ID TR10C_HUMAN Reviewed; 259 AA. AC O14798; O14755; Q08AS6; Q6FH98; Q6UXM5; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 24-JAN-2024, entry version 184. DE RecName: Full=Tumor necrosis factor receptor superfamily member 10C; DE AltName: Full=Antagonist decoy receptor for TRAIL/Apo-2L; DE AltName: Full=Decoy TRAIL receptor without death domain; DE AltName: Full=Decoy receptor 1; DE Short=DcR1; DE AltName: Full=Lymphocyte inhibitor of TRAIL; DE AltName: Full=TNF-related apoptosis-inducing ligand receptor 3; DE Short=TRAIL receptor 3; DE Short=TRAIL-R3; DE AltName: Full=TRAIL receptor without an intracellular domain; DE AltName: CD_antigen=CD263; DE Flags: Precursor; GN Name=TNFRSF10C; Synonyms=DCR1, LIT, TRAILR3, TRID; GN ORFNames=UNQ321/PRO366; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-229. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANT THR-229. RC TISSUE=Foreskin fibroblast; RX PubMed=9314565; DOI=10.1084/jem.186.7.1165; RA Degli-Esposti M.A., Smolak P.J., Walczak H., Waugh J., Huang C.-P., RA DuBose R.F., Goodwin R.G., Smith C.A.; RT "Cloning and characterization of TRAIL-R3, a novel member of the emerging RT TRAIL receptor family."; RL J. Exp. Med. 186:1165-1170(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-229. 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 for RT TRAIL."; RL Science 277:815-818(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND VARIANT RP THR-229. 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANT THR-229. 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., Tschopp J.; RT "Characterization of two receptors for TRAIL."; RL FEBS Lett. 416:329-334(1997). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-229. RX PubMed=9551946; RA Mongkolsapaya J., Cowper A.E., Xu X.-N., Morris G., McMichael A.J., RA Bell J.I., Screaton G.R.; RT "Lymphocyte inhibitor of TRAIL (TNF-related apoptosis-inducing ligand): a RT new receptor protecting lymphocytes from the death ligand TRAIL."; RL J. Immunol. 160:3-6(1998). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-229. 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., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] 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., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., 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., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-229. 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 [11] RP PROTEIN SEQUENCE OF 26-40. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). CC -!- FUNCTION: Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic CC death domain and hence is not capable of inducing apoptosis. May CC protect cells against TRAIL mediated apoptosis by competing with TRAIL- CC R1 and R2 for binding to the ligand. CC -!- INTERACTION: CC O14798; Q13520: AQP6; NbExp=3; IntAct=EBI-717441, EBI-13059134; CC O14798; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-717441, EBI-11343438; CC O14798; Q8WWH4: ASZ1; NbExp=3; IntAct=EBI-717441, EBI-12239061; CC O14798; P11912: CD79A; NbExp=3; IntAct=EBI-717441, EBI-7797864; CC O14798; O75208: COQ9; NbExp=3; IntAct=EBI-717441, EBI-724524; CC O14798; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-717441, EBI-6942903; CC O14798; P00387: CYB5R3; NbExp=3; IntAct=EBI-717441, EBI-1046040; CC O14798; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-717441, EBI-296550; CC O14798; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-717441, EBI-781551; CC O14798; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-717441, EBI-18304435; CC