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Database: UniProt
Entry: P20333
LinkDB: P20333
Original site: P20333 
ID   TNR1B_HUMAN             Reviewed;         461 AA.
AC   P20333; B1AJZ3; Q16042; Q6YI29; Q9UIH1;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 3.
DT   03-SEP-2014, entry version 170.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 1B;
DE   AltName: Full=Tumor necrosis factor receptor 2;
DE            Short=TNF-R2;
DE   AltName: Full=Tumor necrosis factor receptor type II;
DE            Short=TNF-RII;
DE            Short=TNFR-II;
DE   AltName: Full=p75;
DE   AltName: Full=p80 TNF-alpha receptor;
DE   AltName: CD_antigen=CD120b;
DE   AltName: INN=Etanercept;
DE   Contains:
DE     RecName: Full=Tumor necrosis factor receptor superfamily member 1b, membrane form;
DE   Contains:
DE     RecName: Full=Tumor necrosis factor-binding protein 2;
DE     AltName: Full=TBP-2;
DE     AltName: Full=TBPII;
DE   Flags: Precursor;
GN   Name=TNFRSF1B; Synonyms=TNFBR, TNFR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-196.
RX   PubMed=2172983; DOI=10.1073/pnas.87.21.8331;
RA   Kohno T., Brewer M.T., Baker S.L., Schwartz P.E., King M.W.,
RA   Hale K.K., Squires C.H., Thompson R.C., Vannice J.L.;
RT   "A second tumor necrosis factor receptor gene product can shed a
RT   naturally occurring tumor necrosis factor inhibitor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8331-8335(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2160731; DOI=10.1126/science.2160731;
RA   Smith C.A., Davis T., Anderson D., Solam L., Beckmann M.P., Jerzy R.,
RA   Dower S.K., Cosman D., Goodwin R.G.;
RT   "A receptor for tumor necrosis factor defines an unusual family of
RT   cellular and viral proteins.";
RL   Science 248:1019-1023(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=8661109; DOI=10.1006/geno.1996.0327;
RA   Beltinger C.P., White P.S., Maris J.M., Sulman E.P., Jensen S.J.,
RA   Lepaslier D., Stallard B.J., Goeddel D.V., Desauvage F.J.,
RA   Brodeur G.M.;
RT   "Physical mapping and genomic structure of the human TNFR2 gene.";
RL   Genomics 35:94-100(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP   FUNCTION (ISOFORM 2).
RX   PubMed=14688072; DOI=10.1093/intimm/dxh014;
RA   Lainez B., Fernandez-Real J.M., Romero X., Esplugues E., Canete J.D.,
RA   Ricart W., Engel P.;
RT   "Identification and characterization of a novel spliced variant that
RT   encodes human soluble tumor necrosis factor receptor 2.";
RL   Int. Immunol. 16:169-177(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-187; ARG-196;
RP   LYS-232; THR-236; PRO-264 AND ARG-295.
RG   NIEHS SNPs program;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-196; LYS-232;
RP   PRO-269 AND ARG-301.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=PNS;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PROTEIN SEQUENCE OF 23-40; 65-69; 136-141; 300-306 AND 346-362.
RX   PubMed=2173696;
RA   Loetscher H., Schlaeger E.J., Lahm H.-W., Pan Y.-C.E., Lesslauer W.,
RA   Brockhaus M.;
RT   "Purification and partial amino acid sequence analysis of two distinct
RT   tumor necrosis factor receptors from HL60 cells.";
RL   J. Biol. Chem. 265:20131-20138(1990).
RN   [12]
RP   PROTEIN SEQUENCE OF 27-37.
RC   TISSUE=Urine;
RX   PubMed=8015639;
RA   Suzuki J., Tomizawa S., Arai H., Seki Y., Maruyama K., Kuroume T.;
RT   "Purification of two types of TNF inhibitors in the urine of the
RT   patient with chronic glomerulonephritis.";
RL   Nephron 66:386-390(1994).
RN   [13]
RP   PROTEIN SEQUENCE OF 27-31.
