ID TR10B_HUMAN Reviewed; 440 AA. AC O14763; O14720; O15508; O15517; O15531; Q6UXM8; Q7Z360; Q9BVE0; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 13-FEB-2019, entry version 206. DE RecName: Full=Tumor necrosis factor receptor superfamily member 10B; DE AltName: Full=Death receptor 5; DE AltName: Full=TNF-related apoptosis-inducing ligand receptor 2; DE Short=TRAIL receptor 2; DE Short=TRAIL-R2; DE AltName: CD_antigen=CD262; DE Flags: Precursor; GN Name=TNFRSF10B; Synonyms=DR5, KILLER, TRAILR2, TRICK2, ZTNFR9; GN ORFNames=UNQ160/PRO186; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), ALTERNATIVE RP SPLICING, AND VARIANTS LEU-32; VAL-67 AND ALA-191. RX PubMed=9285725; DOI=10.1016/S0960-9822(06)00297-1; RA Screaton G.R., Mongkolsapaya J., Xu X.-N., Cowper A.E., RA McMichael A.J., Bell J.I.; RT "TRICK2, a new alternatively spliced receptor that transduces the RT cytotoxic signal from TRAIL."; RL Curr. Biol. 7:693-696(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF RP N-TERMINUS, AND VARIANT ALA-191. RC TISSUE=Foreskin fibroblast; RX PubMed=9311998; DOI=10.1093/emboj/16.17.5386; RA Walczak H., Degli-Esposti M.A., Johnson R.S., Smolak P.J., Waugh J.Y., RA Boiani N., Timour M.S., Gerhart M.J., Schooley K.A., Smith C.A., RA Goodwin R.G., Rauch C.T.; RT "TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL."; RL EMBO J. 16:5386-5397(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), CHARACTERIZATION, AND RP VARIANTS LEU-32; VAL-67 AND ALA-191. RC TISSUE=Liver, and Spleen; RX PubMed=9373179; DOI=10.1016/S0014-5793(97)01231-3; RA Schneider P., Bodmer J.-L., Thome M., Hofmann K., Holler N., RA Tschopp J.; RT "Characterization of two receptors for TRAIL."; RL FEBS Lett. 416:329-334(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANTS LEU-32 AND RP VAL-67. RX PubMed=9430227; DOI=10.1016/S1074-7613(00)80400-8; RA Chaudhary P.M., Eby M., Jasmin A., Bookwalter A., Murray J., Hood L.; RT "Death receptor 5, a new member of the TNFR family, and DR4 induce RT FADD-dependent apoptosis and activate the NF-kappaB pathway."; RL Immunity 7:821-830(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANTS LEU-32 AND RP VAL-67. RX PubMed=9325248; DOI=10.1074/jbc.272.41.25417; RA MacFarlane M., Ahmad M., Srinivasula S.M., Fernandes-Alnemri T., RA Cohen G.M., Alnemri E.S.; RT "Identification and molecular cloning of two novel receptors for the RT cytotoxic ligand TRAIL."; RL J. Biol. Chem. 272:25417-25420(1997). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RC TISSUE=Ovary; RX PubMed=9326928; DOI=10.1038/ng1097-141; RA Wu G.S., Burns T.F., McDonald E.R. III, Jiang W., Meng R., RA Krantz I.D., Kao G., Gan D.D., Zhou J.Y., Muschel R., Hamilton S.R., RA Spinner N.B., Markowitz S., Wu G., el-Deiry W.S.; RT "KILLER/DR5 is a DNA damage-inducible p53-regulated death receptor RT gene."; RL Nat. Genet. 17:141-143(1997). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RX PubMed=9242610; DOI=10.1126/science.277.5327.815; RA Pan G., Ni J., Wei Y.-F., Yu G.-L., Gentz R., Dixit V.M.; RT "An antagonist decoy receptor and a death domain-containing receptor RT for TRAIL."; RL Science 277:815-818(1997). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANT LEU-32. RX PubMed=9242611; DOI=10.1126/science.277.5327.818; RA Sheridan J.P., Marsters S.A., Pitti R.M., Gurney A., Skubatch M., RA Baldwin D.T., Ramakrishnan L., Gray C.L., Baker K., Wood W.I., RA Goddard A.D., Godowski P.J., Ashkenazi A.; RT "Control of TRAIL-induced apoptosis by a family of signaling and decoy RT receptors."; RL Science 277:818-821(1997). