ID   TR11B_HUMAN             Reviewed;         401 AA.
AC   O00300; B2R9A8; O60236; Q53FX6; Q9UHP4;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 3.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 11B;
DE   AltName: Full=Osteoclastogenesis inhibitory factor;
DE   AltName: Full=Osteoprotegerin;
DE   Flags: Precursor;
GN   Name=TNFRSF11B; Synonyms=OCIF, OPG;
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], AND VARIANT LYS-3.
RC   TISSUE=Kidney;
RX   PubMed=9108485; DOI=10.1016/s0092-8674(00)80209-3;
RA   Simonet W.S., Lacey D.L., Dunstan C.R., Kelley M., Chang M.-S., Luethy R.,
RA   Nguyen H.Q., Wooden S., Bennett L., Boone T., Shimamoto G., Derose M.,
RA   Elliott R., Colombero A., Tan H.-L., Trail G., Sullivan J., Davy E.,
RA   Bucay N., Renshaw-Gegg L., Hughes T.M., Hill D., Pattison W., Campbell P.,
RA   Sander S., Van G., Tarpley J., Derby P., Lee R., Suggs S., Boyle W.J.;
RT   "Osteoprotegerin: a novel secreted protein involved in the regulation of
RT   bone density.";
RL   Cell 89:309-319(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-3.
RC   TISSUE=Lung cancer;
RX   PubMed=9492069; DOI=10.1210/endo.139.3.5837;
RA   Yasuda H., Shima N., Nakagawa N., Mochizuki S., Yano K., Fujise N.,
RA   Sato Y., Goto M., Yamaguchi K., Kuriyama M., Kanno T., Murakami A.,
RA   Tsuda E., Morinaga T., Higashio K.;
RT   "Identity of osteoclastogenesis inhibitory factor (OCIF) and
RT   osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits
RT   osteoclastogenesis in vitro.";
RL   Endocrinology 139:1329-1337(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-3.
RC   TISSUE=Placenta;
RX   PubMed=9688283; DOI=10.1046/j.1432-1327.1998.2540685.x;
RA   Morinaga T., Nakagawa N., Yasuda H., Tsuda E., Higashio K.;
RT   "Cloning and characterization of the gene encoding human
RT   osteoprotegerin/osteoclastogenesis-inhibitory factor.";
RL   Eur. J. Biochem. 254:685-691(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-3.
RC   TISSUE=Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-3 AND MET-104.
RG   NIEHS SNPs program;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [9]
RP   PROTEIN SEQUENCE OF 22-36 AND 378-401.
RX   PubMed=9571159; DOI=10.1006/bbrc.1998.8443;
RA   Tomoyasu A., Goto M., Fujise N., Mochizuki S., Yasuda H., Morinaga T.,
RA   Tsuda E., Higashio K.;
RT   "Characterization of monomeric and homodimeric forms of osteoclastogenesis
RT   inhibitory factor.";
RL   Biochem. Biophys. Res. Commun. 245:382-387(1998).
RN   [10]
RP   PROTEIN SEQUENCE OF 22-36.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-393.
RC   TISSUE=Placenta;
RX   PubMed=12110935;
RA   He Z.-Y., Yang G.-Z., Zhang W.-J., Wu X.-F.;
RT   "Cloning and expression of a novel mutated osteoprogerin/osteoclastogenesis
RT   inhibitory factor gene.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:680-684(1999).
RN   [12]
RP   PROTEIN SEQUENCE OF 242-255; 354-359 AND 369-378, AND FUNCTION.
RX   PubMed=9168977; DOI=10.1006/bbrc.1997.6603;
RA   Tsuda E., Goto M., Mochizuki S., Yano K., Kobayashi F., Morinaga T.,
RA   Higashio K.;
RT   "Isolation of a novel cytokine from human fibroblasts that specifically
RT   inhibits osteoclastogenesis.";
RL   Biochem. Biophys. Res. Commun. 234:137-142(1997).
RN   [13]
RP   INTERACTION WITH TNFSF10.
RX   PubMed=9603945; DOI=10.1074/jbc.273.23.14363;
RA   Emery J.G., McDonnell P., Burke M.B., Deen K.C., Lyn S., Silverman C.,
RA   Dul E., Appelbaum E.R., Eichman C., DiPrinzio R., Dodds R.A., James I.E.,
RA   Rosenberg M., Lee J.C., Young P.R.;
RT   "Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL.";
RL   J. Biol. Chem. 273:14363-14367(1998).
