TNR25_HUMAN
ID TNR25_HUMAN Reviewed; 417 AA.
AC Q93038; B1ALX2; B1ALX3; B7ZLL7; O00275; O00276; O00277; O00278; O00279;
AC O00280; O14865; O14866; P78507; P78515; Q17RU4; Q92983; Q93036; Q93037;
AC Q99722; Q99830; Q99831; Q9BY86; Q9UME0; Q9UME1; Q9UME5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 25;
DE AltName: Full=Apo-3;
DE AltName: Full=Apoptosis-inducing receptor AIR;
DE AltName: Full=Apoptosis-mediating receptor DR3;
DE AltName: Full=Apoptosis-mediating receptor TRAMP;
DE AltName: Full=Death receptor 3;
DE AltName: Full=Lymphocyte-associated receptor of death;
DE Short=LARD;
DE AltName: Full=Protein WSL;
DE AltName: Full=Protein WSL-1;
DE Flags: Precursor;
GN Name=TNFRSF25; Synonyms=APO3, DDR3, DR3, TNFRSF12, WSL, WSL1;
GN ORFNames=UNQ455/PRO779;
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] (ISOFORMS 1; 3 AND 4), AND MUTAGENESIS.
RC TISSUE=Lymphoid tissue;
RX PubMed=8934525; DOI=10.1038/384372a0;
RA Kitson J., Raven T., Jiang Y.-P., Goeddel D.V., Giles K.M., Pun K.-T.,
RA Grinham C.J., Brown R., Farrow S.N.;
RT "A death-domain-containing receptor that mediates apoptosis.";
RL Nature 384:372-375(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=8875942; DOI=10.1126/science.274.5289.990;
RA Chinnaiyan A.M., O'Rourke K., Yu G.-L., Lyons R.H., Garg M., Duan D.R.,
RA Xing L., Gentz R., Ni J., Dixit V.M.;
RT "Signal transduction by DR3, a death domain-containing receptor related to
RT TNFR-1 and CD95.";
RL Science 274:990-992(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Degli-Esposti M.A., Din W.S., Cosman D., Smith C.A., Goodwin R.G.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=8994832; DOI=10.1016/s0960-9822(02)70791-4;
RA Marsters S.A., Sheridan J.P., Donahue C.J., Pitti R.M., Gray C.L.,
RA Goddard A.D., Bauer K.D., Ashkenazi A.;
RT "Apo-3, a new member of the tumor necrosis factor receptor family, contains
RT a death domain and activates apoptosis and NF-kappa-B.";
RL Curr. Biol. 6:1669-1676(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9 AND 10).
RX PubMed=9114039; DOI=10.1073/pnas.94.9.4615;
RA Screaton G.R., Xu X.-N., Olsen A.L., Cowper A.E., Tan R., McMichael A.J.,
RA Bell J.I.;
RT "LARD: a new lymphoid-specific death domain containing receptor regulated
RT by alternative pre-mRNA splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4615-4619(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 11 AND 12).
RX PubMed=9446802; DOI=10.1006/bbrc.1997.7948;
RA Warzocha K., Ribeiro P., Charlot C., Renard N., Coiffier B., Salles G.;
RT "A new death receptor 3 isoform: expression in human lymphoid cell lines
RT and non-Hodgkin's lymphomas.";
RL Biochem. Biophys. Res. Commun. 242:376-379(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT GLY-159.
RA Shiozawa S., Konishi Y., Murayama K., Mukae N., Yamamoto E., Hayashi S.,
RA Sato M., Shiozawa K., Tsukamoto Y.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-23; GLY-159 AND
RP ARG-254.
RG NIEHS SNPs program;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
RC TISSUE=Brain;
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 [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-417, AND FUNCTION.
RC TISSUE=Brain, and Fetal lung;
RX PubMed=9052839; DOI=10.1016/s1074-7613(00)80244-7;
RA Bodmer J.-L., Burns K., Schneider P., Hofmann K., Steiner V., Thome M.,
RA Bornand T., Hahne M., Schroeter M., Wilson A., French L.E., Browning J.L.,
RA Macdonald H.R., Tschopp J.;
RT "TRAMP, a novel apoptosis-mediating receptor with sequence homology to
RT tumor necrosis factor receptor 1 and Fas(Apo-1/CD95).";
RL Immunity 6:79-88(1997).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-417.