RC   TISSUE=Urine;
RX   PubMed=2153136;
RA   Engelmann H., Novick D., Wallach D.;
RT   "Two tumor necrosis factor-binding proteins purified from human urine.
RT   Evidence for immunological cross-reactivity with cell surface tumor
RT   necrosis factor receptors.";
RL   J. Biol. Chem. 265:1531-1536(1990).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 37-461 (ISOFORM 1).
RX   PubMed=1966549; DOI=10.1016/1043-4666(90)90022-L;
RA   Dembic Z., Loetscher H., Gubler U., Pan Y.C., Lahm H.-W., Gentz R.,
RA   Brockhaus M., Lesslauer W.;
RT   "Two human TNF receptors have similar extracellular, but distinct
RT   intracellular, domain sequences.";
RL   Cytokine 2:231-237(1990).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 116-461 (ISOFORM 1), PARTIAL PROTEIN
RP   SEQUENCE, AND VARIANT ARG-196.
RX   PubMed=2166946; DOI=10.1073/pnas.87.16.6151;
RA   Heller R.A., Song K., Onasch M.A., Fischer W.H., Chang D.,
RA   Ringold G.M.;
RT   "Complementary DNA cloning of a receptor for tumor necrosis factor and
RT   demonstration of a shed form of the receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6151-6155(1990).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 154-183, AND VARIANTS ARG-196 AND
RP   LYS-232.
RX   PubMed=11197692; DOI=10.1038/sj.gene.6363700;
RA   Tsuchiya N., Komata T., Matsushita M., Ohashi J., Tokunaga K.;
RT   "New single nucleotide polymorphisms in the coding region of human
RT   TNFR2: association with systemic lupus erythematosus.";
RL   Genes Immun. 1:501-503(2000).
RN   [17]
RP   CHARACTERIZATION.
RX   PubMed=1328224;
RA   Pennica D., Lam V.T., Mize N.K., Weber R.F., Lewis M., Fendly B.M.,
RA   Lipari M.T., Goeddel D.V.;
RT   "Biochemical properties of the 75-kDa tumor necrosis factor receptor.
RT   Characterization of ligand binding, internalization, and receptor
RT   phosphorylation.";
RL   J. Biol. Chem. 267:21172-21178(1992).
RN   [18]
RP   INTERACTION WITH TRAF2.
RX   PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
RA   Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
RT   "A novel family of putative signal transducers associated with the
RT   cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
RL   Cell 78:681-692(1994).
RN   [19]
RP   FUNCTION, AND INTERACTION WITH BMX.
RX   PubMed=12370298; DOI=10.1128/MCB.22.21.7512-7523.2002;
RA   Pan S., An P., Zhang R., He X., Yin G., Min W.;
RT   "Etk/Bmx as a tumor necrosis factor receptor type 2-specific kinase:
RT   role in endothelial cell migration and angiogenesis.";
RL   Mol. Cell. Biol. 22:7512-7523(2002).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 419-428 IN COMPLEX WITH
RP   TRAF2.
RX   PubMed=10206649; DOI=10.1038/19110;
RA   Park Y.C., Burkitt V., Villa A.R., Tong L., Wu H.;
RT   "Structural basis for self-association and receptor recognition of
RT   human TRAF2.";
RL   Nature 398:533-538(1999).
RN   [21]
RP   VARIANTS ARG-196 AND LYS-232.
RX   PubMed=11762942;
RX   DOI=10.1002/1529-0131(200112)44:12<2819::AID-ART469>3.0.CO;2-2;
RA   Morita C., Horiuchi T., Tsukamoto H., Hatta N., Kikuchi Y.,
RA   Arinobu Y., Otsuka T., Sawabe T., Harashima S., Nagasawa K., Niho Y.;
RT   "Association of tumor necrosis factor receptor type II polymorphism
RT   196R with systemic lupus erythematosus in the Japanese: molecular and
RT   functional analysis.";
RL   Arthritis Rheum. 44:2819-2827(2001).
RN   [22]
RP   VARIANT ARG-196.
