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 13-FEB-2019, entry version 159. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT emerging 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 RT for TRAIL."; RL Science 277:815-818(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND RP VARIANT 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., RA 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 RT ligand): a new receptor protecting lymphocytes from the death ligand RT 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., 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 [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., 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 [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 RT project: 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 RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). CC -!- FUNCTION: Receptor for the cytotoxic ligand TRAIL. Lacks a CC cytoplasmic death domain and hence is not capable of inducing CC apoptosis. May protect cells against TRAIL mediated apoptosis by CC competing with TRAIL-R1 and R2 for binding to the ligand. CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. CC -!- TISSUE SPECIFICITY: Higher expression in normal tissues than in CC tumor cell lines. Highly expressed in peripheral blood CC lymphocytes, spleen, skeletal muscle, placenta, lung and heart. CC -!- PTM: N-glycosylated and O-glycosylated. CC -!- SEQUENCE CAUTION: CC Sequence=AAB71413.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=AAC05593.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=AAQ88648.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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 UniGene; Hs.655801; -. DR ProteinModelPortal; O14798; -. DR SMR; O14798; -. DR BioGrid; 114322; 63. DR DIP; DIP-6242N; -. DR IntAct; O14798; 31. DR STRING; 9606.ENSP00000349324; -. DR iPTMnet; O14798; -. DR PhosphoSitePlus; O14798; -. DR BioMuta; TNFRSF10C; -. DR jPOST; O14798; -. DR PaxDb; O14798; -. DR PeptideAtlas; O14798; -. DR PRIDE; O14798; -. DR ProteomicsDB; 48247; -. DR Ensembl; ENST00000356864; ENSP00000349324; ENSG00000173535. DR GeneID; 8794; -. DR KEGG; hsa:8794; -. DR UCSC; uc003xcy.4; human. DR CTD; 8794; -. DR DisGeNET; 8794; -. DR EuPathDB; HostDB:ENSG00000173535.13; -. DR GeneCards; TNFRSF10C; -. DR HGNC; HGNC:11906; TNFRSF10C. DR HPA; CAB025635; -. DR MIM; 603613; gene. DR neXtProt; NX_O14798; -. DR OpenTargets; ENSG00000173535; -. DR PharmGKB; PA36599; -. DR eggNOG; ENOG410JFKD; Eukaryota. DR eggNOG; ENOG410Y7QF; LUCA. DR GeneTree; ENSGT00940000165140; -. DR HOVERGEN; HBG061470; -. DR InParanoid; O14798; -. DR KO; K22701; -. DR OMA; HYLSCTI; -. DR OrthoDB; 1448442at2759; -. DR PhylomeDB; O14798; -. DR TreeFam; TF333916; -. DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands. DR SIGNOR; O14798; -. DR ChiTaRS; TNFRSF10C; human. DR GeneWiki; TNFRSF10C; -. DR GenomeRNAi; 8794; -. DR PRO; PR:O14798; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000173535; Expressed in 197 organ(s), highest expression level in blood. DR ExpressionAtlas; O14798; baseline and differential. DR Genevisible; O14798; HS. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. 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:0042981; P:regulation of apoptotic process; TAS:Reactome. DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central. DR CDD; cd10580; TNFRSF10; 1. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR InterPro; IPR020465; TNFR_10. DR InterPro; IPR034024; TNFRSF10_N. DR Pfam; PF00020; TNFR_c6; 2. DR PRINTS; PR01956; TNFACTORR10. DR SMART; SM00208; TNFR; 2. DR PROSITE; PS00652; TNFR_NGFR_1; 2. DR PROSITE; PS50050; TNFR_NGFR_2; 2. PE 1: Evidence at protein level; KW Apoptosis; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor; KW Lipoprotein; Membrane; Polymorphism; Receptor; Reference proteome; KW Repeat; Signal. FT SIGNAL 1 25 {ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:9242611}. FT CHAIN 26 236 Tumor necrosis factor receptor FT superfamily member 10C. FT /FTId=PRO_0000034582. FT PROPEP 237 259 Removed in mature form. {ECO:0000255}. FT /FTId=PRO_0000034583. FT REPEAT 29 66 TNFR-Cys 1. FT REPEAT 69 109 TNFR-Cys 2. FT REPEAT 110 149 TNFR-Cys 3. FT REPEAT 162 176 TAPE 1. FT REPEAT 177 191 TAPE 2. FT REPEAT 192 206 TAPE 3. FT REPEAT 207 221 TAPE 4. FT REPEAT 222 236 TAPE 5. FT LIPID 236 236 GPI-anchor amidated alanine. FT {ECO:0000255}. FT CARBOHYD 77 77 N-linked (GlcNAc...) (high mannose) FT asparagine. {ECO:0000255}. FT CARBOHYD 140 140 N-linked (GlcNAc...) (high mannose) FT asparagine. {ECO:0000255}. FT CARBOHYD 156 156 N-linked (GlcNAc...) (high mannose) FT asparagine. {ECO:0000255}. FT DISULFID 53 66 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT DISULFID 69 85 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT DISULFID 88 101 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT DISULFID 91 109 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT DISULFID 111 125 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT DISULFID 128 141 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT DISULFID 131 149 {ECO:0000255|PROSITE-ProRule:PRU00206}. FT VARIANT 199 199 T -> N (in dbSNP:rs12550828). FT /FTId=VAR_046534. FT VARIANT 229 229 I -> T (in dbSNP:rs9644063). FT {ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9242610, FT ECO:0000269|PubMed:9242611, FT ECO:0000269|PubMed:9314565, FT ECO:0000269|PubMed:9325248, FT ECO:0000269|PubMed:9373179, FT ECO:0000269|PubMed:9551946}. FT /FTId=VAR_046535. FT CONFLICT 119 119 E -> V (in Ref. 5; AAB81181). FT {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 //