RN   [14]
RP   CHARACTERIZATION, AND MUTAGENESIS OF CYS-400.
RX   PubMed=9478964; DOI=10.1074/jbc.273.9.5117;
RA   Yamaguchi K., Kinosaki M., Goto M., Kobayashi F., Tsuda E., Morinaga T.,
RA   Higashio K.;
RT   "Characterization of structural domains of human osteoclastogenesis
RT   inhibitory factor.";
RL   J. Biol. Chem. 273:5117-5123(1998).
RN   [15]
RP   REVIEW.
RX   PubMed=11505389;
RX   DOI=10.1002/1097-0142(20010801)92:3<460::aid-cncr1344>3.0.co;2-d;
RA   Hofbauer L.C., Neubauer A., Heufelder A.E.;
RT   "Receptor activator of nuclear factor-kappaB ligand and osteoprotegerin:
RT   potential implications for the pathogenesis and treatment of malignant bone
RT   diseases.";
RL   Cancer 92:460-470(2001).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-186 IN COMPLEX WITH TNFSF11,
RP   INTERACTION WITH TNFSF11, SUBUNIT, FUNCTION, MUTAGENESIS OF 78-ASP-GLU-79
RP   AND GLU-116, GLYCOSYLATION AT ASN-178, AND DISULFIDE BONDS.
RX   PubMed=22664871; DOI=10.4049/jimmunol.1103387;
RA   Luan X., Lu Q., Jiang Y., Zhang S., Wang Q., Yuan H., Zhao W., Wang J.,
RA   Wang X.;
RT   "Crystal structure of human RANKL complexed with its decoy receptor
RT   osteoprotegerin.";
RL   J. Immunol. 189:245-252(2012).
RN   [17]
RP   VARIANT PDB5 ASP-182 DEL.
RX   PubMed=12189164; DOI=10.1093/hmg/11.18.2119;
RA   Cundy T., Hegde M., Naot D., Chong B., King A., Wallace R., Mulley J.,
RA   Love D.R., Seidel J., Fawkner M., Banovic T., Callon K.E., Grey A.B.,
RA   Reid I.R., Middleton-Hardie C.A., Cornish J.;
RT   "A mutation in the gene TNFRSF11B encoding osteoprotegerin causes an
RT   idiopathic hyperphosphatasia phenotype.";
RL   Hum. Mol. Genet. 11:2119-2127(2002).
CC   -!- FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby
CC       neutralizes its function in osteoclastogenesis. Inhibits the activation
CC       of osteoclasts and promotes osteoclast apoptosis in vitro. Bone
CC       homeostasis seems to depend on the local ratio between TNFSF11 and
CC       TNFRSF11B. May also play a role in preventing arterial calcification.
CC       May act as decoy receptor for TNFSF10/TRAIL and protect against
CC       apoptosis. TNFSF10/TRAIL binding blocks the inhibition of
CC       osteoclastogenesis. {ECO:0000269|PubMed:22664871,
CC       ECO:0000269|PubMed:9168977}.
CC   -!- SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11.
CC       {ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9603945}.
CC   -!- INTERACTION:
CC       O00300; P42858: HTT; NbExp=3; IntAct=EBI-15481185, EBI-466029;
CC       O00300; P49768-2: PSEN1; NbExp=3; IntAct=EBI-15481185, EBI-11047108;
CC       O00300; O14788: TNFSF11; NbExp=3; IntAct=EBI-15481185, EBI-7404021;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult lung, heart, kidney,
CC       liver, spleen, thymus, prostate, ovary, small intestine, thyroid, lymph
CC       node, trachea, adrenal gland, testis, and bone marrow. Detected at very
CC       low levels in brain, placenta and skeletal muscle. Highly expressed in
CC       fetal kidney, liver and lung.
CC   -!- INDUCTION: Up-regulated by increasing calcium-concentration in the
CC       medium and estrogens. Down-regulated by glucocorticoids.
CC   -!- PTM: N-glycosylated. Contains sialic acid residues.
CC       {ECO:0000269|PubMed:22664871}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- DISEASE: Paget disease of bone 5, juvenile-onset (PDB5) [MIM:239000]:
CC       An autosomal recessive, juvenile-onset form of Paget disease, a
CC       disorder of bone remodeling characterized by increased bone turnover
CC       affecting one or more sites throughout the skeleton, primarily the
CC       axial skeleton. Osteoclastic overactivity followed by compensatory
CC       osteoblastic activity leads to a structurally disorganized mosaic of
CC       bone (woven bone), which is mechanically weaker, larger, less compact,
CC       more vascular, and more susceptible to fracture than normal adult
CC       lamellar bone. PDB5 clinical manifestations include short stature,
CC       progressive long bone deformities, fractures, vertebral collapse, skull
CC       enlargement, and hyperostosis with progressive deafness.