RX   PubMed=12161545; DOI=10.1210/jcem.87.8.8715;
RA   Peral B., San Millan J.L., Castello R., Moghetti P.,
RA   Escobar-Morreale H.F.;
RT   "Comment: the methionine 196 arginine polymorphism in exon 6 of the
RT   TNF receptor 2 gene (TNFRSF1B) is associated with the polycystic ovary
RT   syndrome and hyperandrogenism.";
RL   J. Clin. Endocrinol. Metab. 87:3977-3983(2002).
CC   -!- FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and
CC       approximately 5-fold lower affinity for homotrimeric
CC       TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the
CC       apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This
CC       receptor mediates most of the metabolic effects of TNF-alpha.
CC       Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that
CC       it regulates TNF-alpha function by antagonizing its biological
CC       activity.
CC   -!- SUBUNIT: Binds to TRAF2. Interacts with BMX.
CC   -!- INTERACTION:
CC       P28799:GRN; NbExp=5; IntAct=EBI-358983, EBI-747754;
CC       P01375:TNF; NbExp=2; IntAct=EBI-358983, EBI-359977;
CC       Q12933:TRAF2; NbExp=3; IntAct=EBI-358983, EBI-355744;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC   -!- SUBCELLULAR LOCATION: Tumor necrosis factor-binding protein 2:
CC       Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P20333-1; Sequence=Displayed;
CC       Name=2; Synonyms=DS-TNFR2(Delta7,8), sTNFR2;
CC         IsoId=P20333-2; Sequence=VSP_011826, VSP_011827;
CC   -!- PTM: Phosphorylated; mainly on serine residues and with a very low
CC       level on threonine residues.
CC   -!- PTM: A soluble form (tumor necrosis factor binding protein 2) is
CC       produced from the membrane form by proteolytic processing.
CC   -!- PHARMACEUTICAL: Available under the name Enbrel (Immunex and
CC       Wyeth-Ayerst). Used to treat moderate to severe rheumatoid
CC       arthritis (RA). Enbrel consist of the extracellular ligand-binding
CC       portion of TNFRSF1B linked to an immunoglobulin Fc chain. It binds
CC       to TNF-alpha and blocks its interactions with receptors.
CC   -!- SIMILARITY: Contains 4 TNFR-Cys repeats.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/tnfrsf1b/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tnfrsf1b/";
CC   -!- WEB RESOURCE: Name=Enbrel; Note=Clinical information on Enbrel;
CC       URL="http://www.enbrel.com/index.jspx";
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DR   EMBL; M55994; AAA36755.1; -; mRNA.
DR   EMBL; M32315; AAA59929.1; -; mRNA.
DR   EMBL; U52165; AAC50622.1; -; Genomic_DNA.
DR   EMBL; U52156; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52157; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52158; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52159; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52160; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52161; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52162; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52163; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; U52164; AAC50622.1; JOINED; Genomic_DNA.
DR   EMBL; AY148473; AAN72434.1; -; mRNA.
DR   EMBL; BT019927; AAV38730.1; -; mRNA.
DR   EMBL; AY264804; AAO89076.1; -; Genomic_DNA.
DR   EMBL; AY342040; AAP88939.1; -; Genomic_DNA.
DR   EMBL; AL031276; CAI19225.1; -; Genomic_DNA.
DR   EMBL; AL357835; CAI19225.1; JOINED; Genomic_DNA.
DR   EMBL; AL357835; CAH73721.1; -; Genomic_DNA.
DR   EMBL; AL031276; CAH73721.1; JOINED; Genomic_DNA.
DR   EMBL; CH471130; EAW71733.1; -; Genomic_DNA.
DR   EMBL; BC052977; AAH52977.1; -; mRNA.
DR   EMBL; S63368; AAB19824.2; -; mRNA.
DR   EMBL; M35857; AAA63262.1; -; mRNA.
DR   EMBL; AB030950; BAA89053.1; -; Genomic_DNA.
DR   CCDS; CCDS145.1; -. [P20333-1]
DR   PIR; A35356; A35356.
