TNR21_HUMAN
ID TNR21_HUMAN Reviewed; 655 AA.
AC O75509; B2RDI9; Q0D2P5; Q96D86;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 21;
DE AltName: Full=Death receptor 6;
DE AltName: CD_antigen=CD358;
DE Flags: Precursor;
GN Name=TNFRSF21; Synonyms=DR6; ORFNames=UNQ437/PRO868;
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH TRADD.
RX PubMed=9714541; DOI=10.1016/s0014-5793(98)00791-1;
RA Pan G., Bauer J.H., Haridas V., Wang S., Liu D., Yu G., Vincenz C.,
RA Aggarwal B.B., Ni J., Dixit V.M.;
RT "Identification and functional characterization of DR6, a novel death
RT domain-containing TNF receptor.";
RL FEBS Lett. 431:351-356(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, and Eye;
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 SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-82; ASN-141; ASN-252; ASN-257;
RP ASN-278 AND ASN-289, MUTAGENESIS OF ASN-82; ASN-141; ASN-252; ASN-257;
RP ASN-278 AND ASN-289, INDUCTION BY TNF, AND PALMITOYLATION AT CYS-368.
RX PubMed=19654028; DOI=10.1016/j.bbamcr.2009.07.008;
RA Klima M., Zajedova J., Doubravska L., Andera L.;
RT "Functional analysis of the posttranslational modifications of the death
RT receptor 6.";
RL Biochim. Biophys. Acta 1793:1579-1587(2009).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21725297; DOI=10.1038/nm.2373;
RA Mi S., Lee X., Hu Y., Ji B., Shao Z., Yang W., Huang G., Walus L.,
RA Rhodes K., Gong B.J., Miller R.H., Pepinsky R.B.;
RT "Death receptor 6 negatively regulates oligodendrocyte survival, maturation
RT and myelination.";
RL Nat. Med. 17:816-821(2011).
RN [9]
RP FUNCTION.
RX PubMed=22761420; DOI=10.1074/jbc.m112.362038;
RA Zeng L., Li T., Xu D.C., Liu J., Mao G., Cui M.Z., Fu X., Xu X.;
RT "Death receptor 6 induces apoptosis not through type I or type II pathways,
RT but via a unique mitochondria-dependent pathway by interacting with Bax
RT protein.";
RL J. Biol. Chem. 287:29125-29133(2012).
RN [10]
RP INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH NGFR.
RX PubMed=23559013; DOI=10.1038/cddis.2013.110;
RA Hu Y., Lee X., Shao Z., Apicco D., Huang G., Gong B.J., Pepinsky R.B.,
RA Mi S.;
RT "A DR6/p75(NTR) complex is responsible for beta-amyloid-induced cortical
RT neuron death.";
RL Cell Death Dis. 4:E579-E579(2013).
RN [11]
RP INTERACTION WITH HCV NON-STRUCTURAL PROTEIN 5A (MICROBIAL INFECTION).
RX PubMed=28743875; DOI=10.1038/s41598-017-06740-9;
RA Luong T.T.D., Tran G.V.Q., Shin D.J., Lim Y.S., Hwang S.B.;
RT "Hepatitis C Virus Exploits Death Receptor 6-mediated Signaling Pathway to
RT Facilitate Viral Propagation.";
RL Sci. Rep. 7:6445-6445(2017).
RN [12]
RP STRUCTURE BY NMR OF 562-655.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the carboxyl-terminal CARD-like domain in human
RT TNFR-related death receptor-6.";
RL Submitted (DEC-2006) to the PDB data bank.
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 42-218, AND DISULFIDE BOND.
RX PubMed=21463639; DOI=10.1016/j.jmb.2011.03.048;
RA Kuester M., Kemmerzehl S., Dahms S.O., Roeser D., Than M.E.;
RT "The crystal structure of death receptor 6 (DR6): a potential receptor of
RT the amyloid precursor protein (APP).";
RL J. Mol. Biol. 409:189-201(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 42-349, DISULFIDE BOND, AND
RP GLYCOSYLATION.