CC       {ECO:0000269|PubMed:12189164}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42610/TNFRSF11B";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tnfrsf11b/";
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DR   EMBL; U94332; AAB53709.1; -; mRNA.
DR   EMBL; AB002146; BAA25910.1; -; mRNA.
DR   EMBL; AB008822; BAA32076.1; -; Genomic_DNA.
DR   EMBL; AK313710; BAG36455.1; -; mRNA.
DR   EMBL; AK223155; BAD96875.1; -; mRNA.
DR   EMBL; AY466112; AAR23265.1; -; Genomic_DNA.
DR   EMBL; AC107953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP004283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030155; AAH30155.1; -; mRNA.
DR   EMBL; AF134187; AAF20168.1; -; mRNA.
DR   CCDS; CCDS6326.1; -.
DR   RefSeq; NP_002537.3; NM_002546.3.
DR   PDB; 3URF; X-ray; 2.70 A; Z=22-186.
DR   PDBsum; 3URF; -.
DR   AlphaFoldDB; O00300; -.
DR   SMR; O00300; -.
DR   BioGRID; 111028; 5.
DR   ComplexPortal; CPX-4663; Osteoprotegerin complex.
DR   IntAct; O00300; 4.
DR   STRING; 9606.ENSP00000297350; -.
DR   GlyConnect; 2947; 15 N-Linked glycans (2 sites).
DR   GlyCosmos; O00300; 5 sites, 23 glycans.
DR   GlyGen; O00300; 6 sites, 23 N-linked glycans (2 sites).
DR   iPTMnet; O00300; -.
DR   PhosphoSitePlus; O00300; -.
DR   BioMuta; TNFRSF11B; -.
DR   jPOST; O00300; -.
DR   MassIVE; O00300; -.
DR   PaxDb; 9606-ENSP00000297350; -.
DR   PeptideAtlas; O00300; -.
DR   ProteomicsDB; 47829; -.
DR   Antibodypedia; 13632; 885 antibodies from 43 providers.
DR   DNASU; 4982; -.
DR   Ensembl; ENST00000297350.9; ENSP00000297350.4; ENSG00000164761.9.
DR   GeneID; 4982; -.
DR   KEGG; hsa:4982; -.
DR   MANE-Select; ENST00000297350.9; ENSP00000297350.4; NM_002546.4; NP_002537.3.
DR   UCSC; uc003yon.5; human.
DR   AGR; HGNC:11909; -.
DR   CTD; 4982; -.
DR   DisGeNET; 4982; -.
DR   GeneCards; TNFRSF11B; -.
DR   HGNC; HGNC:11909; TNFRSF11B.
DR   HPA; ENSG00000164761; Group enriched (kidney, thyroid gland).
DR   MalaCards; TNFRSF11B; -.
DR   MIM; 239000; phenotype.
DR   MIM; 602643; gene.
DR   neXtProt; NX_O00300; -.
DR   OpenTargets; ENSG00000164761; -.
DR   Orphanet; 1416; Familial calcium pyrophosphate deposition.
DR   Orphanet; 2801; Juvenile Paget disease.
DR   PharmGKB; PA36602; -.
DR   VEuPathDB; HostDB:ENSG00000164761; -.
DR   eggNOG; ENOG502QVRT; Eukaryota.
DR   GeneTree; ENSGT00940000155167; -.
DR   HOGENOM; CLU_057708_0_0_1; -.
DR   InParanoid; O00300; -.
DR   OMA; CENGVQR; -.
DR   OrthoDB; 5348767at2759; -.
DR   PhylomeDB; O00300; -.
DR   TreeFam; TF331157; -.
DR   PathwayCommons; O00300; -.
DR   Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR   SignaLink; O00300; -.
DR   SIGNOR; O00300; -.
DR   BioGRID-ORCS; 4982; 11 hits in 1153 CRISPR screens.
DR   ChiTaRS; TNFRSF11B; human.
DR   GeneWiki; Osteoprotegerin; -.
DR   GenomeRNAi; 4982; -.
