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 27-MAR-2024, entry version 224. 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 CASP8 to the activated receptor. The resulting death-inducing CC signaling complex (DISC) performs CASP8 proteolytic activation which CC 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|UniProtKB:P25445}. CC -!- SUBUNIT: Component of the death-induced signaling complex (DISC) CC composed of cell surface receptor FAS/CD95, adapter protein FADD and CC the CASP8 protease; recruitment of CASP8 to the complex is required for CC processing of CASP8 into the p18 and p10 subunits (By similarity). CC Interacts directly (via DED domain) with NOL3 (via CARD domain); CC inhibits death-inducing signaling complex (DISC) assembly by inhibiting CC the increase in FAS-FADD binding induced by FAS activation CC (PubMed:15383280). 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 CALM (By similarity). In the absence of stimulation, CC interacts with BIRC2, DDX3X and GSK3B. The interaction with BIRC2 and CC DDX3X is further enhanced upon receptor stimulation and accompanied by CC DDX3X and BIRC2 cleavage (By similarity). CC {ECO:0000250|UniProtKB:P25445, ECO:0000269|PubMed:11034606, CC ECO:0000269|PubMed:15383280, 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) (PubMed:1372394). Lpr mice show lymphadenopathy and CC autoantibody production (PubMed:1372394). {ECO:0000269|PubMed:1372394}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 12. DR DIP; DIP-31093N; -. DR IntAct; P25446; 11. DR MINT; P25446; -. DR STRING; 10090.ENSMUSP00000025691; -. DR GlyCosmos; P25446; 2 sites, No reported glycans. DR GlyGen; P25446; 4 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P25446; -. DR PhosphoSitePlus; P25446; -. DR SwissPalm; P25446; -. DR EPD; P25446; -. DR jPOST; P25446; -. DR MaxQB; P25446; -. DR PaxDb; 10090-ENSMUSP00000025691; -. DR PeptideAtlas; P25446; -. DR ProteomicsDB; 258946; -. DR Pumba; P25446; -. DR ABCD; P25446; 16 sequenced antibodies. DR Antibodypedia; 4525; 3239 antibodies from 54 providers. DR DNASU; 14102; -. DR Ensembl; ENSMUST00000025691.13; ENSMUSP00000025691.6; ENSMUSG00000024778.14. DR GeneID; 14102; -. DR KEGG; mmu:14102; -. DR UCSC; uc008hgi.2; mouse. DR AGR; MGI:95484; -. 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; RDTKCRC; -. DR OrthoDB; 24515at2759; -. 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 78 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 159 other cell types or tissues. DR ExpressionAtlas; P25446; baseline and differential. 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: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:0045121; C:membrane raft; 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: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: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; Death Domain, Fas; 1. DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2. 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; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 6; 1. DR PANTHER; PTHR46874:SF1; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 6; 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; DEATH domain; 1. DR SUPFAM; SSF57586; TNF receptor-like; 2. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS00652; TNFR_NGFR_1; 2. DR PROSITE; PS50050; TNFR_NGFR_2; 2. DR Genevisible; P25446; MM. 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 //