RX PubMed=22525750; DOI=10.1107/s0907444912004490;
RA Ru H., Zhao L., Ding W., Jiao L., Shaw N., Liang W., Zhang L., Hung L.W.,
RA Matsugaki N., Wakatsuki S., Liu Z.J.;
RT "S-SAD phasing study of death receptor 6 and its solution conformation
RT revealed by SAXS.";
RL Acta Crystallogr. D 68:521-530(2012).
CC -!- FUNCTION: Promotes apoptosis, possibly via a pathway that involves the
CC activation of NF-kappa-B. Can also promote apoptosis mediated by BAX
CC and by the release of cytochrome c from the mitochondria into the
CC cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in
CC response to amyloid peptides derived from APP, and is required for both
CC normal cell body death and axonal pruning. Trophic-factor deprivation
CC triggers the cleavage of surface APP by beta-secretase to release sAPP-
CC beta which is further cleaved to release an N-terminal fragment of APP
CC (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and
CC degeneration of both neuronal cell bodies (via caspase-3) and axons
CC (via caspase-6). Negatively regulates oligodendrocyte survival,
CC maturation and myelination. Plays a role in signaling cascades
CC triggered by stimulation of T-cell receptors, in the adaptive immune
CC response and in the regulation of T-cell differentiation and
CC proliferation. Negatively regulates T-cell responses and the release of
CC cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells.
CC Negatively regulates the production of IgG, IgM and IgM in response to
CC antigens. May inhibit the activation of JNK in response to T-cell
CC stimulation. {ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:22761420,
CC ECO:0000269|PubMed:9714541}.
CC -!- SUBUNIT: Interacts with N-APP (By similarity). Associates with TRADD.
CC Interacts with NGFR. {ECO:0000250, ECO:0000269|PubMed:23559013,
CC ECO:0000269|PubMed:9714541}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus (HCV)
CC non-structural protein 5A; this interaction allows the modulation by
CC the virus of JNK, p38 MAPK, STAT3, and Akt signaling pathways in a DR6-
CC dependent manner. {ECO:0000269|PubMed:28743875}.
CC -!- INTERACTION:
CC O75509; P08138: NGFR; NbExp=4; IntAct=EBI-2313231, EBI-1387782;
CC O75509; O43765: SGTA; NbExp=3; IntAct=EBI-2313231, EBI-347996;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19654028};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:19654028}.
CC -!- TISSUE SPECIFICITY: Detected in fetal spinal cord and in brain neurons,
CC with higher levels in brain from Alzheimer disease patients (at protein
CC level). Highly expressed in heart, brain, placenta, pancreas, lymph
CC node, thymus and prostate. Detected at lower levels in lung, skeletal
CC muscle, kidney, testis, uterus, small intestine, colon, spleen, bone
CC marrow and fetal liver. Very low levels were found in adult liver and
CC peripheral blood leukocytes. {ECO:0000269|PubMed:21725297,
CC ECO:0000269|PubMed:23559013, ECO:0000269|PubMed:9714541}.
CC -!- INDUCTION: Up-regulated by TNF. {ECO:0000269|PubMed:19654028,
CC ECO:0000269|PubMed:23559013}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10241.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF068868; AAC34583.1; -; mRNA.
DR EMBL; AY358304; AAQ88671.1; -; mRNA.
DR EMBL; AK315560; BAG37936.1; -; mRNA.
DR EMBL; BT007420; AAP36088.1; -; mRNA.
DR EMBL; AL096801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010241; AAH10241.1; ALT_INIT; mRNA.
DR EMBL; BC017730; AAH17730.1; -; mRNA.
DR EMBL; BC021572; AAH21572.1; -; mRNA.
DR CCDS; CCDS4921.1; -.
DR RefSeq; NP_055267.1; NM_014452.4.
DR PDB; 2DBH; NMR; -; A=567-655.
DR PDB; 3QO4; X-ray; 2.20 A; A=42-218.
DR PDB; 3U3P; X-ray; 2.09 A; A=42-348.
DR PDB; 3U3Q; X-ray; 2.70 A; A=42-348.
DR PDB; 3U3S; X-ray; 2.70 A; A=42-348.
DR PDB; 3U3T; X-ray; 3.21 A; A=42-348.
DR PDB; 3U3V; X-ray; 2.96 A; A=42-348.
DR PDBsum; 2DBH; -.