RC TISSUE=Brain;
RA Chaudhary P.M., Hood L.E.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP INTERACTION WITH BAG4.
RX PubMed=9915703; DOI=10.1126/science.283.5401.543;
RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
RT "Prevention of constitutive TNF receptor 1 signaling by silencer of death
RT domains.";
RL Science 283:543-546(1999).
RN [15]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [16]
RP GLYCOSYLATION AT ARG-352 (MICROBIAL INFECTION), AND MUTAGENESIS OF ARG-250.
RX PubMed=30979585; DOI=10.1016/j.molcel.2019.03.028;
RA Ding J., Pan X., Du L., Yao Q., Xue J., Yao H., Wang D.C., Li S., Shao F.;
RT "Structural and functional insights into host death domains inactivation by
RT the bacterial arginine GlcNAcyltransferase effector.";
RL Mol. Cell 74:922-935(2019).
CC -!- FUNCTION: Receptor for TNFSF12/APO3L/TWEAK. Interacts directly with the
CC adapter TRADD. Mediates activation of NF-kappa-B and induces apoptosis.
CC May play a role in regulating lymphocyte homeostasis.
CC {ECO:0000269|PubMed:8875942, ECO:0000269|PubMed:8994832,
CC ECO:0000269|PubMed:9052839}.
CC -!- SUBUNIT: Homodimer. Interacts strongly via the death domains with
CC TNFRSF1 and TRADD to activate at least two distinct signaling cascades,
CC apoptosis and NF-kappa-B signaling. Interacts with BAG4.
CC {ECO:0000269|PubMed:9915703}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 9]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 11]: Cell membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 10]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 12]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=1; Synonyms=WSL-1, LARD-1A;
CC IsoId=Q93038-1; Sequence=Displayed;
CC Name=2; Synonyms=LARD-1B;
CC IsoId=Q93038-2; Sequence=VSP_006504;
CC Name=3; Synonyms=WSL-S1, LARD-3;
CC IsoId=Q93038-3; Sequence=VSP_006497, VSP_006498;
CC Name=4; Synonyms=WSL-S2, LARD-2;
CC IsoId=Q93038-4; Sequence=VSP_006501, VSP_006502;
CC Name=5; Synonyms=LARD-4, LARD-11;
CC IsoId=Q93038-5; Sequence=VSP_006495;
CC Name=6; Synonyms=LARD-5;
CC IsoId=Q93038-6; Sequence=VSP_006491, VSP_006495;
CC Name=7; Synonyms=LARD-6;
CC IsoId=Q93038-7; Sequence=VSP_006491, VSP_006493, VSP_006494;
CC Name=8; Synonyms=LARD-7;
CC IsoId=Q93038-8; Sequence=VSP_006492;
CC Name=9; Synonyms=LARD-8;
CC IsoId=Q93038-9; Sequence=VSP_006491;
CC Name=10; Synonyms=LARD-9;
CC IsoId=Q93038-10; Sequence=VSP_006503;
CC Name=11; Synonyms=Beta;
CC IsoId=Q93038-11; Sequence=VSP_006496;
CC Name=12; Synonyms=Beta soluble;
CC IsoId=Q93038-12; Sequence=VSP_006499, VSP_006500;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in thymocytes and lymphocytes.
CC Detected in lymphocyte-rich tissues such as thymus, colon, intestine,
CC and spleen. Also found in the prostate.
CC -!- PTM: (Microbial infection) Glycosylated at Arg-352 by enteropathogenic
CC E.coli protein NleB1. {ECO:0000305|PubMed:30979585}.
CC -!- PTM: Glycosylated. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 12]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/tnfrsf25/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y09392; CAA70561.1; -; mRNA.
DR EMBL; Y09392; CAA70559.1; -; mRNA.
DR EMBL; Y09392; CAA70560.1; -; mRNA.
DR EMBL; U72763; AAC50819.1; -; mRNA.
DR EMBL; U83599; AAB41434.1; -; Genomic_DNA.
DR EMBL; U83600; AAB41435.1; -; Genomic_DNA.
DR EMBL; U78029; AAB40918.1; -; mRNA.
DR EMBL; U74611; AAB39714.1; -; mRNA.
DR EMBL; U94501; AAC51306.1; -; mRNA.
DR EMBL; U94504; AAC51309.1; -; mRNA.
DR EMBL; U94502; AAC51307.1; -; mRNA.
DR EMBL; U94503; AAC51308.1; -; mRNA.
