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Fas-associated death domain protein (Death domain-containing adapter protein BG4) (FAS-associating death domain-containing protein) (dFADD)

 FADD_DROME              Reviewed;         239 AA.
Q9V3B4; A4V9R5; A4V9R6; A4V9R7;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 122.
RecName: Full=Fas-associated death domain protein;
AltName: Full=Death domain-containing adapter protein BG4;
AltName: Full=FAS-associating death domain-containing protein;
Short=dFADD;
Name=Fadd; Synonyms=BG4; ORFNames=CG12297;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG22535.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DREDD,
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=10934188; DOI=10.1074/jbc.C000341200;
Hu S., Yang X.;
"dFADD, a novel death domain-containing adapter protein for the
Drosophila caspase DREDD.";
J. Biol. Chem. 275:30761-30764(2000).
[2] {ECO:0000312|EMBL:AAF44325.1}
NUCLEOTIDE SEQUENCE [MRNA].
Zhou L., Steller H.;
"BG4_a potential Drosophila homologue of FAS-associating death-domain
containing protein (FADD).";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000312|EMBL:AAF55950.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000305, ECO:0000312|EMBL:AAF55950.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-201, AND VARIANTS MET-71;
PRO-87; PRO-135; THR-143 AND GLN-149.
STRAIN=G02, G125, G130, and G140;
PubMed=17465907; DOI=10.1111/j.1420-9101.2007.01305.x;
Jiggins F.M., Kim K.W.;
"A screen for immunity genes evolving under positive selection in
Drosophila.";
J. Evol. Biol. 20:965-970(2007).
[6] {ECO:0000305}
FUNCTION, AND INTERACTION WITH IMD.
PubMed=12433364; DOI=10.1016/S1074-7613(02)00454-5;
Naitza S., Rosse C., Kappler C., Georgel P., Belvin M., Gubb D.,
Camonis J., Hoffmann J.A., Reichhart J.-M.;
"The Drosophila immune defense against Gram-negative infection
requires the death protein dFADD.";
Immunity 17:575-581(2002).
[7]
INTERACTION WITH DREDD.
PubMed=22549468; DOI=10.1038/emboj.2012.121;
Meinander A., Runchel C., Tenev T., Chen L., Kim C.H., Ribeiro P.S.,
Broemer M., Leulier F., Zvelebil M., Silverman N., Meier P.;
"Ubiquitylation of the initiator caspase DREDD is required for innate
immune signalling.";
EMBO J. 31:2770-2783(2012).
-!- FUNCTION: Component of the IMD signaling pathway and is required
for the host defense against Gram-negative bacteria. Interacts
with Dredd, promotes cleavage of Dredd and is necessary and
sufficient for enhancing Dredd-induced apoptosis.
{ECO:0000269|PubMed:10934188, ECO:0000269|PubMed:12433364}.
-!- SUBUNIT: Interacts (via N-terminus) with Dredd; likely to bind
Dredd simultaneously with Diap2 to form a trimeric complex
(PubMed:10934188, PubMed:22549468). Interacts with imd
(PubMed:12433364). {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:12433364, ECO:0000269|PubMed:22549468}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10934188}.
-!- DEVELOPMENTAL STAGE: Expressed between 3-12 hours of embryonic
development. {ECO:0000269|PubMed:10934188}.
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EMBL; AF295103; AAG22535.1; -; mRNA.
EMBL; AF222005; AAF44325.1; -; mRNA.
EMBL; AE014297; AAF55950.1; -; Genomic_DNA.
EMBL; AM412815; CAL85438.1; -; Genomic_DNA.
EMBL; AM412816; CAL85439.1; -; Genomic_DNA.
EMBL; AM412817; CAL85440.1; -; Genomic_DNA.
EMBL; AM412818; CAL85441.1; -; Genomic_DNA.
RefSeq; NP_651006.1; NM_142749.3.
UniGene; Dm.1273; -.
ProteinModelPortal; Q9V3B4; -.
BioGrid; 67555; 103.
DIP; DIP-18912N; -.
IntAct; Q9V3B4; 9.
MINT; Q9V3B4; -.
STRING; 7227.FBpp0083574; -.
PaxDb; Q9V3B4; -.
PRIDE; Q9V3B4; -.
EnsemblMetazoa; FBtr0084176; FBpp0083574; FBgn0038928.
GeneID; 42594; -.
KEGG; dme:Dmel_CG12297; -.
UCSC; CG12297-RA; d. melanogaster.
CTD; 8772; -.
FlyBase; FBgn0038928; Fadd.
eggNOG; ENOG410J662; Eukaryota.
eggNOG; ENOG410Y56G; LUCA.
InParanoid; Q9V3B4; -.
KO; K02373; -.
OMA; LIEEDDC; -.
OrthoDB; EOG091G0GZR; -.
PhylomeDB; Q9V3B4; -.
Reactome; R-DME-214397; Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
GenomeRNAi; 42594; -.
PRO; PR:Q9V3B4; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0038928; -.
ExpressionAtlas; Q9V3B4; baseline and differential.
Genevisible; Q9V3B4; DM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0050700; F:CARD domain binding; IPI:FlyBase.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0006955; P:immune response; IMP:FlyBase.
GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; TAS:FlyBase.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
Pfam; PF00531; Death; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Reference proteome.
CHAIN 1 239 Fas-associated death domain protein.
/FTId=PRO_0000271422.
DOMAIN 151 237 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 1 105 Death-inducing.
VARIANT 71 71 I -> M (in strain: G130 and G140).
{ECO:0000269|PubMed:17465907}.
VARIANT 87 87 K -> P (in strain: G125, G130 and G140).
{ECO:0000269|PubMed:17465907}.
VARIANT 135 135 T -> P (in strain: G02, G125, G130 and
G140). {ECO:0000269|PubMed:17465907}.
VARIANT 143 143 P -> T (in strain: G02, G130 and G140).
{ECO:0000269|PubMed:17465907}.
VARIANT 149 149 H -> Q (in strain: G125).
{ECO:0000269|PubMed:17465907}.
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


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