TR11B_HUMAN
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 03-AUG-2022, entry version 180.
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 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="http://atlasgeneticsoncology.org/Genes/TNFRSF11BID42610ch8q24.html";
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 GlyGen; O00300; 6 sites, 18 N-linked glycans (2 sites).
DR iPTMnet; O00300; -.
DR PhosphoSitePlus; O00300; -.
DR BioMuta; TNFRSF11B; -.
DR jPOST; O00300; -.
DR MassIVE; O00300; -.
DR PaxDb; O00300; -.
DR PeptideAtlas; O00300; -.
DR PRIDE; O00300; -.
DR ProteomicsDB; 47829; -.
DR Antibodypedia; 13632; 795 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 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; KFLCCTL; -.
DR OrthoDB; 358120at2759; -.
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; 9 hits in 1073 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 126 other tissues.
DR ExpressionAtlas; O00300; baseline and differential.
DR Genevisible; O00300; HS.
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; IEA:Ensembl.
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 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; IPR022323; TNFR_11.
DR InterPro; IPR017371; TNFR_11B.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 3.
DR PIRSF; PIRSF038065; TNFR_11B; 1.
DR PRINTS; PR01961; TNFACTORR11.
DR PRINTS; PR01975; TNFACTORR11B.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 4.
DR SUPFAM; SSF47986; SSF47986; 2.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
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