DR   Pharos; O00300; Tbio.
DR   PRO; PR:O00300; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; O00300; Protein.
DR   Bgee; ENSG00000164761; Expressed in cartilage tissue and 127 other cell types or tissues.
DR   ExpressionAtlas; O00300; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; TAS:ProtInc.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR   GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR   GO; GO:0042489; P:negative regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:ComplexPortal.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   CDD; cd01670; Death; 1.
DR   CDD; cd10581; TNFRSF11B; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR022323; TNFR_11.
DR   InterPro; IPR017371; TNFR_11B.
DR   PANTHER; PTHR23097; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER; 1.
DR   PANTHER; PTHR23097:SF90; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 11B; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00020; TNFR_c6; 4.
DR   PIRSF; PIRSF038065; TNFR_11B; 1.
DR   PRINTS; PR01961; TNFACTORR11.
DR   PRINTS; PR01975; TNFACTORR11B.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM01411; Ephrin_rec_like; 2.
DR   SMART; SM00208; TNFR; 4.
DR   SUPFAM; SSF47986; DEATH domain; 2.
DR   SUPFAM; SSF57586; TNF receptor-like; 2.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 2.
DR   Genevisible; O00300; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Direct protein sequencing; Disease variant;
KW   Disulfide bond; Glycoprotein; Receptor; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15340161,
FT                   ECO:0000269|PubMed:9571159"
FT   CHAIN           22..401
FT                   /note="Tumor necrosis factor receptor superfamily member
FT                   11B"
FT                   /id="PRO_0000034587"
FT   REPEAT          24..62
FT                   /note="TNFR-Cys 1"
FT   REPEAT          65..105
FT                   /note="TNFR-Cys 2"
FT   REPEAT          107..142
FT                   /note="TNFR-Cys 3"
FT   REPEAT          145..185
FT                   /note="TNFR-Cys 4"
FT   DOMAIN          198..269
FT                   /note="Death 1"
FT   DOMAIN          270..365
FT                   /note="Death 2"
FT   SITE            400
FT                   /note="Involved in dimerization"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22664871"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        44..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        65..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        83..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        87..105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        107..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        124..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        145..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   DISULFID        166..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT                   ECO:0000269|PubMed:22664871"
FT   VARIANT         3
FT                   /note="N -> K (in dbSNP:rs2073618)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:9108485, ECO:0000269|PubMed:9492069,
FT                   ECO:0000269|PubMed:9688283, ECO:0000269|Ref.6"
FT                   /id="VAR_013439"
FT   VARIANT         104
FT                   /note="V -> M (in dbSNP:rs11573906)"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="VAR_018957"
FT   VARIANT         182
FT                   /note="Missing (in PDB5; dbSNP:rs796051868)"
FT                   /evidence="ECO:0000269|PubMed:12189164"
FT                   /id="VAR_019413"
FT   MUTAGEN         78..79
FT                   /note="DE->AA: Decreases inhibition of osteoclast
FT                   differentiation."
FT                   /evidence="ECO:0000269|PubMed:22664871"
FT   MUTAGEN         116
FT                   /note="E->A: Reduces affinity for TNFSF11. Decreases
FT                   inhibition of osteoclast differentiation."
FT                   /evidence="ECO:0000269|PubMed:22664871"
FT   MUTAGEN         400..401
FT                   /note="Missing: Abolishes dimerization."
FT   MUTAGEN         400
FT                   /note="C->S: Abolishes dimerization."
FT                   /evidence="ECO:0000269|PubMed:9478964"
FT   CONFLICT        263
FT                   /note="D -> A (in Ref. 1; AAB53709)"
FT                   /evidence="ECO:0000305"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          48..52
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:3URF"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:3URF"
SQ   SEQUENCE   401 AA;  46026 MW;  2A23AC07BFA1E2DE CRC64;
     MNNLLCCALV FLDISIKWTT QETFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT
     VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK
     HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT
     HDNICSGNSE STQKCGIDVT LCEEAFFRFA VPTKFTPNWL SVLVDNLPGT KVNAESVERI
     KRQHSSQEQT FQLLKLWKHQ NKDQDIVKKI IQDIDLCENS VQRHIGHANL TFEQLRSLME
     SLPGKKVGAE DIEKTIKACK PSDQILKLLS LWRIKNGDQD TLKGLMHALK HSKTYHFPKT
     VTQSLKKTIR FLHSFTMYKL YQKLFLEMIG NQVQSVKISC L
//