DR EMBL; U94505; AAC51310.1; -; mRNA.
DR EMBL; U94506; AAC51311.1; -; mRNA.
DR EMBL; U94507; AAC51312.1; -; mRNA.
DR EMBL; U94508; AAC51313.1; -; mRNA.
DR EMBL; U94509; AAC51314.1; -; mRNA.
DR EMBL; U94510; AAC51315.1; -; mRNA.
DR EMBL; U94512; AAC51316.1; -; mRNA.
DR EMBL; U83598; AAB41433.1; -; mRNA.
DR EMBL; AF026070; AAC39556.1; -; mRNA.
DR EMBL; AF026071; AAB82288.1; -; mRNA.
DR EMBL; AB051850; BAB40662.1; -; Genomic_DNA.
DR EMBL; AB051851; BAB40663.1; -; Genomic_DNA.
DR EMBL; AY358309; AAQ88676.1; -; mRNA.
DR EMBL; AY254324; AAO63495.1; -; Genomic_DNA.
DR EMBL; U75380; AAC51192.1; -; mRNA.
DR EMBL; AL158217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117189; AAI17190.1; -; mRNA.
DR EMBL; BC143886; AAI43887.1; -; mRNA.
DR EMBL; U75381; AAC51193.1; -; mRNA.
DR EMBL; U83597; AAB41432.1; -; mRNA.
DR CCDS; CCDS71.1; -. [Q93038-1]
DR CCDS; CCDS72.1; -. [Q93038-11]
DR CCDS; CCDS73.1; -. [Q93038-10]
DR CCDS; CCDS74.1; -. [Q93038-9]
DR CCDS; CCDS75.1; -. [Q93038-8]
DR RefSeq; NP_001034753.1; NM_001039664.1. [Q93038-5]
DR RefSeq; NP_003781.1; NM_003790.2. [Q93038-1]
DR RefSeq; NP_683866.1; NM_148965.1. [Q93038-11]
DR RefSeq; NP_683867.1; NM_148966.1. [Q93038-10]
DR RefSeq; NP_683868.1; NM_148967.1. [Q93038-9]
DR RefSeq; NP_683871.1; NM_148970.1. [Q93038-8]
DR PDB; 5YGP; X-ray; 2.09 A; A/B/C/D=328-415.
DR PDB; 5YGS; X-ray; 2.69 A; A/B/C/D=328-415.
DR PDBsum; 5YGP; -.
DR PDBsum; 5YGS; -.
DR AlphaFoldDB; Q93038; -.
DR SMR; Q93038; -.
DR BioGRID; 114258; 13.
DR DIP; DIP-59563N; -.
DR IntAct; Q93038; 1.
DR STRING; 9606.ENSP00000367013; -.
DR GlyGen; Q93038; 4 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q93038; -.
DR BioMuta; TNFRSF25; -.
DR DMDM; 2501233; -.
DR MassIVE; Q93038; -.
DR PeptideAtlas; Q93038; -.
DR PRIDE; Q93038; -.
DR ProteomicsDB; 75674; -. [Q93038-1]
DR ProteomicsDB; 75675; -. [Q93038-10]
DR ProteomicsDB; 75678; -. [Q93038-2]
DR ProteomicsDB; 75680; -. [Q93038-4]
DR ProteomicsDB; 75685; -. [Q93038-9]
DR Antibodypedia; 13011; 698 antibodies from 42 providers.
DR DNASU; 8718; -.
DR Ensembl; ENST00000348333.7; ENSP00000314451.3; ENSG00000215788.11. [Q93038-9]
DR Ensembl; ENST00000351748.7; ENSP00000326762.3; ENSG00000215788.11. [Q93038-8]
DR Ensembl; ENST00000351959.9; ENSP00000337713.5; ENSG00000215788.11. [Q93038-10]
DR Ensembl; ENST00000356876.8; ENSP00000349341.3; ENSG00000215788.11. [Q93038-1]
DR Ensembl; ENST00000377782.7; ENSP00000367013.3; ENSG00000215788.11. [Q93038-11]
DR Ensembl; ENST00000414040.6; ENSP00000404274.2; ENSG00000215788.11. [Q93038-3]
DR Ensembl; ENST00000485036.5; ENSP00000431554.1; ENSG00000215788.11. [Q93038-12]
DR Ensembl; ENST00000502588.5; ENSP00000423121.1; ENSG00000215788.11. [Q93038-6]
DR Ensembl; ENST00000502730.5; ENSP00000421976.1; ENSG00000215788.11. [Q93038-7]
DR Ensembl; ENST00000510563.5; ENSP00000424071.1; ENSG00000215788.11. [Q93038-5]
DR GeneID; 8718; -.