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS RP LEU-32; VAL-67 AND ALA-191. RX PubMed=10072170; DOI=10.1016/S0304-3835(98)00230-4; RA Arai T., Akiyama Y., Okabe S., Saito K., Iwai T., Yuasa Y.; RT "Genomic organization and mutation analyses of the DR5/TRAIL receptor RT 2 gene in colorectal carcinomas."; RL Cancer Lett. 133:197-204(1998). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). RA Cao X., Zhang W., Wan T.; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND VARIANTS LEU-32 AND RP VAL-67. RA Farrah T., Vu T., Gilbert T., Gross J., O'Hara P.; RT "Homo sapiens homolog of tumor necrosis factor receptor."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), AND VARIANT RP LEU-32. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT RP LEU-32. RC TISSUE=Colon endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANTS RP LEU-32 AND ALA-191. RC TISSUE=Cervix; 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 [16] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [17] RP FUNCTION, AND INDUCTION. RX PubMed=15322075; DOI=10.1074/jbc.M406933200; RA Yamaguchi H., Wang H.G.; RT "CHOP is involved in endoplasmic reticulum stress-induced apoptosis by RT enhancing DR5 expression in human carcinoma cells."; RL J. Biol. Chem. 279:45495-45502(2004). RN [18] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL141. RX PubMed=23498957; DOI=10.1016/j.chom.2013.02.003; RA Smith W., Tomasec P., Aicheler R., Loewendorf A., Nemcovicova I., RA Wang E.C., Stanton R.J., Macauley M., Norris P., Willen L., RA Ruckova E., Nomoto A., Schneider P., Hahn G., Zajonc D.M., Ware C.F., RA Wilkinson G.W., Benedict C.A.; RT "Human cytomegalovirus glycoprotein UL141 targets the TRAIL death RT receptors to thwart host innate antiviral defenses."; RL Cell Host Microbe 13:324-335(2013). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 54-183 IN COMPLEX WITH RP TNFSF10, DISULFIDE BOND, AND SUBUNIT. RX PubMed=10549288; DOI=10.1016/S1097-2765(00)80207-5; RA Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., RA Kelley R.F., Ashkenazi A., de Vos A.M.; RT "Triggering cell death: the crystal structure of Apo2L/TRAIL in a RT complex with death receptor 5."; RL Mol. Cell 4:563-571(1999). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 69-184 IN COMPLEX WITH RP TNFSF10, AND DISULFIDE BOND. RX PubMed=10542098; DOI=10.1038/14935; RA Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., RA Jones E.Y., Screaton G.R.; RT "Structure of the TRAIL-DR5 complex reveals mechanisms conferring RT specificity in apoptotic initiation."; RL Nat. Struct. Biol. 6:1048-1053(1999). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 58-184, INTERACTION WITH RP HUMAN CYTOMEGALOVIRUS PROTEIN UL141, AND DISULFIDE BOND. RX PubMed=23555243; DOI=10.1371/journal.ppat.1003224; RA Nemcovicova I., Benedict C.A., Zajonc D.M.; RT "Structure of human cytomegalovirus UL141 binding to TRAIL-R2 reveals RT novel, non-canonical death receptor interactions."; RL PLoS Pathog. 9:E1003224-E1003224(2013). CC -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL CC (PubMed:10549288). The adapter molecule FADD recruits caspase-8 to CC the activated receptor. The resulting death-inducing signaling CC complex (DISC) performs caspase-8 proteolytic activation which CC initiates the subsequent cascade of caspases (aspartate-specific CC cysteine proteases) mediating apoptosis. Promotes the activation CC of NF-kappa-B. Essential for ER stress-induced apoptosis. CC {ECO:0000269|PubMed:10542098, ECO:0000269|PubMed:10549288, CC ECO:0000269|PubMed:15322075}. CC -!