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Database: UniProt
Entry: O14763
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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   29-OCT-2014, entry version 165.
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.
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.
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, AND INTERACTION WITH
RP   HUMAN CYTOMEGALOVIRUS PROTEIN UL141.
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. The
CC       adapter molecule FADD recruits caspase-8 to the activated
CC       receptor. The resulting death-inducing signaling complex (DISC)
CC       performs caspase-8 proteolytic activation which initiates the
CC       subsequent cascade of caspases (aspartate-specific cysteine
CC       proteases) mediating apoptosis. Promotes the activation of NF-
CC       kappa-B. Essential for ER stress-induced apoptosis.
CC       {ECO:0000269|PubMed:15322075}.
CC   -!- SUBUNIT: Homotrimer. Can interact with TRADD and RIPK1. Interacts
CC       with HCMV protein UL141; this interaction prevents TNFRSF10B cell
CC       surface expression. Two TNFRSF10B monomers interact with a UL141
CC       homodimer. {ECO:0000269|PubMed:23498957,
CC       ECO:0000269|PubMed:23555243}.
CC   -!- INTERACTION:
CC       P50591:TNFSF10; NbExp=21; IntAct=EBI-518882, EBI-495373;
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   -!- SIMILARITY: Contains 1 death domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00064}.
CC   -!- SIMILARITY: Contains 3 TNFR-Cys repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00206}.
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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   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; 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; 4I9X; -.
DR   PDBsum; 4N90; -.
DR   PDBsum; 4OD2; -.
DR   ProteinModelPortal; O14763; -.
DR   SMR; O14763; 75-182.
DR   BioGrid; 114323; 49.
DR   DIP; DIP-33566N; -.
DR   IntAct; O14763; 6.
DR   MINT; MINT-109111; -.
DR   STRING; 9606.ENSP00000276431; -.
DR   ChEMBL; CHEMBL1075153; -.
DR   GuidetoPHARMACOLOGY; 1880; -.
DR   PhosphoSite; O14763; -.
DR   MaxQB; O14763; -.
DR   PaxDb; O14763; -.
DR   PRIDE; O14763; -.
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.2; human. [O14763-2]
DR   UCSC; uc003xcu.2; human. [O14763-1]
DR   CTD; 8795; -.
DR   GeneCards; GC08M022877; -.
DR   HGNC; HGNC:11905; TNFRSF10B.
DR   HPA; HPA023625; -.
DR   MIM; 275355; phenotype.
DR   MIM; 603612; gene.
DR   neXtProt; NX_O14763; -.
DR   Orphanet; 67037; Squamous cell carcinoma of head and neck.
DR   PharmGKB; PA36598; -.
DR   eggNOG; NOG131298; -.
DR   GeneTree; ENSGT00730000110985; -.
DR   HOVERGEN; HBG061626; -.
DR   InParanoid; O14763; -.
DR   KO; K04722; -.
DR   OMA; EMEVQEP; -.
DR   OrthoDB; EOG71VSSN; -.
DR   PhylomeDB; O14763; -.
DR   TreeFam; TF333916; -.
DR   Reactome; REACT_1503; Caspase-8 activation.
DR   Reactome; REACT_164011; Regulation by c-FLIP.
DR   Reactome; REACT_402; TRAIL signaling.
DR   Reactome; REACT_832; Dimerization of procaspase-8.
DR   SignaLink; O14763; -.
DR   EvolutionaryTrace; O14763; -.
DR   GeneWiki; TNFRSF10B; -.
DR   GenomeRNAi; 8795; -.
DR   NextBio; 32984; -.
DR   PRO; PR:O14763; -.
DR   Bgee; O14763; -.
DR   CleanEx; HS_TNFRSF10B; -.
DR   ExpressionAtlas; O14763; baseline and differential.
DR   Genevestigator; O14763; -.
DR   GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004872; F: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:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR   GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR   Gene3D; 1.10.533.10; -; 1.
DR   InterPro; IPR011029; DEATH-like_dom.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020465; TNFR_10.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00020; TNFR_c6; 1.
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
FT   DISULFID     97    113
FT   DISULFID    116    129
FT   DISULFID    119    137
FT   DISULFID    139    153
FT   DISULFID    156    170
FT   DISULFID    160    178
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:4I9X}.
FT   STRAND       89     91       {ECO:0000244|PDB:1D4V}.
FT   STRAND       94     96       {ECO:0000244|PDB:4I9X}.
FT   TURN         99    101       {ECO:0000244|PDB:4I9X}.
FT   STRAND      106    108       {ECO:0000244|PDB:4I9X}.
FT   STRAND      110    112       {ECO:0000244|PDB:2H9G}.
FT   STRAND      123    127       {ECO:0000244|PDB:4I9X}.
FT   STRAND      131    133       {ECO:0000244|PDB:1D4V}.
FT   STRAND      136    139       {ECO:0000244|PDB:4I9X}.
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
//
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