DR KEGG; hsa:8718; -.
DR MANE-Select; ENST00000356876.8; ENSP00000349341.3; NM_003790.3; NP_003781.1.
DR UCSC; uc001ana.4; human. [Q93038-1]
DR CTD; 8718; -.
DR DisGeNET; 8718; -.
DR GeneCards; TNFRSF25; -.
DR HGNC; HGNC:11910; TNFRSF25.
DR HPA; ENSG00000215788; Tissue enhanced (lymphoid tissue, pituitary gland, skin).
DR MIM; 603366; gene.
DR neXtProt; NX_Q93038; -.
DR OpenTargets; ENSG00000215788; -.
DR PharmGKB; PA36603; -.
DR VEuPathDB; HostDB:ENSG00000215788; -.
DR eggNOG; ENOG502S19V; Eukaryota.
DR GeneTree; ENSGT00940000161888; -.
DR HOGENOM; CLU_053353_0_0_1; -.
DR InParanoid; Q93038; -.
DR OMA; GVFWVQV; -.
DR OrthoDB; 726174at2759; -.
DR PhylomeDB; Q93038; -.
DR TreeFam; TF333916; -.
DR PathwayCommons; Q93038; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; Q93038; -.
DR SIGNOR; Q93038; -.
DR BioGRID-ORCS; 8718; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; TNFRSF25; human.
DR GeneWiki; TNFRSF25; -.
DR GenomeRNAi; 8718; -.
DR Pharos; Q93038; Tbio.
DR PRO; PR:Q93038; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q93038; protein.
DR Bgee; ENSG00000215788; Expressed in right hemisphere of cerebellum and 128 other tissues.
DR ExpressionAtlas; Q93038; baseline and differential.
DR Genevisible; Q93038; HS.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd13420; TNFRSF25; 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; IPR022329; TNFR_25.
DR InterPro; IPR034050; TNFRSF25_N.
DR PANTHER; PTHR47220; PTHR47220; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01972; TNFACTORR25.
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; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..417
FT /note="Tumor necrosis factor receptor superfamily member
FT 25"
FT /id="PRO_0000034606"
FT TOPO_DOM 25..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 34..71
FT /note="TNFR-Cys 1"
FT REPEAT 72..115
FT /note="TNFR-Cys 2"
FT REPEAT 116..163
FT /note="TNFR-Cys 3"
FT REPEAT 164..192
FT /note="TNFR-Cys 4"
FT DOMAIN 332..413
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="(Microbial infection) N-beta-linked (GlcNAc)
FT arginine"
FT /evidence="ECO:0000305|PubMed:30979585"
FT DISULFID 35..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 48..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 51..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 73..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 92..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 95..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 117..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 138..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 141..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 165..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 179..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 187..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 54..236
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:9114039"
FT /id="VSP_006492"
FT VAR_SEQ 54..98
FT /note="Missing (in isoform 6, isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:9114039"
FT /id="VSP_006491"
FT VAR_SEQ 156..171
FT /note="SRRDTDCGTCLPGFYE -> HPSVTLGQRPHPSSTS (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9114039"
FT /id="VSP_006493"
FT VAR_SEQ 172..417
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9114039"
FT /id="VSP_006494"
FT VAR_SEQ 182..417
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9114039"
FT /id="VSP_006495"
FT VAR_SEQ 182..277
FT /note="STLGSCPERCAAVCGWRQMFWVQVLLAGLVVPLLLGATLTYTYRHCWPHKPL
FT VTADEAGMEALTPPPATHLSPLDSAHTLLAPPDSSEKICTVQLV -> PPPSLAGAPWG
FT AVQSAVPLSVAGGRVGGVLGMRVGELGWTEGRRVRRGATTQHPPAAFSVLGPGAPGWPC