- SUBUNIT: Monomer (PubMed:10549288). Can interact with TRADD and CC RIPK1. Interacts with HCMV protein UL141; this interaction CC prevents TNFRSF10B cell surface expression. Two TNFRSF10B monomers CC interact with a UL141 homodimer. Three TNFRSF10B molecules CC interact with TNFSF10 homotrimer (PubMed:10549288). CC {ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:23498957, CC ECO:0000269|PubMed:23555243}. CC -!- INTERACTION: CC P50591:TNFSF10; NbExp=21; IntAct=EBI-518882, EBI-495373; CC Q96MV8:ZDHHC15; NbExp=4; IntAct=EBI-518882, EBI-12837904; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Long; Synonyms=TRICK2B; CC IsoId=O14763-1; Sequence=Displayed; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=3; CC IsoId=O14763-3; Sequence=VSP_039125; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=Short; Synonyms=TRICK2A; CC IsoId=O14763-2; Sequence=VSP_006490; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues; CC very highly expressed in tumor cell lines such as HeLaS3, K-562, CC HL-60, SW480, A-549 and G-361; highly expressed in heart, CC peripheral blood lymphocytes, liver, pancreas, spleen, thymus, CC prostate, ovary, uterus, placenta, testis, esophagus, stomach and CC throughout the intestinal tract; not detectable in brain. CC -!- INDUCTION: By ER stress. Regulated by p53/TP53. CC {ECO:0000269|PubMed:15322075}. CC -!- DISEASE: Squamous cell carcinoma of the head and neck (HNSCC) CC [MIM:275355]: A non-melanoma skin cancer affecting the head and CC neck. The hallmark of cutaneous SCC is malignant transformation of CC normal epidermal keratinocytes. Note=The disease may be caused by CC mutations affecting the gene represented in this entry. 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; AF018657; AAB70577.1; -; mRNA. DR EMBL; AF018658; AAB70578.1; -; mRNA. DR EMBL; AF016849; AAC51778.1; -; mRNA. DR EMBL; AF016266; AAB81180.1; -; mRNA. DR EMBL; AF016268; AAC01565.1; -; mRNA. DR EMBL; AF020501; AAB71412.1; -; mRNA. DR EMBL; AF022386; AAB71949.1; -; mRNA. DR EMBL; AF012628; AAB67109.1; -; mRNA. DR EMBL; AF012535; AAB67103.1; -; mRNA. DR EMBL; AB014718; BAA33723.1; -; Genomic_DNA. DR EMBL; AF153687; AAF75587.1; -; mRNA. DR EMBL; AF192548; AAF07175.1; -; mRNA. DR EMBL; AY358277; AAQ88644.1; -; mRNA. DR EMBL; BX538104; CAD98017.1; -; mRNA. DR EMBL; AC107959; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001281; AAH01281.1; -; mRNA. DR CCDS; CCDS6035.1; -. [O14763-1] DR CCDS; CCDS6036.1; -. [O14763-2] DR RefSeq; NP_003833.4; NM_003842.4. [O14763-1] DR RefSeq; NP_671716.2; NM_147187.2. [O14763-2] DR UniGene; Hs.521456; -. DR UniGene; Hs.661668; -. DR PDB; 1D0G; X-ray; 2.40 A; R/S/T=54-183. DR PDB; 1D4V; X-ray; 2.20 A; A=69-184. DR PDB; 1DU3; X-ray; 2.20 A; A/B/C/G/H/I=54-183. DR PDB; 1ZA3; X-ray; 3.35 A; R/S=54-183. DR PDB; 2H9G; X-ray; 2.32 A; R/S=54-183. DR PDB; 3X3F; X-ray; 2.10 A; A=54-184. DR PDB; 4I9X; X-ray; 2.10 A; C/D=58-184. DR PDB; 4N90; X-ray; 3.30 A; R/S/T=57-182. DR PDB; 4OD2; X-ray; 3.20 A; S=73-183. DR PDBsum; 1D0G; -. DR PDBsum; 1D4V; -. DR PDBsum; 1DU3; -. DR PDBsum; 1ZA3; -. DR PDBsum; 2H9G; -. DR PDBsum; 3X3F; -. DR PDBsum; 4I9X; -. DR PDBsum; 4N90; -. DR PDBsum; 4OD2; -. DR ProteinModelPortal; O14763; -. DR SMR; O14763; -. DR BioGrid; 114323; 67. DR CORUM; O14763; -. DR DIP; DIP-33566N; -. DR IntAct; O14763; 17. DR MINT; O14763; -. DR STRING; 9606.ENSP00000276431; -. DR BindingDB; O14763; -. DR ChEMBL; CHEMBL1075153; -. DR DrugBank; DB05895; HGS-TR2J. DR GuidetoPHARMACOLOGY; 1880; -. DR iPTMnet; O14763; -. DR PhosphoSitePlus; O14763; -. DR SwissPalm; O14763; -. DR BioMuta; TNFRSF10B; -. DR