TR10A_HUMAN
ID TR10A_HUMAN Reviewed; 468 AA.
AC O00220; A8K5I4; Q53Y72; Q96E62;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 10A;
DE AltName: Full=Death receptor 4;
DE AltName: Full=TNF-related apoptosis-inducing ligand receptor 1;
DE Short=TRAIL receptor 1;
DE Short=TRAIL-R1;
DE AltName: CD_antigen=CD261;
DE Flags: Precursor;
GN Name=TNFRSF10A; Synonyms=APO2, DR4, TRAILR1;
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 VARIANTS ARG-141; THR-209 AND LYS-441.
RX PubMed=9082980; DOI=10.1126/science.276.5309.111;
RA Pan G., O'Rourke K., Chinnaiyan A.M., Gentz R., Ebner R., Ni J.,
RA Dixit V.M.;
RT "The receptor for the cytotoxic ligand TRAIL.";
RL Science 276:111-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-441.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-141; THR-209 AND
RP LYS-441.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-441.
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-441.
RC TISSUE=Ovary;
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 [7]
RP FUNCTION.
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 FADD-
RT dependent apoptosis and activate the NF-kappaB pathway.";
RL Immunity 7:821-830(1997).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP INTERACTION WITH ARAP1.
RX PubMed=18165900; DOI=10.1007/s10495-007-0171-8;
RA Simova S., Klima M., Cermak L., Sourkova V., Andera L.;
RT "Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of
RT TRAIL-R1/DR4 to the plasma membrane.";
RL Apoptosis 13:423-436(2008).
RN [10]
RP INTERACTION WITH DDX3X; GSK3B AND BIRC2.
RX PubMed=18846110; DOI=10.1038/cdd.2008.124;
RA Sun M., Song L., Li Y., Zhou T., Jope R.S.;
RT "Identification of an antiapoptotic protein complex at death receptors.";
RL Cell Death Differ. 15:1887-1900(2008).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP CYS-261; CYS-262; CYS-263; CYS-268; CYS-274 AND CYS-279.
RX PubMed=19090789; DOI=10.1042/bj20081212;
RA Rossin A., Derouet M., Abdel-Sater F., Hueber A.O.;
RT "Palmitoylation of the TRAIL receptor DR4 confers an efficient TRAIL-
RT induced cell death signalling.";
RL Biochem. J. 419:185-192(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-466, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=22240897; DOI=10.1038/cdd.2011.209;
RA Oh Y., Jeon Y.J., Hong G.S., Kim I., Woo H.N., Jung Y.K.;
RT "Regulation in the targeting of TRAIL receptor 1 to cell surface via GODZ
RT for TRAIL sensitivity in tumor cells.";
RL Cell Death Differ. 19:1196-1207(2012).
RN [14]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL141 (MICROBIAL INFECTION).
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., Ruckova E.,
RA Nomoto A., Schneider P., Hahn G., Zajonc D.M., Ware C.F., Wilkinson G.W.,
RA Benedict C.A.;
RT "Human cytomegalovirus glycoprotein UL141 targets the TRAIL death receptors
RT to thwart host innate antiviral defenses.";
RL Cell Host Microbe 13:324-335(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-52, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [17] {ECO:0007744|PDB:5CIR}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 125-232 IN COMPLEX WITH TNFSF10,
RP SUBUNIT, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=26457518; DOI=10.1107/s2053230x15016416;
RA Ramamurthy V., Yamniuk A.P., Lawrence E.J., Yong W., Schneeweis L.A.,
RA Cheng L., Murdock M., Corbett M.J., Doyle M.L., Sheriff S.;
RT "The structure of the death receptor 4-TNF-related apoptosis-inducing
RT ligand (DR4-TRAIL) complex.";
RL Acta Crystallogr. F 71:1273-1281(2015).
CC -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL
CC (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to the
CC activated receptor. The resulting death-inducing signaling complex
CC (DISC) performs caspase-8 proteolytic activation which initiates the
CC subsequent cascade of caspases (aspartate-specific cysteine proteases)
CC mediating apoptosis (PubMed:19090789). Promotes the activation of NF-
CC kappa-B (PubMed:9430227). {ECO:0000269|PubMed:19090789,
CC ECO:0000269|PubMed:9430227}.
CC -!- SUBUNIT: Monomer (PubMed:26457518). Homooligomers and heterooligomers
CC with TNFRSF10B (PubMed:19090789). Three TNFRSF10A molecules interact
CC with the TNFSF10 homotrimer (PubMed:26457518). Can interact with TRADD
CC and RIPK1. Interacts with ARAP1. In the absence of stimulation,
CC interacts with BIRC2, DDX3X and GSK3B. The interaction with BIRC2 and
CC DDX3X is further enhanced upon receptor stimulation and accompanied by
CC DDX3X and BIRC2 cleavage (PubMed:18846110). Interacts with ZDHHC3
CC (PubMed:22240897). {ECO:0000269|PubMed:18165900,
CC ECO:0000269|PubMed:18846110, ECO:0000269|PubMed:19090789,
CC ECO:0000269|PubMed:22240897, ECO:0000269|PubMed:26457518}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCMV protein UL141; this
CC interaction prevents TNFRSF10A cell surface expression.