DR   RefSeq; NP_001057.1; NM_001066.2. [P20333-1]
DR   UniGene; Hs.256278; -.
DR   PDB; 1CA9; X-ray; 2.30 A; G/H=420-428.
DR   PDB; 3ALQ; X-ray; 3.00 A; R/S/T/U/V/W=33-205.
DR   PDBsum; 1CA9; -.
DR   PDBsum; 3ALQ; -.
DR   ProteinModelPortal; P20333; -.
DR   SMR; P20333; 37-200.
DR   BioGrid; 112987; 26.
DR   DIP; DIP-78N; -.
DR   IntAct; P20333; 12.
DR   MINT; MINT-134958; -.
DR   STRING; 9606.ENSP00000365435; -.
DR   ChEMBL; CHEMBL1250356; -.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00065; Infliximab.
DR   GuidetoPHARMACOLOGY; 1871; -.
DR   PhosphoSite; P20333; -.
DR   DMDM; 21264534; -.
DR   PaxDb; P20333; -.
DR   PeptideAtlas; P20333; -.
DR   PRIDE; P20333; -.
DR   DNASU; 7133; -.
DR   Ensembl; ENST00000376259; ENSP00000365435; ENSG00000028137. [P20333-1]
DR   GeneID; 7133; -.
DR   KEGG; hsa:7133; -.
DR   UCSC; uc001att.3; human. [P20333-1]
DR   CTD; 7133; -.
DR   GeneCards; GC01P012161; -.
DR   HGNC; HGNC:11917; TNFRSF1B.
DR   HPA; CAB013045; -.
DR   HPA; HPA004796; -.
DR   MIM; 191191; gene.
DR   neXtProt; NX_P20333; -.
DR   PharmGKB; PA36610; -.
DR   eggNOG; NOG42764; -.
DR   HOGENOM; HOG000132845; -.
DR   HOVERGEN; HBG054237; -.
DR   InParanoid; P20333; -.
DR   KO; K05141; -.
DR   OMA; GNASMDA; -.
DR   OrthoDB; EOG786H2Q; -.
DR   PhylomeDB; P20333; -.
DR   TreeFam; TF331157; -.
DR   EvolutionaryTrace; P20333; -.
DR   GeneWiki; TNFRSF1B; -.
DR   GenomeRNAi; 7133; -.
DR   NextBio; 27909; -.
DR   PMAP-CutDB; P20333; -.
DR   PRO; PR:P20333; -.
DR   ArrayExpress; P20333; -.
DR   Bgee; P20333; -.
DR   CleanEx; HS_TNFRSF1B; -.
DR   Genevestigator; P20333; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043196; C:varicosity; IEA:Ensembl.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; TAS:ProtInc.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR   GO; GO:0006955; P:immune response; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR   GO; GO:0050779; P:RNA destabilization; IEA:Ensembl.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020411; TNFR_1B.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PRINTS; PR01919; TNFACTORR1B.
DR   SMART; SM00208; TNFR; 4.
DR   PROSITE; PS00652; TNFR_NGFR_1; 2.
DR   PROSITE; PS50050; TNFR_NGFR_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; Cell membrane;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Membrane; Pharmaceutical; Phosphoprotein; Polymorphism;
KW   Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22
FT   CHAIN        23    461       Tumor necrosis factor receptor
FT                                superfamily member 1b, membrane form.
FT                                /FTId=PRO_0000034548.
FT   CHAIN        27      ?       Tumor necrosis factor-binding protein 2.
FT                                /FTId=PRO_0000034549.
FT   TOPO_DOM     23    257       Extracellular (Potential).
FT   TRANSMEM    258    287       Helical; (Potential).
FT   TOPO_DOM    288    461       Cytoplasmic (Potential).
FT   REPEAT       39     76       TNFR-Cys 1.
FT   REPEAT       77    118       TNFR-Cys 2.
FT   REPEAT      119    162       TNFR-Cys 3.
FT   REPEAT      163    201       TNFR-Cys 4.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (Potential).
FT   DISULFID     40     53       By similarity.