EPD; O14763; -. DR jPOST; O14763; -. DR MaxQB; O14763; -. DR PaxDb; O14763; -. DR PeptideAtlas; O14763; -. DR PRIDE; O14763; -. DR ProteomicsDB; 48210; -. DR ProteomicsDB; 48211; -. [O14763-2] DR ProteomicsDB; 48212; -. [O14763-3] DR DNASU; 8795; -. DR Ensembl; ENST00000276431; ENSP00000276431; ENSG00000120889. [O14763-1] DR Ensembl; ENST00000347739; ENSP00000317859; ENSG00000120889. [O14763-2] DR GeneID; 8795; -. DR KEGG; hsa:8795; -. DR UCSC; uc003xct.4; human. [O14763-1] DR CTD; 8795; -. DR DisGeNET; 8795; -. DR EuPathDB; HostDB:ENSG00000120889.12; -. DR GeneCards; TNFRSF10B; -. DR HGNC; HGNC:11905; TNFRSF10B. DR HPA; HPA023625; -. DR MalaCards; TNFRSF10B; -. DR MIM; 275355; phenotype. DR MIM; 603612; gene. DR neXtProt; NX_O14763; -. DR OpenTargets; ENSG00000120889; -. DR Orphanet; 500481; Squamous cell carcinoma of salivary glands. DR Orphanet; 494547; Squamous cell carcinoma of the hypopharynx. DR Orphanet; 494550; Squamous cell carcinoma of the larynx. DR Orphanet; 502366; Squamous cell carcinoma of the lip. DR Orphanet; 500464; Squamous cell carcinoma of the nasal cavity and paranasal sinuses. DR Orphanet; 502363; Squamous cell carcinoma of the oral cavity. DR Orphanet; 500478; Squamous cell carcinoma of the oropharynx. DR PharmGKB; PA36598; -. DR eggNOG; ENOG410IZX0; Eukaryota. DR eggNOG; ENOG4111ZZM; LUCA. DR GeneTree; ENSGT00940000164765; -. DR HOVERGEN; HBG061626; -. DR InParanoid; O14763; -. DR KO; K04722; -. DR OMA; GRDCISC; -. DR OrthoDB; 1448442at2759; -. DR PhylomeDB; O14763; -. DR TreeFam; TF333916; -. DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-3371378; Regulation by c-FLIP. DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis. DR Reactome; R-HSA-5218900; CASP8 activity is inhibited. DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands. DR Reactome; R-HSA-69416; Dimerization of procaspase-8. DR Reactome; R-HSA-75158; TRAIL signaling. DR SignaLink; O14763; -. DR SIGNOR; O14763; -. DR EvolutionaryTrace; O14763; -. DR GeneWiki; TNFRSF10B; -. DR GenomeRNAi; 8795; -. DR PRO; PR:O14763; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000120889; Expressed in 223 organ(s), highest expression level in oviduct epithelium. DR ExpressionAtlas; O14763; baseline and differential. DR Genevisible; O14763; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB. DR GO; GO:0045569; F:TRAIL binding; NAS:UniProtKB. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome. DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:Reactome. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; NAS:UniProtKB. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome. DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; TAS:Reactome. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB. DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central. DR CDD; cd08315; Death_TRAILR_DR4_DR5; 1. DR CDD; cd10580; TNFRSF10; 1. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_domain. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR InterPro; IPR020465; TNFR_10. DR InterPro; IPR034024; TNFRSF10_N. DR InterPro; IPR034029; TNFRSF10A/B_death. DR Pfam; PF00531; Death; 1. DR Pfam; PF00020; TNFR_c6; 2. DR PIRSF; PIRSF037867; CD261_antigen; 1. DR PRINTS; PR01956; TNFACTORR10. DR SMART; SM00005; DEATH; 1. DR SMART; SM00208; TNFR; 2. 