DR PDBsum; 3QO4; -.
DR PDBsum; 3U3P; -.
DR PDBsum; 3U3Q; -.
DR PDBsum; 3U3S; -.
DR PDBsum; 3U3T; -.
DR PDBsum; 3U3V; -.
DR AlphaFoldDB; O75509; -.
DR SMR; O75509; -.
DR BioGRID; 118090; 23.
DR CORUM; O75509; -.
DR DIP; DIP-53299N; -.
DR IntAct; O75509; 14.
DR MINT; O75509; -.
DR STRING; 9606.ENSP00000296861; -.
DR GlyConnect; 1981; 6 N-Linked glycans (5 sites).
DR GlyGen; O75509; 9 sites, 6 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; O75509; -.
DR PhosphoSitePlus; O75509; -.
DR SwissPalm; O75509; -.
DR BioMuta; TNFRSF21; -.
DR EPD; O75509; -.
DR jPOST; O75509; -.
DR MassIVE; O75509; -.
DR MaxQB; O75509; -.
DR PaxDb; O75509; -.
DR PeptideAtlas; O75509; -.
DR PRIDE; O75509; -.
DR ProteomicsDB; 50058; -.
DR Antibodypedia; 1463; 647 antibodies from 41 providers.
DR DNASU; 27242; -.
DR Ensembl; ENST00000296861.2; ENSP00000296861.2; ENSG00000146072.6.
DR GeneID; 27242; -.
DR KEGG; hsa:27242; -.
DR MANE-Select; ENST00000296861.2; ENSP00000296861.2; NM_014452.5; NP_055267.1.
DR UCSC; uc003oyv.5; human.
DR CTD; 27242; -.
DR DisGeNET; 27242; -.
DR GeneCards; TNFRSF21; -.
DR HGNC; HGNC:13469; TNFRSF21.
DR HPA; ENSG00000146072; Tissue enhanced (brain, urinary bladder).
DR MIM; 605732; gene.
DR neXtProt; NX_O75509; -.
DR OpenTargets; ENSG00000146072; -.
DR PharmGKB; PA37775; -.
DR VEuPathDB; HostDB:ENSG00000146072; -.
DR eggNOG; ENOG502QVMX; Eukaryota.
DR GeneTree; ENSGT00940000156212; -.
DR HOGENOM; CLU_027496_0_0_1; -.
DR InParanoid; O75509; -.
DR OMA; THQQGPH; -.
DR OrthoDB; 869160at2759; -.
DR PhylomeDB; O75509; -.
DR TreeFam; TF331157; -.
DR PathwayCommons; O75509; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR SignaLink; O75509; -.
DR SIGNOR; O75509; -.
DR BioGRID-ORCS; 27242; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; TNFRSF21; human.
DR EvolutionaryTrace; O75509; -.
DR GeneWiki; TNFRSF21; -.
DR GenomeRNAi; 27242; -.
DR Pharos; O75509; Tbio.
DR PRO; PR:O75509; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O75509; protein.
DR Bgee; ENSG00000146072; Expressed in islet of Langerhans and 196 other tissues.
DR ExpressionAtlas; O75509; baseline and differential.
DR Genevisible; O75509; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002250; P:adaptive immune response; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR GO; GO:0001783; P:B cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0006959; P:humoral immune response; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISS:UniProtKB.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISS:UniProtKB.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; ISS:UniProtKB.
DR GO; GO:0032714; P:negative regulation of interleukin-5 production; ISS:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd08778; Death_TNFRSF21; 1.
DR CDD; cd10583; TNFRSF21; 1.
DR Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022330; TNFR_21.
DR InterPro; IPR034037; TNFRSF21_death.
DR InterPro; IPR034034; TNFRSF21_N.
DR PANTHER; PTHR46921; PTHR46921; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 3.