FT GPPPAWGHPDLHIPPLLASQAPGYCR (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:9446802"
FT /id="VSP_006499"
FT VAR_SEQ 182..218
FT /note="STLGSCPERCAAVCGWRQMFWVQVLLAGLVVPLLLGA -> VLGPGAPGWPC
FT GPPPAWGHPDLHIPPLLASQAPGYCR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8934525,
FT ECO:0000303|PubMed:9114039"
FT /id="VSP_006497"
FT VAR_SEQ 182..200
FT /note="STLGSCPERCAAVCGWRQM -> PPPSLAGAPWGAVQSAVPLSVAGGRVGV
FT (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:9446802"
FT /id="VSP_006496"
FT VAR_SEQ 200..253
FT /note="MFWVQVLLAGLVVPLLLGATLTYTYRHCWPHKPLVTADEAGMEALTPPPATH
FT LS -> SRWCAGNARGRTGMDRGEAGEEGGNHPTPTSCFQCSGSRCSWLALWSPSCLGP
FT P (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8934525,
FT ECO:0000303|PubMed:9114039"
FT /id="VSP_006501"
FT VAR_SEQ 200..237
FT /note="MFWVQVLLAGLVVPLLLGATLTYTYRHCWPHKPLVTAD -> N (in
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9114039"
FT /id="VSP_006503"
FT VAR_SEQ 219..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8934525,
FT ECO:0000303|PubMed:9114039"
FT /id="VSP_006498"
FT VAR_SEQ 236
FT /note="A -> AA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9114039"
FT /id="VSP_006504"
FT VAR_SEQ 254..417
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8934525,
FT ECO:0000303|PubMed:9114039"
FT /id="VSP_006502"
FT VAR_SEQ 278..417
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000303|PubMed:9446802"
FT /id="VSP_006500"
FT VARIANT 23
FT /note="R -> Q (in dbSNP:rs35771371)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_018826"
FT VARIANT 159
FT /note="D -> G (in dbSNP:rs11800462)"
FT /evidence="ECO:0000269|Ref.7, ECO:0000269|Ref.9"
FT /id="VAR_018827"
FT VARIANT 254
FT /note="P -> R (in dbSNP:rs34529016)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_018828"
FT VARIANT 370
FT /note="R -> L (in dbSNP:rs1064590)"
FT /id="VAR_011814"
FT VARIANT 381
FT /note="R -> H (in dbSNP:rs1059333)"
FT /id="VAR_011815"
FT MUTAGEN 354
FT /note="L->A: Suppresses homodimerization, TNFR1
FT interaction, and apoptosis induction."
FT /evidence="ECO:0000269|PubMed:8934525"
FT MUTAGEN 356
FT /note="L->A: Suppresses homodimerization, and TNFR1
FT interaction."
FT /evidence="ECO:0000269|PubMed:8934525"
FT MUTAGEN 373
FT /note="D->A: Suppresses homodimerization, and TNFR1
FT interaction."
FT /evidence="ECO:0000269|PubMed:8934525"
FT CONFLICT 4..6
FT /note="RPR -> AAA (in Ref. 12; AAC51192/AAC51193)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="P -> H (in Ref. 13; AAB41435)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> L (in Ref. 12 and 13)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> R (in Ref. 1 and 6)"
FT /evidence="ECO:0000305"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:5YGP"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:5YGP"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5YGP"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:5YGP"
FT HELIX 359..382
FT /evidence="ECO:0007829|PDB:5YGP"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:5YGP"
FT HELIX 390..397
FT /evidence="ECO:0007829|PDB:5YGP"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:5YGP"
SQ SEQUENCE 417 AA; 45385 MW; 5226319DFDB46706 CRC64;
MEQRPRGCAA VAAALLLVLL GARAQGGTRS PRCDCAGDFH KKIGLFCCRG CPAGHYLKAP
CTEPCGNSTC LVCPQDTFLA WENHHNSECA RCQACDEQAS QVALENCSAV ADTRCGCKPG
WFVECQVSQC VSSSPFYCQP CLDCGALHRH TRLLCSRRDT DCGTCLPGFY EHGDGCVSCP
TSTLGSCPER CAAVCGWRQM FWVQVLLAGL VVPLLLGATL TYTYRHCWPH KPLVTADEAG
MEALTPPPAT HLSPLDSAHT LLAPPDSSEK ICTVQLVGNS WTPGYPETQE ALCPQVTWSW
DQLPSRALGP AAAPTLSPES PAGSPAMMLQ PGPQLYDVMD AVPARRWKEF VRTLGLREAE
IEAVEVEIGR FRDQQYEMLK RWRQQQPAGL GAVYAALERM GLDGCVEDLR SRLQRGP