FT   DISULFID     54     67       By similarity.
FT   DISULFID     57     75       By similarity.
FT   DISULFID     78     93       By similarity.
FT   DISULFID     96    110       By similarity.
FT   DISULFID    100    118       By similarity.
FT   DISULFID    120    126       By similarity.
FT   DISULFID    134    143       By similarity.
FT   DISULFID    137    161       By similarity.
FT   DISULFID    164    179       By similarity.
FT   VAR_SEQ     263    268       GLIVGV -> ASLACR (in isoform 2).
FT                                /FTId=VSP_011826.
FT   VAR_SEQ     269    461       Missing (in isoform 2).
FT                                /FTId=VSP_011827.
FT   VARIANT     187    187       V -> M (in dbSNP:rs2228494).
FT                                /FTId=VAR_017176.
FT   VARIANT     196    196       M -> R (frequent polymorphism; seems to
FT                                be associated with hyperandrogenism,
FT                                polycystic ovary syndrome (PCOS) and
FT                                systemic lupus erythematosus;
FT                                dbSNP:rs1061622).
FT                                /FTId=VAR_015434.
FT   VARIANT     232    232       E -> K (in dbSNP:rs5746026).
FT                                /FTId=VAR_015435.
FT   VARIANT     236    236       A -> T (in dbSNP:rs5746027).
FT                                /FTId=VAR_017177.
FT   VARIANT     264    264       L -> P (in dbSNP:rs2229700).
FT                                /FTId=VAR_017178.
FT   VARIANT     269    269       T -> P (in dbSNP:rs17879042).
FT                                /FTId=VAR_017179.
FT   VARIANT     295    295       Q -> R (in dbSNP:rs5746032).
FT                                /FTId=VAR_017180.
FT   VARIANT     301    301       P -> R (in dbSNP:rs17883432).
FT                                /FTId=VAR_017181.
FT   CONFLICT     35     37       EPG -> APT (in Ref. 12; AA sequence).
FT   CONFLICT     98     98       S -> P (in Ref. 4; AAN72434).
FT   CONFLICT    102    102       S -> P (in Ref. 4; AAN72434).
FT   CONFLICT    141    141       R -> P (in Ref. 15; AAA63262).
FT   CONFLICT    363    363       A -> T (in Ref. 15; AAA63262).
FT   STRAND       44     47
FT   TURN         48     51
FT   STRAND       52     55
FT   STRAND       61     65
FT   STRAND       74     77
FT   STRAND       86     88
FT   STRAND      104    108
FT   STRAND      112    114
FT   STRAND      117    120
FT   STRAND      124    129
FT   STRAND      131    139
FT   STRAND      147    151
FT   TURN        154    156
FT   STRAND      160    163
FT   STRAND      174    176
FT   STRAND      194    196
SQ   SEQUENCE   461 AA;  48291 MW;  603D0AE1CD69ACBF CRC64;
     MAPVAVWAAL AVGLELWAAA HALPAQVAFT PYAPEPGSTC RLREYYDQTA QMCCSKCSPG
     QHAKVFCTKT SDTVCDSCED STYTQLWNWV PECLSCGSRC SSDQVETQAC TREQNRICTC
     RPGWYCALSK QEGCRLCAPL RKCRPGFGVA RPGTETSDVV CKPCAPGTFS NTTSSTDICR
     PHQICNVVAI PGNASMDAVC TSTSPTRSMA PGAVHLPQPV STRSQHTQPT PEPSTAPSTS
     FLLPMGPSPP AEGSTGDFAL PVGLIVGVTA LGLLIIGVVN CVIMTQVKKK PLCLQREAKV
     PHLPADKARG TQGPEQQHLL ITAPSSSSSS LESSASALDR RAPTRNQPQA PGVEASGAGE
     ARASTGSSDS SPGGHGTQVN VTCIVNVCSS SDHSSQCSSQ ASSTMGDTDS SPSESPKDEQ
     VPFSKEECAF RSQLETPETL LGSTEEKPLP LGVPDAGMKP S
//
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