Q61160 (FADD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein FADD

Alternative name(s):
FAS-associated death domain protein
FAS-associating death domain-containing protein
Mediator of receptor induced toxicity

Gene names

Name:	Fadd
Synonyms:	Mort1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis By similarity. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling By similarity.
Subunit structure	Interacts with CFLAR, PEA15 and MBD4. When phosphorylated, part of a complex containing HIPK3 and FAS. May interact with MAVS/IPS1. Interacts with LRDD By similarity. Interacts with FAS By similarity.
Domain	Contains a death domain involved in the binding of the corresponding domain within Fas receptor.
Post-translational modification	Phosphorylated.
Sequence similarities	Contains 1 death domain. Contains 1 DED (death effector) domain.

Ontologies

Keywords
Biological process	Apoptosis Immunity Innate immunity
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from direct assay. Source: MGI innate immune response Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

Protein FADD

PRO_0000191280

Regions

Domain

3 – 81

79

DED

Domain

97 – 181

85

Death

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Modified residue

41

1

Phosphoserine By similarity

Modified residue

191

1

Phosphoserine By similarity

Experimental info

Sequence conflict

168

1

C → F in AAA97876. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

205

Helix Strand Turn

Details...

Helix

94 – 118

25

Helix

123 – 132

10

Helix

137 – 152

16

Helix

153 – 156

4

Helix

158 – 168

11

Helix

171 – 181

11

Sequences

	Sequence		Length	Mass (Da)
	Q61160 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 4BC8D86B33A58783	FASTA	205	22,960
	10 20 30 40 50 60 MDPFLVLLHS LSGSLSGNDL MELKFLCRER VSKRKLERVQ SGLDLFTVLL EQNDLERGHT 70 80 90 100 110 120 GLLRELLASL RRHDLLQRLD DFEAGTATAA PPGEADLQVA FDIVCDNVGR DWKRLARELK 130 140 150 160 170 180 VSEAKMDGIE EKYPRSLSER VRESLKVWKN AEKKNASVAG LVKALRTCRL NLVADLVEEA 190 200 QESVSKSENM SPVLRDSTVS SSETP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis." Zhang J., Winoto A. Mol. Cell. Biol. 16:2756-2763(1996) [PubMed: 8649383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways." Hsu H., Shu H.-B., Pan M.G., Goeddel D.V. Cell 84:299-308(1996) [PubMed: 8565075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Heart and Thymus.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary gland and Salivary gland.
[5]	"The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD." Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S. J. Biol. Chem. 274:16337-16342(1999) [PubMed: 10347191] [Abstract] Cited for: STRUCTURE BY NMR OF 89-183.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U50406 mRNA. Translation: AAB07789.1.
U43184 mRNA. Translation: AAA97876.1.
AK084808 mRNA. Translation: BAC39283.1.
AK169798 mRNA. Translation: BAE41374.1.
AK170927 mRNA. Translation: BAE42120.1.
BC004584 mRNA. Translation: AAH04584.1.
BC021400 mRNA. Translation: AAH21400.1.

IPI

IPI00117888.

RefSeq

NP_034305.1. NM_010175.5.

UniGene

Mm.5126.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FAD	NMR	-	A	89-183	[»]

ProteinModelPortal

Q61160.

SMR

Q61160. Positions 1-183.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34771N.

IntAct

Q61160. 9 interactions.

MINT

MINT-1514991.

STRING

Q61160.

PTM databases

PhosphoSite

Q61160.

Proteomic databases

PRIDE

Q61160.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000033394; ENSMUSP00000033394; ENSMUSG00000031077.

GeneID

14082.

KEGG

mmu:14082.

UCSC

uc009kql.1. mouse.

Organism-specific databases

CTD

8772.

MGI

MGI:109324. Fadd.

Phylogenomic databases

eggNOG

roNOG16707.

HOGENOM

HBG446838.

HOVERGEN

HBG000853.

InParanoid

Q61160.

OMA

EQNDLEP.

OrthoDB

EOG4JHCH7.

PhylomeDB

Q61160.

Gene expression databases

ArrayExpress

Q61160.

Bgee

Q61160.

CleanEx

MM_FADD.

Genevestigator

Q61160.

GermOnline

ENSMUSG00000031077. Mus musculus.

Family and domain databases

InterPro

IPR000488. Death.
IPR011029. DEATH-like.
IPR001875. DED.
IPR016729. FADD.
[Graphical view]

Gene3D

G3DSA:1.10.533.10. DEATH_like. 2 hits.

KO

K02373.

Pfam

PF00531. Death. 1 hit.
PF01335. DED. 1 hit.
[Graphical view]

PIRSF

PIRSF018586. FADD. 1 hit.

SMART

SM00005. DEATH. 1 hit.
SM00031. DED. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50017. DEATH_DOMAIN. 1 hit.
PS50168. DED. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

285096.

SOURCE

Search...

Entry information

Entry name

FADD_MOUSE

Accession

Primary (citable) accession number: Q61160
Secondary accession number(s): Q3TC37, Q61082

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program