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 01-MAY-2013, entry version 157.
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/jc.87.8.3977;
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 -!- 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 IPI; IPI00023501; -.
DR IPI; IPI00473089; -.
DR PIR; A35356; A35356.
DR RefSeq; NP_001057.1; NM_001066.2.
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 DIP; DIP-78N; -.
DR IntAct; P20333; 9.
DR MINT; MINT-134958; -.
DR STRING; 9606.ENSP00000365435; -.
DR PhosphoSite; P20333; -.
DR DMDM; 21264534; -.
DR PaxDb; P20333; -.
DR PeptideAtlas; P20333; -.
DR PRIDE; P20333; -.
DR DNASU; 7133; -.
DR Ensembl; ENST00000376259; ENSP00000365435; ENSG00000028137.
DR GeneID; 7133; -.
DR KEGG; hsa:7133; -.
DR UCSC; uc001att.3; human.
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; KDEQVPF; -.
DR OrthoDB; EOG48D0W0; -.
DR PhylomeDB; P20333; -.
DR Pathway_Interaction_DB; tnfpathway; TNF receptor signaling pathway.
DR ChEMBL; CHEMBL1250356; -.
DR DrugBank; DB00005; Etanercept.
DR DrugBank; DB00065; Infliximab.
DR EvolutionaryTrace; P20333; -.
DR GenomeRNAi; 7133; -.
DR NextBio; 27909; -.
DR PMAP-CutDB; P20333; -.
DR ArrayExpress; P20333; -.
DR Bgee; P20333; -.
DR CleanEx; HS_TNFRSF1B; -.
DR Genevestigator; P20333; -.
DR GermOnline; ENSG00000028137; Homo sapiens.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IEA:Compara.
DR GO; GO:0005634; C:nucleus; IEA:Compara.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043196; C:varicosity; IEA:Compara.
DR GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Compara.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0006955; P:immune response; IEA:Compara.
DR GO; GO:0006954; P:inflammatory response; IEA:Compara.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Compara.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR GO; GO:0050779; P:RNA destabilization; IEA:Compara.
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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