ID   FADD_MOUSE              Reviewed;         205 AA.
AC   Q61160; Q3TC37; Q61082;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   19-JAN-2010, entry version 89.
DE   RecName: Full=Protein FADD;
DE   AltName: Full=FAS-associated death domain protein;
DE   AltName: Full=FAS-associating death domain-containing protein;
DE   AltName: Full=Mediator of receptor induced toxicity;
GN   Name=Fadd; Synonyms=Mort1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96220459; PubMed=8649383;
RA   Zhang J., Winoto A.;
RT   "A mouse Fas-associated protein with homology to the human Mort1/FADD
RT   protein is essential for Fas-induced apoptosis.";
RL   Mol. Cell. Biol. 16:2756-2763(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96152659; PubMed=8565075; DOI=10.1016/S0092-8674(00)80984-8;
RA   Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.;
RT   "TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF
RT   receptor 1 signal transduction pathways.";
RL   Cell 84:299-308(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   STRUCTURE BY NMR OF 89-183.
RX   PubMed=10347191; DOI=10.1074/jbc.274.23.16337;
RA   Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S.;
RT   "The solution structure of FADD death domain. Structural basis of
RT   death domain interactions of Fas and FADD.";
RL   J. Biol. Chem. 274:16337-16342(1999).
CC   -!- FUNCTION: Apoptotic adaptor molecule that recruits caspase-8 or
CC       caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The
CC       resulting aggregate called the death-inducing signaling complex
CC       (DISC) performs caspase-8 proteolytic activation. Active caspase-8
CC       initiates the subsequent cascade of caspases mediating apoptosis
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with CFLAR, PEA15 and MBD4. When
CC       phosphorylated, part of a complex containing HIPK3 and FAS. May
CC       interact with MAVS/IPS1. Interacts with LRDD (By similarity).
CC   -!- INTERACTION:
CC       O89110:Casp8; NbExp=1; IntAct=EBI-524415, EBI-851690;
CC       O35732-1:Cflar; NbExp=1; IntAct=EBI-524415, EBI-851729;
CC       Q9ERH7:Hipk3; NbExp=1; IntAct=EBI-524415, EBI-524356;
CC   -!- DOMAIN: Contains a death domain involved in the binding of the
CC       corresponding domain within Fas receptor.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 DED (death effector) domain.
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DR   EMBL; U50406; AAB07789.1; -; mRNA.
DR   EMBL; U43184; AAA97876.1; -; mRNA.
DR   EMBL; AK084808; BAC39283.1; -; mRNA.
DR   EMBL; AK169798; BAE41374.1; -; mRNA.
DR   EMBL; AK170927; BAE42120.1; -; mRNA.
DR   EMBL; BC004584; AAH04584.1; -; mRNA.
DR   EMBL; BC021400; AAH21400.1; -; mRNA.
DR   IPI; IPI00117888; -.
DR   RefSeq; NP_034305.1; -.
DR   UniGene; Mm.5126; -.
DR   PDB; 1FAD; NMR; -; A=89-183.
DR   PDBsum; 1FAD; -.
DR   SMR; Q61160; 2-183.
DR   DIP; DIP-34771N; -.
DR   IntAct; Q61160; 7.
DR   STRING; Q61160; -.
DR   PhosphoSite; Q61160; -.
DR   PRIDE; Q61160; -.
DR   Ensembl; ENSMUST00000033394; ENSMUSP00000033394; ENSMUSG00000031077; Mus musculus.
DR   GeneID; 14082; -.
DR   KEGG; mmu:14082; -.
DR   UCSC; uc009kql.1; mouse.
DR   CTD; 14082; -.
DR   MGI; MGI:109324; Fadd.
DR   eggNOG; roNOG16707; -.
DR   HOGENOM; HBG446838; -.
DR   HOVERGEN; Q61160; -.
DR   InParanoid; Q61160; -.
DR   OMA; LEQNDLE; -.
DR   OrthoDB; EOG9QRKP8; -.
DR   PhylomeDB; Q61160; -.
DR   NextBio; 285096; -.
DR   ArrayExpress; Q61160; -.
DR   Bgee; Q61160; -.
DR   CleanEx; MM_FADD; -.
DR   Genevestigator; Q61160; -.
DR   GermOnline; ENSMUSG00000031077; Mus musculus.
DR   GO; GO:0006915; P:apoptosis; IDA:MGI.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR001875; DED.
DR   InterPro; IPR016729; FADD.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF01335; DED; 1.
DR   PIRSF; PIRSF018586; FADD; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00031; DED; 1.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS50168; DED; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Phosphoprotein.
FT   CHAIN         1    205       Protein FADD.
FT                                /FTId=PRO_0000191280.
FT   DOMAIN        3     81       DED.
FT   DOMAIN       97    181       Death.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   CONFLICT    168    168       C -> F (in Ref. 2; AAA97876).
FT   HELIX        94    118
FT   HELIX       123    132
FT   HELIX       137    152
FT   HELIX       153    156
FT   HELIX       158    168
FT   HELIX       171    181
SQ   SEQUENCE   205 AA;  22960 MW;  4BC8D86B33A58783 CRC64;
     MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL EQNDLERGHT
     GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA FDIVCDNVGR DWKRLARELK
     VSEAKMDGIE EKYPRSLSER VRESLKVWKN AEKKNASVAG LVKALRTCRL NLVADLVEEA
     QESVSKSENM SPVLRDSTVS SSETP
//