TR10B_MOUSE
ID TR10B_MOUSE Reviewed; 381 AA.
AC Q9QZM4; Q6GSD9; Q9JJL5; Q9JJL6;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 10B;
DE AltName: Full=Death receptor 5;
DE AltName: Full=MK;
DE AltName: CD_antigen=CD262;
DE Flags: Precursor;
GN Name=Tnfrsf10b; Synonyms=Dr5, Killer;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=10383128;
RA Wu G.S., Burns T.F., Zhan Y., Alnemri E.S., El-Deiry W.S.;
RT "Molecular cloning and functional analysis of the mouse homologue of the
RT KILLER/DR5 tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)
RT death receptor.";
RL Cancer Res. 59:2770-2775(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Spleen;
RA Nakamura Y., Tamari M., Watanabe O.;
RT "Mouse TRAIL receptor.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Embryo, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [5]
RP GLYCOSYLATION AT ARG-293 (MICROBIAL INFECTION).
RX PubMed=30902834; DOI=10.1074/mcp.ra118.001093;
RA Newson J.P.M., Scott N.E., Yeuk Wah Chung I., Wong Fok Lung T., Giogha C.,
RA Gan J., Wang N., Strugnell R.A., Brown N.F., Cygler M., Pearson J.S.,
RA Hartland E.L.;
RT "Salmonella effectors SseK1 and SseK3 target death domain proteins in the
RT TNF and TRAIL signaling pathways.";
RL Mol. Cell. Proteomics 18:1138-1156(2019).
CC -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter
CC molecule FADD recruits caspase-8 to the activated receptor. The
CC resulting death-inducing signaling complex (DISC) performs caspase-8
CC proteolytic activation which initiates the subsequent cascade of
CC caspases (aspartate-specific cysteine proteases) mediating apoptosis.
CC Promotes the activation of NF-kappa-B. Essential for ER stress-induced
CC apoptosis. {ECO:0000250|UniProtKB:O14763}.
CC -!- SUBUNIT: Monomer. Can interact with TRADD and RIPK1. Three TNFRSF10B
CC molecules interact with the TNFSF10 homotrimer. In the absence of
CC stimulation, interacts with BIRC2, DDX3X and GSK3B. The interaction
CC with BIRC2 and DDX3X is further enhanced upon receptor stimulation and
CC accompanied by DDX3X and BIRC2 cleavage (By similarity).
CC {ECO:0000250|UniProtKB:O14763}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, lung and kidney.
CC -!- INDUCTION: TNFRSF10B is regulated by the tumor suppressor p53.
CC -!- PTM: (Microbial infection) Glycosylated at Arg-293 by S.typhimurium
CC protein Ssek3. {ECO:0000269|PubMed:30902834}.
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DR EMBL; AF176833; AAD52656.1; -; mRNA.
DR EMBL; AB031081; BAA96462.1; -; mRNA.
DR EMBL; AB031082; BAA96463.1; -; Genomic_DNA.
DR EMBL; AK050753; BAC34404.1; -; mRNA.
DR EMBL; AK080069; BAC37821.1; -; mRNA.
DR EMBL; AK154993; BAE32980.1; -; mRNA.
DR EMBL; BC065141; AAH65141.1; -; mRNA.
DR CCDS; CCDS27243.1; -.
DR RefSeq; NP_064671.2; NM_020275.4.
DR AlphaFoldDB; Q9QZM4; -.
DR SMR; Q9QZM4; -.
DR IntAct; Q9QZM4; 1.
DR STRING; 10090.ENSMUSP00000022663; -.
DR iPTMnet; Q9QZM4; -.
DR PhosphoSitePlus; Q9QZM4; -.
DR EPD; Q9QZM4; -.
DR MaxQB; Q9QZM4; -.
DR PaxDb; Q9QZM4; -.
DR PeptideAtlas; Q9QZM4; -.
DR PRIDE; Q9QZM4; -.
DR ProteomicsDB; 259297; -.
DR DNASU; 21933; -.
DR Ensembl; ENSMUST00000022663; ENSMUSP00000022663; ENSMUSG00000022074.
DR GeneID; 21933; -.
DR KEGG; mmu:21933; -.
DR UCSC; uc007umu.2; mouse.
DR CTD; 8795; -.
DR MGI; MGI:1341090; Tnfrsf10b.
DR VEuPathDB; HostDB:ENSMUSG00000022074; -.
DR eggNOG; ENOG502RBEC; Eukaryota.
DR GeneTree; ENSGT00940000162427; -.
DR HOGENOM; CLU_038161_1_0_1; -.
DR InParanoid; Q9QZM4; -.
DR OMA; CLPCEHG; -.
DR OrthoDB; 1448442at2759; -.
DR PhylomeDB; Q9QZM4; -.
DR TreeFam; TF333916; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-3371378; Regulation by c-FLIP.
DR Reactome; R-MMU-5218900; CASP8 activity is inhibited.
DR Reactome; R-MMU-69416; Dimerization of procaspase-8.
DR Reactome; R-MMU-75158; TRAIL signaling.
DR BioGRID-ORCS; 21933; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Tnfrsf10b; mouse.
DR PRO; PR:Q9QZM4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QZM4; protein.
DR Bgee; ENSMUSG00000022074; Expressed in kidney vasculature and 74 other tissues.
DR Genevisible; Q9QZM4; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0045569; F:TRAIL binding; IEA:InterPro.
DR GO; GO:0036463; F:TRAIL receptor activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:GOC.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central.
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 Apoptosis; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..381
FT /note="Tumor necrosis factor receptor superfamily member
FT 10B"
FT /id="PRO_0000034581"
FT TOPO_DOM 53..180
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 26..86
FT /note="TNFR-Cys 1"
FT REPEAT 87..129
FT /note="TNFR-Cys 2"
FT REPEAT 130..169
FT /note="TNFR-Cys 3"
FT DOMAIN 273..356
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 228..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 293
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000269|PubMed:30902834"
FT DISULFID 74..85
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 88..105
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 108..121
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 111..129
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 131..145
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 148..161
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 151..169
FT /evidence="ECO:0000250|UniProtKB:O14763,
FT ECO:0000255|PROSITE-ProRule:PRU00206"
FT CONFLICT 42
FT /note="V -> M (in Ref. 2; BAA96462/BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="H -> R (in Ref. 2; BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> E (in Ref. 2; BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="K -> N (in Ref. 2; BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="L -> AT (in Ref. 2; BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="R -> RAYP (in Ref. 2; BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="S -> L (in Ref. 2; BAA96462/BAA96463)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="K -> R (in Ref. 2; BAA96463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42165 MW; 222531758F4ADE0A CRC64;
MEPPGPSTPT ASAAARADHY TPGLRPLPKR RLLYSFALLL AVLQAVFVPV TANPAHNRPA
GLQRPEESPS RGPCLAGQYL SEGNCKPCRE GIDYTSHSNH SLDSCILCTV CKEDKVVETR
CNITTNTVCR CKPGTFEDKD SPEICQSCSN CTDGEEELTS CTPRENRKCV SKTAWASWHK
LGLWIGLLVP VVLLIGALLV WKTGAWRQWL LCIKRGCERD PESANSVHSS LLDRQTSSTT
NDSNHNTEPG KTQKTGKKLL VPVNGNDSAD DLKFIFEYCS DIVPFDSWNR LMRQLGLTDN
QIQMVKAETL VTREALYQML LKWRHQTGRS ASINHLLDAL EAVEERDAME KIEDYAVKSG
RFTYQNAAAQ PETGPGGSQC V