O14798; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-717441, EBI-13345167; CC O14798; O60883: GPR37L1; NbExp=3; IntAct=EBI-717441, EBI-2927498; CC O14798; P48051: KCNJ6; NbExp=3; IntAct=EBI-717441, EBI-12017638; CC O14798; O95279: KCNK5; NbExp=3; IntAct=EBI-717441, EBI-3934936; CC O14798; P10620: MGST1; NbExp=3; IntAct=EBI-717441, EBI-2691601; CC O14798; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-717441, EBI-750085; CC O14798; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-717441, EBI-716063; CC O14798; O43765: SGTA; NbExp=3; IntAct=EBI-717441, EBI-347996; CC O14798; O14863: SLC30A4; NbExp=3; IntAct=EBI-717441, EBI-13918058; CC O14798; P27105: STOM; NbExp=3; IntAct=EBI-717441, EBI-1211440; CC O14798; Q96A49: SYAP1; NbExp=3; IntAct=EBI-717441, EBI-10770179; CC O14798; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-717441, EBI-3923061; CC O14798; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-717441, EBI-11742770; CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. CC -!- TISSUE SPECIFICITY: Higher expression in normal tissues than in tumor CC cell lines. Highly expressed in peripheral blood lymphocytes, spleen, CC skeletal muscle, placenta, lung and heart. CC -!- PTM: N-glycosylated and O-glycosylated. CC -!- SEQUENCE CAUTION: CC Sequence=AAB71413.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAC05593.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAQ88648.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF020502; AAB71413.1; ALT_INIT; mRNA. DR EMBL; AF014794; AAC05593.1; ALT_INIT; mRNA. DR EMBL; AF012629; AAB67110.1; -; mRNA. DR EMBL; AF012536; AAB67104.1; -; mRNA. DR EMBL; AF016267; AAB81181.1; -; mRNA. DR EMBL; AF033854; AAB87506.1; -; mRNA. DR EMBL; AY358281; AAQ88648.1; ALT_INIT; mRNA. DR EMBL; CR541857; CAG46655.1; -; mRNA. DR EMBL; AC107959; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC125041; AAI25042.1; -; mRNA. DR EMBL; BC125042; AAI25043.1; -; mRNA. DR CCDS; CCDS6037.1; -. DR RefSeq; NP_003832.2; NM_003841.4. DR AlphaFoldDB; O14798; -. DR SMR; O14798; -. DR BioGRID; 114322; 101. DR DIP; DIP-6242N; -. DR IntAct; O14798; 31. DR STRING; 9606.ENSP00000349324; -. DR GlyCosmos; O14798; 4 sites, 1 glycan. DR GlyGen; O14798; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; O14798; -. DR PhosphoSitePlus; O14798; -. DR BioMuta; TNFRSF10C; -. DR MassIVE; O14798; -. DR PaxDb; 9606-ENSP00000349324; -. DR PeptideAtlas; O14798; -. DR ProteomicsDB; 48247; -. DR Antibodypedia; 9707; 739 antibodies from 39 providers. DR DNASU; 8794; -. DR Ensembl; ENST00000356864.4; ENSP00000349324.4; ENSG00000173535.15. DR GeneID; 8794; -. DR KEGG; hsa:8794; -. DR MANE-Select; ENST00000356864.4; ENSP00000349324.4; NM_003841.5; NP_003832.3. DR UCSC; uc003xcy.4; human. DR AGR; HGNC:11906; -. DR CTD; 8794; -. DR DisGeNET; 8794; -. DR GeneCards; TNFRSF10C; -. DR HGNC; HGNC:11906; TNFRSF10C. DR HPA; ENSG00000173535; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 603613; gene. DR neXtProt; NX_O14798; -. DR OpenTargets; ENSG00000173535; -. DR PharmGKB; PA36599; -. DR VEuPathDB; HostDB:ENSG00000173535; -. DR eggNOG; ENOG502RBEC; Eukaryota. DR GeneTree; ENSGT00940000165140; -. DR HOGENOM; CLU_930534_0_0_1; -. DR InParanoid; O14798; -. DR OMA; QVSNCTS; -. DR OrthoDB; 4604019at2759; -. DR PhylomeDB; O14798; -. DR TreeFam; TF333916; -. DR PathwayCommons; O14798; -. DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands. DR SignaLink; O14798; -. DR SIGNOR; O14798; -. DR BioGRID-ORCS; 8794; 11 hits in 1149 CRISPR screens. DR ChiTaRS; TNFRSF10C; human. DR GeneWiki; TNFRSF10C; -. DR GenomeRNAi; 8794; -. DR Pharos; O14798; Tbio. DR PRO; PR:O14798; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; O14798; Protein. DR Bgee; ENSG00000173535; Expressed in blood and 126 other cell types or tissues. DR ExpressionAtlas; O14798; baseline and differential. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0045569; F:TRAIL binding; IEA:InterPro. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc. DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central. DR CDD; cd10580; TNFRSF10; 1. DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR InterPro; IPR020465; TNFR_10. DR InterPro; IPR034024; TNFRSF10_N. DR PANTHER; PTHR46330; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 10B; 1. DR PANTHER; PTHR46330:SF13; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 10C; 1. DR Pfam; PF00020; TNFR_c6; 2. DR PRINTS; PR01956; TNFACTORR10. DR SMART; SM00208; TNFR; 2. DR SUPFAM; SSF57586; TNF receptor-like; 3. DR PROSITE; PS00652; TNFR_NGFR_1; 2. DR PROSITE; PS50050; TNFR_NGFR_2; 2. DR Genevisible; O14798; HS. PE 1: Evidence at protein level; KW Apoptosis; Cell membrane; Direct protein sequencing; Disulfide bond; KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Receptor; KW Reference proteome; Repeat; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:9242611" FT CHAIN 26..236 FT /note="Tumor necrosis factor receptor superfamily member FT 10C" FT /id="PRO_0000034582" FT PROPEP 237..259 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000034583" FT REPEAT 29..66 FT /note="TNFR-Cys 1" FT REPEAT 69..109 FT /note="TNFR-Cys 2" FT REPEAT 110..149 FT /note="TNFR-Cys 3" FT REPEAT 162..176 FT /note="TAPE 1" FT REPEAT 177..191 FT /note="TAPE 2" FT REPEAT 192..206 FT /note="TAPE 3" FT REPEAT 207..221 FT /note="TAPE 4" FT REPEAT 222..236 FT /note="TAPE 5" FT REGION 30..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 160..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 30..45 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..221 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 236 FT /note="GPI-anchor amidated alanine" FT /evidence="ECO:0000255" FT CARBOHYD 77 FT /note="N-linked (GlcNAc...) (high mannose) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) (high mannose) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 156 FT /note="N-linked (GlcNAc...) (high mannose) asparagine" FT /evidence="ECO:0000255" FT DISULFID 53..66 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 69..85 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 88..101 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 91..109 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 111..125 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 128..141 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 131..149 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT VARIANT 199 FT /note="T -> N (in dbSNP:rs12550828)" FT /id="VAR_046534" FT VARIANT 229 FT /note="I -> T (in dbSNP:rs9644063)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9242610, FT ECO:0000269|PubMed:9242611, ECO:0000269|PubMed:9314565, FT ECO:0000269|PubMed:9325248, ECO:0000269|PubMed:9373179, FT ECO:0000269|PubMed:9551946" FT /id="VAR_046535" FT CONFLICT 119 FT /note="E -> V (in Ref. 5; AAB81181)" FT /evidence="ECO:0000305" SQ SEQUENCE 259 AA; 27407 MW; 40CBF7FCEEAE4C69 CRC64; MARIPKTLKF VVVIVAVLLP VLAYSATTAR QEEVPQQTVA PQQQRHSFKG EECPAGSHRS EHTGACNPCT EGVDYTNASN NEPSCFPCTV CKSDQKHKSS CTMTRDTVCQ CKEGTFRNEN SPEMCRKCSR CPSGEVQVSN CTSWDDIQCV EEFGANATVE TPAAEETMNT SPGTPAPAAE ETMNTSPGTP APAAEETMTT SPGTPAPAAE ETMTTSPGTP APAAEETMIT SPGTPASSHY LSCTIVGIIV LIVLLIVFV //