 27 other tissues.
DR ExpressionAtlas; Q9V3B4; baseline and differential.
DR Genevisible; Q9V3B4; DM.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0050700; F:CARD domain binding; IPI:FlyBase.
DR GO; GO:0089720; F:caspase binding; IBA:GO_Central.
DR GO; GO:0005123; F:death receptor binding; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IMP:FlyBase.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; TAS:FlyBase.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR Pfam; PF00531; Death; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Reference proteome.
FT CHAIN 1..239
FT /note="Fas-associated death domain protein"
FT /id="PRO_0000271422"
FT DOMAIN 151..237
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..105
FT /note="Death-inducing"
FT VARIANT 71
FT /note="I -> M (in strain: G130 and G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 87
FT /note="K -> P (in strain: G125, G130 and G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 135
FT /note="T -> P (in strain: G02, G125, G130 and G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 143
FT /note="P -> T (in strain: G02, G130 and G140)"
FT /evidence="ECO:0000269|PubMed:17465907"
FT VARIANT 149
FT /note="H -> Q (in strain: G125)"
FT /evidence="ECO:0000269|PubMed:17465907"
SQ SEQUENCE 239 AA; 27421 MW; F43CFAA546C3FCD9 CRC64;
MTAGRHWSYD SLKQIAIDGC TENVEQLKLI FVEEIGSRRR SDCIRTIEDL IDCLERADEL
SEYNVEPLRR ISGNMPQLIE ALSAYTKPEN ILGHPVNLYQ ELRLAEELRQ QLRIAPASQN
AQPSVSELAA AVPPTAIQNY ATPAAFTDHK RTMVFKKISE ELGRYWRRLG RSAGIGEGQM
DTIEERYPHD LKSQILRLLQ LIEEDDCHDP KHFLLRLCRA LGDCGRNDLR KRVEQIMSH
