TR10C_HUMAN
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 03-AUG-2022, entry version 176.
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; 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};
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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 GlyGen; O14798; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O14798; -.
DR PhosphoSitePlus; O14798; -.
DR BioMuta; TNFRSF10C; -.
DR MassIVE; O14798; -.
DR PaxDb; O14798; -.
DR PeptideAtlas; O14798; -.
DR PRIDE; O14798; -.
DR ProteomicsDB; 48247; -.
DR Antibodypedia; 9707; 701 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 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; ETMNTSP; -.
DR OrthoDB; 1448442at2759; -.
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 1071 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 125 other tissues.
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: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; 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
