TNR22_MOUSE
ID TNR22_MOUSE Reviewed; 198 AA.
AC Q9ER62; Q8VHB9; Q9CZA4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 22;
DE AltName: Full=Decoy TRAIL receptor 2;
DE AltName: Full=TNF receptor family member SOBa;
DE AltName: Full=TNF receptor homolog 2;
DE AltName: Full=Tumor necrosis factor receptor p60 homolog 2;
GN Name=Tnfrsf22; Synonyms=Dctrailr2, Tnfrh2, Tnfrsf1al2;
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 [GENOMIC DNA / MRNA] (ISOFORM 2).
RC STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RX PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
RA Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R., Lane N.,
RA Reik W., Walter J.;
RT "Sequence and functional comparison in the Beckwith-Wiedemann region:
RT implications for a novel imprinting centre and extended imprinting.";
RL Hum. Mol. Genet. 9:2691-2706(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND 3D-STRUCTURE
RP MODELING OF 62-170.
RC STRAIN=NIH Swiss;
RX PubMed=12466268; DOI=10.1074/jbc.m210783200;
RA Schneider P., Olson D., Tardivel A., Browning B., Lugovskoy A., Gong D.,
RA Dobles M., Hertig S., Hofmann K., Van Vlijmen H., Hsu Y.-M., Burkly L.C.,
RA Tschopp J., Zheng T.S.;
RT "Identification of a new murine tumor necrosis factor receptor locus that
RT contains two novel murine receptors for tumor necrosis factor-related
RT apoptosis-inducing ligand (TRAIL).";
RL J. Biol. Chem. 278:5444-5454(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RA Risser P., Mao W., Baldwin D.T., Pan G.;
RT "Characterization of SOBa, a murine member of the TNFR family.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
CC -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. Lacks a
CC cytoplasmic death domain and hence is not capable of inducing
CC apoptosis. Protects cells against TRAIL mediated apoptosis possibly
CC through ligand competition. Cannot induce the NF-kappa-B pathway.
CC {ECO:0000269|PubMed:12466268}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ER62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ER62-2; Sequence=VSP_007648;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28502.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC16406.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC27353.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ278265; CAC16406.1; ALT_FRAME; mRNA.
DR EMBL; AJ276505; CAC27353.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY165626; AAN87806.1; -; mRNA.
DR EMBL; AY165627; AAN87807.1; -; mRNA.
DR EMBL; AY046551; AAL05073.1; -; mRNA.
DR EMBL; AK012838; BAB28502.2; ALT_INIT; mRNA.
DR CCDS; CCDS22043.1; -. [Q9ER62-2]
DR CCDS; CCDS80846.1; -. [Q9ER62-1]
DR RefSeq; NP_001298074.1; NM_001311145.1. [Q9ER62-1]
DR RefSeq; NP_076169.2; NM_023680.4. [Q9ER62-2]
DR AlphaFoldDB; Q9ER62; -.
DR SMR; Q9ER62; -.
DR STRING; 10090.ENSMUSP00000075018; -.
DR GlyGen; Q9ER62; 2 sites.
DR EPD; Q9ER62; -.
DR MaxQB; Q9ER62; -.
DR PaxDb; Q9ER62; -.
DR PRIDE; Q9ER62; -.
DR ProteomicsDB; 259481; -. [Q9ER62-1]
DR ProteomicsDB; 259482; -. [Q9ER62-2]
DR DNASU; 79202; -.
DR Ensembl; ENSMUST00000075588; ENSMUSP00000075018; ENSMUSG00000010751. [Q9ER62-1]
DR Ensembl; ENSMUST00000084396; ENSMUSP00000081432; ENSMUSG00000010751. [Q9ER62-2]
DR Ensembl; ENSMUST00000146692; ENSMUSP00000119297; ENSMUSG00000010751. [Q9ER62-2]
DR GeneID; 79202; -.
DR KEGG; mmu:79202; -.
DR UCSC; uc009kps.1; mouse. [Q9ER62-2]
DR UCSC; uc009kpt.1; mouse. [Q9ER62-1]
DR CTD; 79202; -.
DR MGI; MGI:1930270; Tnfrsf22.
DR VEuPathDB; HostDB:ENSMUSG00000010751; -.
DR eggNOG; ENOG502RBEC; Eukaryota.
DR GeneTree; ENSGT00930000151070; -.
DR HOGENOM; CLU_130470_0_0_1; -.
DR InParanoid; Q9ER62; -.
DR OMA; NECTETA; -.
DR OrthoDB; 1457206at2759; -.
DR PhylomeDB; Q9ER62; -.
DR TreeFam; TF333916; -.
DR BioGRID-ORCS; 79202; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Tnfrsf22; mouse.
DR PRO; PR:Q9ER62; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9ER62; protein.
DR Bgee; ENSMUSG00000010751; Expressed in embryonic post-anal tail and 82 other tissues.
DR ExpressionAtlas; Q9ER62; baseline and differential.
DR Genevisible; Q9ER62; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IDA:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
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; cd15837; TNFRSF26; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR034062; TNFRSF26_N.
DR Pfam; PF00020; TNFR_c6; 2.
DR SMART; SM00208; TNFR; 3.
DR PROSITE; PS00652; TNFR_NGFR_1; 3.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..198
FT /note="Tumor necrosis factor receptor superfamily member
FT 22"
FT /id="PRO_0000058937"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 47..82
FT /note="TNFR-Cys 1"
FT REPEAT 84..124
FT /note="TNFR-Cys 2"
FT REPEAT 125..165
FT /note="TNFR-Cys 3"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 60..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 63..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 85..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 103..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 106..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 126..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 144..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 147..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 171..198
FT /note="NPRNRLFLLLSPLSVLIVSVVVFRIIRR -> RRSASVAWPI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11063728,
FT ECO:0000303|PubMed:12466268, ECO:0000303|PubMed:16141072"
FT /id="VSP_007648"
FT CONFLICT 12
FT /note="L -> V (in Ref. 2; AAL05073)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="L -> C (in Ref. 1; CAC16406)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..30
FT /note="LLLL -> CVV (in Ref. 1; CAC16406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22375 MW; EBF8F52961EA9983 CRC64;
MFGFFCSLVS SLSRWFLWRR LLLLLLLLLL NLPLQVKFAM LELHSFKCPA GEYWSKDVCC
KNCSAGTFVK APCEIPHTQG QCEKCHPGTF TEKDNYLDAC ILCSTCDKDQ EMVADCSATS
DRKCQCRTGL YYYDPKFPES CRPCTKCPQG IPVLQECNST ANTVCSSSVS NPRNRLFLLL
SPLSVLIVSV VVFRIIRR