DR PRINTS; PR01971; TNFACTORR21.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 4.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Apoptosis; Cell membrane; Disulfide bond;
KW Glycoprotein; Host-virus interaction; Immunity; Lipoprotein; Membrane;
KW Palmitate; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..655
FT /note="Tumor necrosis factor receptor superfamily member
FT 21"
FT /id="PRO_0000034602"
FT TOPO_DOM 42..349
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 50..88
FT /note="TNFR-Cys 1"
FT REPEAT 90..131
FT /note="TNFR-Cys 2"
FT REPEAT 133..167
FT /note="TNFR-Cys 3"
FT REPEAT 170..211
FT /note="TNFR-Cys 4"
FT DOMAIN 415..498
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 243..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 368
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19654028"
FT DISULFID 67..80
FT DISULFID 70..88
FT DISULFID 91..106
FT DISULFID 109..123
FT DISULFID 113..131
FT DISULFID 133..144
FT DISULFID 150..168
FT DISULFID 171..186
FT DISULFID 192..211
FT MUTAGEN 82
FT /note="N->Q: Abolishes one glycosylation site and reduces
FT total N-glycosylation; when associated with Q-252; Q-278
FT and Q-289."
FT /evidence="ECO:0000269|PubMed:19654028"
FT MUTAGEN 141
FT /note="N->Q: Abolishes one glycosylation site and reduces
FT total N-glycosylation; when associated with Q-82; Q-252; Q-
FT 278 and Q-289."
FT /evidence="ECO:0000269|PubMed:19654028"
FT MUTAGEN 252
FT /note="N->Q: Abolishes one glycosylation site and reduces
FT total N-glycosylation; when associated with Q-278 and Q-
FT 289."
FT /evidence="ECO:0000269|PubMed:19654028"
FT MUTAGEN 257
FT /note="N->Q: Abolishes one glycosylation site and reduces
FT total N-glycosylation; when associated with Q-82; Q-141; Q-
FT 252; Q-278 and Q-289."
FT /evidence="ECO:0000269|PubMed:19654028"
FT MUTAGEN 278
FT /note="N->Q: Abolishes one glycosylation site and reduces
FT total N-glycosylation. Abolishes one glycosylation site and
FT reduces total N-glycosylation; when associated with Q-82;
FT Q-141; Q-252; Q-257 and Q-289."
FT /evidence="ECO:0000269|PubMed:19654028"
FT MUTAGEN 289
FT /note="N->Q: Abolishes one glycosylation site and reduces
FT total N-glycosylation; when associated with Q-278."
FT /evidence="ECO:0000269|PubMed:19654028"
FT MUTAGEN 368
FT /note="C->V: Abolishes palmitoylation."
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3U3P"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3U3T"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3U3V"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3U3P"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3U3P"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:2DBH"
FT HELIX 579..591
FT /evidence="ECO:0007829|PDB:2DBH"
FT HELIX 598..606
FT /evidence="ECO:0007829|PDB:2DBH"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:2DBH"
FT HELIX 621..635
FT /evidence="ECO:0007829|PDB:2DBH"
FT HELIX 637..650
FT /evidence="ECO:0007829|PDB:2DBH"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:2DBH"
SQ SEQUENCE 655 AA; 71845 MW; 48939391C4852A33 CRC64;
MGTSPSSSTA LASCSRIARR ATATMIAGSL LLLGFLSTTT AQPEQKASNL IGTYRHVDRA
TGQVLTCDKC PAGTYVSEHC TNTSLRVCSS CPVGTFTRHE NGIEKCHDCS QPCPWPMIEK
LPCAALTDRE CTCPPGMFQS NATCAPHTVC PVGWGVRKKG TETEDVRCKQ CARGTFSDVP
SSVMKCKAYT DCLSQNLVVI KPGTKETDNV CGTLPSFSSS TSPSPGTAIF PRPEHMETHE
VPSSTYVPKG MNSTESNSSA SVRPKVLSSI QEGTVPDNTS SARGKEDVNK TLPNLQVVNH
QQGPHHRHIL KLLPSMEATG GEKSSTPIKG PKRGHPRQNL HKHFDINEHL PWMIVLFLLL
VLVVIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSMTP TQNREKWIYY CNGHGIDILK
LVAAQVGSQW KDIYQFLCNA SEREVAAFSN GYTADHERAY AALQHWTIRG PEASLAQLIS
ALRQHRRNDV VEKIRGLMED TTQLETDKLA LPMSPSPLSP SPIPSPNAKL ENSALLTVEP
SPQDKNKGFF VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF
DDMLHFLNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH LPDLL
