TNR6_MOUSE
ID TNR6_MOUSE Reviewed; 327 AA.
AC P25446; Q6GT31; Q9DCQ1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 6;
DE AltName: Full=Apo-1 antigen;
DE AltName: Full=Apoptosis-mediating surface antigen FAS;
DE AltName: Full=FASLG receptor;
DE AltName: CD_antigen=CD95;
DE Flags: Precursor;
GN Name=Fas; Synonyms=Apt1, Tnfrsf6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=1371136;
RA Watanabe-Fukunaga R., Brannan C.I., Itoh N., Yonehara S., Copeland N.G.,
RA Jenkins N.A., Nagata S.;
RT "The cDNA structure, expression, and chromosomal assignment of the mouse
RT Fas antigen.";
RL J. Immunol. 148:1274-1279(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Koczan D., Ibrahim S.M., Thiesen H.J.;
RT "Role of a mutant fas receptor in a transgenic mouse.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=17545588; DOI=10.1158/0008-5472.can-06-4006;
RA Villa-Morales M., Santos J., Perez-Gomez E., Quintanilla M.,
RA Fernandez-Piqueras J.;
RT "A role for the Fas/FasL system in modulating genetic susceptibility to T-
RT cell lymphoblastic lymphomas.";
RL Cancer Res. 67:5107-5116(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RX PubMed=7680478; DOI=10.1073/pnas.90.5.1756;
RA Adachi M., Watanabe-Fukunaga R., Nagata S.;
RT "Aberrant transcription caused by the insertion of an early transposable
RT element in an intron of the Fas antigen gene of lpr mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1756-1760(1993).
RN [8]
RP INTERACTION WITH DAXX.
RX PubMed=9215629; DOI=10.1016/s0092-8674(00)80294-9;
RA Yang X., Khosravi-Far R., Chang H.Y., Baltimore D.;
RT "Daxx, a novel Fas-binding protein that activates JNK and apoptosis.";
RL Cell 89:1067-1076(1997).
RN [9]
RP INTERACTION WITH HIPK3.
RX PubMed=11034606; DOI=10.1084/jem.192.8.1165;
RA Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K.,
RA Tschopp J.;
RT "FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces
RT FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase
RT activation.";
RL J. Exp. Med. 192:1165-1174(2000).
RN [10]
RP INTERACTION WITH NOL3.
RX PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
RA Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B., Hayakawa Y.,
RA Lee P., Korsmeyer S.J., Kitsis R.N.;
RT "Inhibition of both the extrinsic and intrinsic death pathways through
RT nonhomotypic death-fold interactions.";
RL Mol. Cell 15:901-912(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND THR-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206; SER-217; SER-220 AND
RP THR-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INDUCTION.
RX PubMed=23785138; DOI=10.1523/jneurosci.2757-12.2013;
RA Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
RA Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
RT "p75 neurotrophin receptor is a clock gene that regulates oscillatory
RT components of circadian and metabolic networks.";
RL J. Neurosci. 33:10221-10234(2013).
RN [15]
RP VARIANT LPR ASN-246.
RX PubMed=1372394; DOI=10.1038/356314a0;
RA Watanabe-Fukunaga R., Brannan C.I., Copeland N.G., Jenkins N.A., Nagata S.;
RT "Lymphoproliferation disorder in mice explained by defects in Fas antigen
RT that mediates apoptosis.";
RL Nature 356:314-317(1992).
CC -!- FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits
CC caspase-8 to the activated receptor. The resulting death-inducing
CC signaling complex (DISC) performs caspase-8 proteolytic activation
CC which initiates the subsequent cascade of caspases (aspartate-specific
CC cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may
CC have a role in the induction of peripheral tolerance, in the antigen-
CC stimulated suicide of mature T-cells, or both (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds DAXX (PubMed:9215629). Interacts with HIPK3
CC (PubMed:11034606). Part of a complex containing HIPK3 and FADD (By
CC similarity). Binds RIPK1 and FAIM2. Interacts with BABAM2 and FEM1B.
CC Interacts with FADD (By similarity). Interacts directly (via DED
CC domain) with NOL3 (via CARD domain); inhibits death-inducing signaling
CC complex (DISC) assembly by inhibiting the increase in FAS-FADD binding
CC induced by FAS activation (PubMed:15383280). Interacts with CALM (By
CC similarity). In the absence of stimulation, interacts with BIRC2, DDX3X
CC and GSK3B. The interaction with BIRC2 and DDX3X is further enhanced
CC upon receptor stimulation and accompanied by DDX3X and BIRC2 cleavage
CC (By similarity). {ECO:0000250|UniProtKB:P25445,
CC ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:15383280,
CC ECO:0000269|PubMed:9215629}.