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; Alternative splicing; Apoptosis; Complete proteome; KW Direct protein sequencing; Disulfide bond; Membrane; Polymorphism; KW Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 55 {ECO:0000269|PubMed:9311998}. FT CHAIN 56 440 Tumor necrosis factor receptor FT superfamily member 10B. FT /FTId=PRO_0000034580. FT TOPO_DOM 56 210 Extracellular. {ECO:0000255}. FT TRANSMEM 211 231 Helical. {ECO:0000255}. FT TOPO_DOM 232 440 Cytoplasmic. {ECO:0000255}. FT REPEAT 57 94 TNFR-Cys 1. FT REPEAT 97 137 TNFR-Cys 2. FT REPEAT 138 178 TNFR-Cys 3. FT REPEAT 192 206 TAPE. FT DOMAIN 339 422 Death. {ECO:0000255|PROSITE- FT ProRule:PRU00064}. FT COMPBIAS 250 253 Poly-Gly. FT DISULFID 81 94 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT DISULFID 97 113 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT DISULFID 116 129 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT DISULFID 119 137 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT DISULFID 139 153 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000244|PDB:4N90, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT DISULFID 156 170 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT DISULFID 160 178 {ECO:0000244|PDB:1D0G, FT ECO:0000244|PDB:1D4V, FT ECO:0000244|PDB:4I9X, FT ECO:0000269|PubMed:10542098, FT ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:23555243}. FT VAR_SEQ 119 440 Missing (in isoform 3). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_039125. FT VAR_SEQ 185 213 Missing (in isoform Short). FT {ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:9242610, FT ECO:0000303|PubMed:9242611, FT ECO:0000303|PubMed:9285725, FT ECO:0000303|PubMed:9325248, FT ECO:0000303|PubMed:9326928, FT ECO:0000303|PubMed:9430227, FT ECO:0000303|Ref.10, ECO:0000303|Ref.11}. FT /FTId=VSP_006490. FT VARIANT 32 32 P -> L (in dbSNP:rs1129424). FT {ECO:0000269|PubMed:10072170, FT ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:9242611, FT ECO:0000269|PubMed:9285725, FT ECO:0000269|PubMed:9325248, FT ECO:0000269|PubMed:9373179, FT ECO:0000269|PubMed:9430227, FT ECO:0000269|Ref.11}. FT /FTId=VAR_016153. FT VARIANT 67 67 A -> V (in dbSNP:rs1047266). FT {ECO:0000269|PubMed:10072170, FT ECO:0000269|PubMed:9285725, FT ECO:0000269|PubMed:9325248, FT ECO:0000269|PubMed:9373179, FT ECO:0000269|PubMed:9430227, FT ECO:0000269|Ref.11}. FT /FTId=VAR_016154. FT VARIANT 191 191 V -> A (in dbSNP:rs13265018). FT {ECO:0000269|PubMed:10072170, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9285725, FT ECO:0000269|PubMed:9311998, FT ECO:0000269|PubMed:9373179}. FT /FTId=VAR_059831. FT CONFLICT 439 439 M -> L (in Ref. 8; AAB67103 and 12; FT AAQ88644). {ECO:0000305}. FT STRAND 77 79 {ECO:0000244|PDB:1D4V}. FT STRAND 85 87 {ECO:0000244|PDB:3X3F}. FT STRAND 89 91 {ECO:0000244|PDB:1D4V}. FT STRAND 94 96 {ECO:0000244|PDB:3X3F}. FT TURN 99 101 {ECO:0000244|PDB:3X3F}. FT STRAND 106 108 {ECO:0000244|PDB:3X3F}. FT STRAND 110 112 {ECO:0000244|PDB:3X3F}. FT STRAND 123 127 {ECO:0000244|PDB:3X3F}. FT STRAND 131 133 {ECO:0000244|PDB:1D4V}. FT STRAND 136 142 {ECO:0000244|PDB:3X3F}. FT STRAND 143 145 {ECO:0000244|PDB:4I9X}. FT STRAND 153 155 {ECO:0000244|PDB:4I9X}. FT STRAND 164 166 {ECO:0000244|PDB:4I9X}. FT STRAND 172 174 {ECO:0000244|PDB:1DU3}. FT STRAND 178 180 {ECO:0000244|PDB:4I9X}. SQ SEQUENCE 440 AA; 47878 MW; 60358EAF2A835870 CRC64; MEQRGQNAPA ASGARKRHGP GPREARGARP GPRVPKTLVL VVAAVLLLVS AESALITQQD LAPQQRAAPQ QKRSSPSEGL CPPGHHISED GRDCISCKYG QDYSTHWNDL LFCLRCTRCD SGEVELSPCT TTRNTVCQCE EGTFREEDSP EMCRKCRTGC PRGMVKVGDC TPWSDIECVH KESGTKHSGE VPAVEETVTS SPGTPASPCS LSGIIIGVTV AAVVLIVAVF VCKSLLWKKV LPYLKGICSG GGGDPERVDR SSQRPGAEDN VLNEIVSILQ PTQVPEQEME VQEPAEPTGV NMLSPGESEH LLEPAEAERS QRRRLLVPAN EGDPTETLRQ CFDDFADLVP FDSWEPLMRK LGLMDNEIKV AKAEAAGHRD TLYTMLIKWV NKTGRDASVH TLLDALETLG ERLAKQKIED HLLSSGKFMY LEGNADSAMS //