CC {ECO:0000269|PubMed:23498957}.
CC -!- INTERACTION:
CC O00220; Q96P48: ARAP1; NbExp=4; IntAct=EBI-518861, EBI-710003;
CC O00220; Q14790: CASP8; NbExp=9; IntAct=EBI-518861, EBI-78060;
CC O00220; Q08380: LGALS3BP; NbExp=2; IntAct=EBI-518861, EBI-354956;
CC O00220; P50591: TNFSF10; NbExp=4; IntAct=EBI-518861, EBI-495373;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22240897};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000269|PubMed:19090789, ECO:0000269|PubMed:22240897}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:22240897}. Note=Palmitoylation is required
CC for association with membranes. {ECO:0000269|PubMed:22240897}.
CC -!- TISSUE SPECIFICITY: Widely expressed. High levels are found in spleen,
CC peripheral blood leukocytes, small intestine and thymus, but also in K-
CC 562 erythroleukemia cells, MCF-7 breast carcinoma cells and activated
CC T-cells.
CC -!- PTM: Palmitoylated (PubMed:19090789). Palmitoylation of TNFRSF10A is
CC required for its association with lipid rafts, oligomerization and
CC function in TRAIL-induced cell death (PubMed:19090789). Palmitoylated
CC by ZDHHC3 (Probable). {ECO:0000269|PubMed:19090789,
CC ECO:0000305|PubMed:22240897}.
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DR EMBL; U90875; AAC51226.1; -; mRNA.
DR EMBL; BT006906; AAP35552.1; -; mRNA.
DR EMBL; AK291299; BAF83988.1; -; mRNA.
DR EMBL; EF064713; ABK41896.1; -; Genomic_DNA.
DR EMBL; AC100861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012866; AAH12866.1; -; mRNA.
DR CCDS; CCDS6039.1; -.
DR RefSeq; NP_003835.3; NM_003844.3.
DR PDB; 5CIR; X-ray; 3.00 A; E/F/G=125-232.
DR PDBsum; 5CIR; -.
DR AlphaFoldDB; O00220; -.
DR SMR; O00220; -.
DR BioGRID; 114325; 143.
DR IntAct; O00220; 88.
DR MINT; O00220; -.
DR STRING; 9606.ENSP00000221132; -.
DR BindingDB; O00220; -.
DR ChEMBL; CHEMBL3551; -.
DR GuidetoPHARMACOLOGY; 1879; -.
DR GlyGen; O00220; 5 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; O00220; -.
DR PhosphoSitePlus; O00220; -.
DR SwissPalm; O00220; -.
DR BioMuta; TNFRSF10A; -.
DR EPD; O00220; -.
DR jPOST; O00220; -.
DR MassIVE; O00220; -.
DR MaxQB; O00220; -.
DR PaxDb; O00220; -.
DR PeptideAtlas; O00220; -.
DR PRIDE; O00220; -.
DR ProteomicsDB; 47790; -.
DR ABCD; O00220; 12 sequenced antibodies.
DR Antibodypedia; 9727; 1167 antibodies from 50 providers.
DR DNASU; 8797; -.
DR Ensembl; ENST00000221132.8; ENSP00000221132.3; ENSG00000104689.10.
DR GeneID; 8797; -.
DR KEGG; hsa:8797; -.
DR MANE-Select; ENST00000221132.8; ENSP00000221132.3; NM_003844.4; NP_003835.3.
DR UCSC; uc003xda.4; human.
DR CTD; 8797; -.
DR DisGeNET; 8797; -.
DR GeneCards; TNFRSF10A; -.
DR HGNC; HGNC:11904; TNFRSF10A.
DR HPA; ENSG00000104689; Low tissue specificity.
DR MIM; 603611; gene.
DR neXtProt; NX_O00220; -.
DR OpenTargets; ENSG00000104689; -.
DR PharmGKB; PA36597; -.
DR VEuPathDB; HostDB:ENSG00000104689; -.
DR eggNOG; ENOG502RBEC; Eukaryota.
DR GeneTree; ENSGT00940000162957; -.
DR InParanoid; O00220; -.
DR OMA; CLPCEHG; -.
DR OrthoDB; 1448442at2759; -.
DR PhylomeDB; O00220; -.
DR TreeFam; TF333916; -.
DR PathwayCommons; O00220; -.
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; O00220; -.
DR SIGNOR; O00220; -.
DR BioGRID-ORCS; 8797; 19 hits in 1086 CRISPR screens.
DR ChiTaRS; TNFRSF10A; human.
DR GeneWiki; TNFRSF10A; -.
DR GenomeRNAi; 8797; -.
DR Pharos; O00220; Tchem.
DR PRO; PR:O00220; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O00220; protein.
DR Bgee; ENSG00000104689; Expressed in buccal mucosa cell and 174 other tissues.
DR ExpressionAtlas; O00220; baseline and differential.