CC -!- INTERACTION:
CC P25446; O89110: Casp8; NbExp=3; IntAct=EBI-296206, EBI-851690;
CC P25446; O35613: Daxx; NbExp=2; IntAct=EBI-296206, EBI-77304;
CC P25446; Q61160: Fadd; NbExp=3; IntAct=EBI-296206, EBI-524415;
CC P25446; Q9ERH7: Hipk3; NbExp=3; IntAct=EBI-296206, EBI-524356;
CC P25446; Q60953: Pml; NbExp=6; IntAct=EBI-296206, EBI-3895605;
CC P25446; Q9UER7: DAXX; Xeno; NbExp=4; IntAct=EBI-296206, EBI-77321;
CC P25446; Q13158: FADD; Xeno; NbExp=8; IntAct=EBI-296206, EBI-494804;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51867};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P51867}.
CC Membrane raft {ECO:0000250|UniProtKB:P25445}.
CC -!- TISSUE SPECIFICITY: Detected in various tissues including thymus,
CC liver, lung, heart, and adult ovary. {ECO:0000269|PubMed:1371136}.
CC -!- INDUCTION: Expression oscillates in a circadian manner in the liver
CC with peak levels seen at CT12. {ECO:0000269|PubMed:23785138}.
CC -!- DOMAIN: Contains a death domain involved in the binding of FADD, and
CC maybe to other cytosolic adapter proteins.
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC7 prevents the lysosomal
CC degradation of FAS regulating its expression at the plasma membrane.
CC {ECO:0000250|UniProtKB:P25445}.
CC -!- DISEASE: Note=Defects in Fas are the cause of the lymphoproliferation
CC phenotype (lpr). Lpr mice show lymphadenopathy and autoantibody
CC production.
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DR EMBL; M83649; AAA37593.1; -; mRNA.
DR EMBL; AK002590; BAB22211.1; -; mRNA.
DR EMBL; AJ295702; CAC00638.1; -; Genomic_DNA.
DR EMBL; AJ295703; CAC00638.1; JOINED; Genomic_DNA.
DR EMBL; AJ295704; CAC00638.1; JOINED; Genomic_DNA.
DR EMBL; DQ846748; ABI24112.1; -; mRNA.
DR EMBL; CH466534; EDL41748.1; -; Genomic_DNA.
DR EMBL; BC061160; AAH61160.1; -; mRNA.
DR EMBL; S56490; AAB25700.1; -; Genomic_DNA.
DR EMBL; S56485; AAB25700.1; JOINED; Genomic_DNA.
DR EMBL; S56486; AAB25700.1; JOINED; Genomic_DNA.
DR CCDS; CCDS29758.1; -.
DR PIR; A46484; A46484.
DR RefSeq; NP_032013.2; NM_007987.2.
DR PDB; 2NA6; NMR; -; A/B/C=167-193.
DR PDB; 3OQ9; X-ray; 6.80 A; A/B/C/D/E=223-308.
DR PDBsum; 2NA6; -.
DR PDBsum; 3OQ9; -.
DR AlphaFoldDB; P25446; -.
DR SMR; P25446; -.
DR BioGRID; 199594; 10.
DR DIP; DIP-31093N; -.
DR IntAct; P25446; 11.
DR MINT; P25446; -.
DR STRING; 10090.ENSMUSP00000025691; -.
DR GlyGen; P25446; 2 sites.
DR iPTMnet; P25446; -.
DR PhosphoSitePlus; P25446; -.
DR SwissPalm; P25446; -.
DR EPD; P25446; -.
DR jPOST; P25446; -.
DR MaxQB; P25446; -.
DR PaxDb; P25446; -.
DR PeptideAtlas; P25446; -.
DR PRIDE; P25446; -.
DR ProteomicsDB; 258946; -.
DR ABCD; P25446; 16 sequenced antibodies.
DR Antibodypedia; 4525; 2990 antibodies from 54 providers.
DR DNASU; 14102; -.
DR Ensembl; ENSMUST00000025691; ENSMUSP00000025691; ENSMUSG00000024778.
DR GeneID; 14102; -.
DR KEGG; mmu:14102; -.
DR UCSC; uc008hgi.2; mouse.
DR CTD; 355; -.