DR Genevisible; O00220; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005035; F:death receptor activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0045569; F:TRAIL binding; NAS:UniProtKB.
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:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; TAS:ProtInc.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR CDD; cd08315; Death_TRAILR_DR4_DR5; 1.
DR CDD; cd10580; TNFRSF10; 1.
DR Gene3D; 1.10.533.10; -; 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; Apoptosis; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; Membrane; Methylation; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..468
FT /note="Tumor necrosis factor receptor superfamily member
FT 10A"
FT /id="PRO_0000034579"
FT TOPO_DOM 24..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 107..145
FT /note="TNFR-Cys 1"
FT REPEAT 147..188
FT /note="TNFR-Cys 2"
FT REPEAT 189..229
FT /note="TNFR-Cys 3"
FT DOMAIN 365..448
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 17..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT DISULFID 148..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT DISULFID 167..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT DISULFID 170..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT DISULFID 190..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT DISULFID 207..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT DISULFID 211..229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR"
FT VARIANT 11
FT /note="G -> V (in dbSNP:rs34737614)"
FT /id="VAR_052349"
FT VARIANT 33
FT /note="T -> I (in dbSNP:rs20577)"
FT /id="VAR_016149"
FT VARIANT 105
FT /note="P -> R (in dbSNP:rs11986840)"
FT /id="VAR_052350"
FT VARIANT 141
FT /note="H -> R (in dbSNP:rs17620)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9082980"
FT /id="VAR_016150"
FT VARIANT 209
FT /note="R -> T (in dbSNP:rs20575)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9082980"
FT /id="VAR_016151"
FT VARIANT 228
FT /note="E -> A (in dbSNP:rs20576)"
FT /id="VAR_016152"
FT VARIANT 297
FT /note="N -> H (in dbSNP:rs17088980)"
FT /id="VAR_052351"
FT VARIANT 441
FT /note="R -> K (in dbSNP:rs2230229)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9082980,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.4"
FT /id="VAR_052352"
FT MUTAGEN 261
FT /note="C->S: No effect on palmitoylation. Loss of
FT palmitoylation, decreased association with membranes,
FT decreased oligomerization, decreased death-induced
FT signaling complex assembly associated with decreased
FT function in TRAIL-induced cell death; when associated with
FT S-262 and S-263."
FT /evidence="ECO:0000269|PubMed:19090789,
FT ECO:0000269|PubMed:22240897"
FT MUTAGEN 262
FT /note="C->S: No effect on palmitoylation. Loss of
FT palmitoylation, decreased association with membranes,
FT decreased oligomerization, decreased death-induced
FT signaling complex assembly associated with decreased
FT function in TRAIL-induced cell death; when associated with
FT S-261 and S-263."
FT /evidence="ECO:0000269|PubMed:19090789"
FT MUTAGEN 263
FT /note="C->S: No effect on palmitoylation. Loss of
FT palmitoylation, decreased association with membranes,
FT decreased oligomerization, decreased death-induced
FT signaling complex assembly associated with decreased
FT function in TRAIL-induced cell death; when associated with
FT S-261 and S-262."
FT /evidence="ECO:0000269|PubMed:19090789"
FT MUTAGEN 268
FT /note="C->S: No effect on palmitoylation."
FT /evidence="ECO:0000269|PubMed:19090789"
FT MUTAGEN 274
FT /note="C->S: No effect on palmitoylation."
FT /evidence="ECO:0000269|PubMed:19090789"
FT MUTAGEN 279
FT /note="C->S: No effect on palmitoylation."
FT /evidence="ECO:0000269|PubMed:19090789"
FT CONFLICT 281
FT /note="W -> C (in Ref. 3; BAF83988)"
FT /evidence="ECO:0000305"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5CIR"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5CIR"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5CIR"
SQ SEQUENCE 468 AA; 50089 MW; 7E96619D0BDC0CD4 CRC64;
MAPPPARVHL GAFLAVTPNP GSAASGTEAA AATPSKVWGS SAGRIEPRGG GRGALPTSMG
QHGPSARARA GRAPGPRPAR EASPRLRVHK TFKFVVVGVL LQVVPSSAAT IKLHDQSIGT
QQWEHSPLGE LCPPGSHRSE HPGACNRCTE GVGYTNASNN LFACLPCTAC KSDEEERSPC
TTTRNTACQC KPGTFRNDNS AEMCRKCSRG CPRGMVKVKD CTPWSDIECV HKESGNGHNI
WVILVVTLVV PLLLVAVLIV CCCIGSGCGG DPKCMDRVCF WRLGLLRGPG AEDNAHNEIL
SNADSLSTFV SEQQMESQEP ADLTGVTVQS PGEAQCLLGP AEAEGSQRRR LLVPANGADP
TETLMLFFDK FANIVPFDSW DQLMRQLDLT KNEIDVVRAG TAGPGDALYA MLMKWVNKTG
RNASIHTLLD ALERMEERHA REKIQDLLVD SGKFIYLEDG TGSAVSLE