DR MGI; MGI:95484; Fas.
DR VEuPathDB; HostDB:ENSMUSG00000024778; -.
DR eggNOG; ENOG502S0SV; Eukaryota.
DR GeneTree; ENSGT00950000183126; -.
DR HOGENOM; CLU_067123_1_0_1; -.
DR InParanoid; P25446; -.
DR OMA; QDTKCRC; -.
DR OrthoDB; 993446at2759; -.
DR PhylomeDB; P25446; -.
DR TreeFam; TF333916; -.
DR Reactome; R-MMU-3371378; Regulation by c-FLIP.
DR Reactome; R-MMU-5218900; CASP8 activity is inhibited.
DR Reactome; R-MMU-69416; Dimerization of procaspase-8.
DR Reactome; R-MMU-75157; FasL/ CD95L signaling.
DR BioGRID-ORCS; 14102; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Fas; mouse.
DR EvolutionaryTrace; P25446; -.
DR PRO; PR:P25446; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P25446; protein.
DR Bgee; ENSMUSG00000024778; Expressed in granulocyte and 157 other tissues.
DR ExpressionAtlas; P25446; baseline and differential.
DR Genevisible; P25446; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; ISO:MGI.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0019724; P:B cell mediated immunity; IMP:MGI.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0071455; P:cellular response to hyperoxia; ISO:MGI.
DR GO; GO:0071285; P:cellular response to lithium ion; IMP:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0031104; P:dendrite regeneration; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
DR GO; GO:0036337; P:Fas signaling pathway; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IGI:MGI.
DR GO; GO:0006925; P:inflammatory cell apoptotic process; IDA:MGI.
DR GO; GO:0070227; P:lymphocyte apoptotic process; IDA:MGI.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0097527; P:necroptotic signaling pathway; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0050869; P:negative regulation of B cell activation; IMP:MGI.
DR GO; GO:1900148; P:negative regulation of Schwann cell migration; ISO:MGI.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; ISO:MGI.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IC:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IMP:MGI.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0051384; P:response to glucocorticoid; IMP:MGI.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0048536; P:spleen development; IMP:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR CDD; cd08316; Death_FAS_TNFRSF6; 1.
DR CDD; cd10579; TNFRSF6; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR008063; Fas_rcpt.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR033998; TNFRSF6_death.
DR InterPro; IPR033999; TNFRSF6_N.
DR PANTHER; PTHR46874; PTHR46874; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01680; TNFACTORR6.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 3.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Calmodulin-binding; Cell membrane;
KW Disease variant; Disulfide bond; Glycoprotein; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..327
FT /note="Tumor necrosis factor receptor superfamily member 6"
FT /id="PRO_0000034567"
FT TOPO_DOM 22..169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 43..79
FT /note="TNFR-Cys 1"
FT REPEAT 80..123
FT /note="TNFR-Cys 2"
FT REPEAT 124..162
FT /note="TNFR-Cys 3"
FT DOMAIN 222..306
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 204..309
FT /note="Interaction with HIPK3"
FT /evidence="ECO:0000269|PubMed:11034606"
FT REGION 222..246
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT LIPID 194
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 56..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 59..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 81..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 100..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 103..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 125..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 142..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 145..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VARIANT 246
FT /note="I -> N (in lpr)"
FT /evidence="ECO:0000269|PubMed:1372394"
FT CONFLICT 38
FT /note="R -> H (in Ref. 1; AAA37593, 2; CAC00638 and 7;
FT AAB25700)"
FT /evidence="ECO:0000305"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:2NA6"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2NA6"
SQ SEQUENCE 327 AA; 37437 MW; D8DA95CA525CED56 CRC64;
MLWIWAVLPL VLAGSQLRVH TQGTNSISES LKLRRRVRET DKNCSEGLYQ GGPFCCQPCQ
PGKKKVEDCK MNGGTPTCAP CTEGKEYMDK NHYADKCRRC TLCDEEHGLE VETNCTLTQN
TKCKCKPDFY CDSPGCEHCV RCASCEHGTL EPCTATSNTN CRKQSPRNRL WLLTILVLLI
PLVFIYRKYR KRKCWKRRQD DPESRTSSRE TIPMNASNLS LSKYIPRIAE DMTIQEAKKF
ARENNIKEGK IDEIMHDSIQ DTAEQKVQLL LCWYQSHGKS DAYQDLIKGL KKAECRRTLD
KFQDMVQKDL GKSTPDTGNE NEGQCLE
