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Tumor necrosis factor receptor superfamily member 11B (Osteoclastogenesis inhibitory factor) (Osteoprotegerin)

 TR11B_HUMAN             Reviewed;         401 AA.
O00300; B2R9A8; O60236; Q53FX6; Q9UHP4;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 3.
13-FEB-2019, entry version 163.
RecName: Full=Tumor necrosis factor receptor superfamily member 11B;
AltName: Full=Osteoclastogenesis inhibitory factor;
AltName: Full=Osteoprotegerin;
Flags: Precursor;
Name=TNFRSF11B; Synonyms=OCIF, OPG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-3.
TISSUE=Kidney;
PubMed=9108485; DOI=10.1016/S0092-8674(00)80209-3;
Simonet W.S., Lacey D.L., Dunstan C.R., Kelley M., Chang M.-S.,
Luethy R., Nguyen H.Q., Wooden S., Bennett L., Boone T., Shimamoto G.,
Derose M., Elliott R., Colombero A., Tan H.-L., Trail G., Sullivan J.,
Davy E., Bucay N., Renshaw-Gegg L., Hughes T.M., Hill D., Pattison W.,
Campbell P., Sander S., Van G., Tarpley J., Derby P., Lee R.,
Suggs S., Boyle W.J.;
"Osteoprotegerin: a novel secreted protein involved in the regulation
of bone density.";
Cell 89:309-319(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-3.
TISSUE=Lung cancer;
PubMed=9492069; DOI=10.1210/endo.139.3.5837;
Yasuda H., Shima N., Nakagawa N., Mochizuki S., Yano K., Fujise N.,
Sato Y., Goto M., Yamaguchi K., Kuriyama M., Kanno T., Murakami A.,
Tsuda E., Morinaga T., Higashio K.;
"Identity of osteoclastogenesis inhibitory factor (OCIF) and
osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits
osteoclastogenesis in vitro.";
Endocrinology 139:1329-1337(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-3.
TISSUE=Placenta;
PubMed=9688283; DOI=10.1046/j.1432-1327.1998.2540685.x;
Morinaga T., Nakagawa N., Yasuda H., Tsuda E., Higashio K.;
"Cloning and characterization of the gene encoding human
osteoprotegerin/osteoclastogenesis-inhibitory factor.";
Eur. J. Biochem. 254:685-691(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-3.
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-3 AND MET-104.
NIEHS SNPs program;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 22-36 AND 378-401.
PubMed=9571159; DOI=10.1006/bbrc.1998.8443;
Tomoyasu A., Goto M., Fujise N., Mochizuki S., Yasuda H., Morinaga T.,
Tsuda E., Higashio K.;
"Characterization of monomeric and homodimeric forms of
osteoclastogenesis inhibitory factor.";
Biochem. Biophys. Res. Commun. 245:382-387(1998).
[10]
PROTEIN SEQUENCE OF 22-36.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-393.
TISSUE=Placenta;
PubMed=12110935;
He Z.-Y., Yang G.-Z., Zhang W.-J., Wu X.-F.;
"Cloning and expression of a novel mutated
osteoprogerin/osteoclastogenesis inhibitory factor gene.";
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 31:680-684(1999).
[12]
PROTEIN SEQUENCE OF 242-255; 354-359 AND 369-378, AND FUNCTION.
PubMed=9168977; DOI=10.1006/bbrc.1997.6603;
Tsuda E., Goto M., Mochizuki S., Yano K., Kobayashi F., Morinaga T.,
Higashio K.;
"Isolation of a novel cytokine from human fibroblasts that
specifically inhibits osteoclastogenesis.";
Biochem. Biophys. Res. Commun. 234:137-142(1997).
[13]
INTERACTION WITH TNFSF10.
PubMed=9603945; DOI=10.1074/jbc.273.23.14363;
Emery J.G., McDonnell P., Burke M.B., Deen K.C., Lyn S., Silverman C.,
Dul E., Appelbaum E.R., Eichman C., DiPrinzio R., Dodds R.A.,
James I.E., Rosenberg M., Lee J.C., Young P.R.;
"Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL.";
J. Biol. Chem. 273:14363-14367(1998).
[14]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-400.
PubMed=9478964; DOI=10.1074/jbc.273.9.5117;
Yamaguchi K., Kinosaki M., Goto M., Kobayashi F., Tsuda E.,
Morinaga T., Higashio K.;
"Characterization of structural domains of human osteoclastogenesis
inhibitory factor.";
J. Biol. Chem. 273:5117-5123(1998).
[15]
REVIEW.
PubMed=11505389;
DOI=10.1002/1097-0142(20010801)92:3<460::AID-CNCR1344>3.0.CO;2-D;
Hofbauer L.C., Neubauer A., Heufelder A.E.;
"Receptor activator of nuclear factor-kappaB ligand and
osteoprotegerin: potential implications for the pathogenesis and
treatment of malignant bone diseases.";
Cancer 92:460-470(2001).
[16]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-186 IN COMPLEX WITH
TNFSF11, INTERACTION WITH TNFSF11, SUBUNIT, FUNCTION, MUTAGENESIS OF
78-ASP-GLU-79 AND GLU-116, GLYCOSYLATION AT ASN-178, AND DISULFIDE
BONDS.
PubMed=22664871; DOI=10.4049/jimmunol.1103387;
Luan X., Lu Q., Jiang Y., Zhang S., Wang Q., Yuan H., Zhao W.,
Wang J., Wang X.;
"Crystal structure of human RANKL complexed with its decoy receptor
osteoprotegerin.";
J. Immunol. 189:245-252(2012).
[17]
VARIANT PDB5 ASP-182 DEL.
PubMed=12189164; DOI=10.1093/hmg/11.18.2119;
Cundy T., Hegde M., Naot D., Chong B., King A., Wallace R., Mulley J.,
Love D.R., Seidel J., Fawkner M., Banovic T., Callon K.E., Grey A.B.,
Reid I.R., Middleton-Hardie C.A., Cornish J.;
"A mutation in the gene TNFRSF11B encoding osteoprotegerin causes an
idiopathic hyperphosphatasia phenotype.";
Hum. Mol. Genet. 11:2119-2127(2002).
-!- FUNCTION: Acts as decoy receptor for TNFSF11/RANKL and thereby
neutralizes its function in osteoclastogenesis. Inhibits the
activation of osteoclasts and promotes osteoclast apoptosis in
vitro. Bone homeostasis seems to depend on the local ratio between
TNFSF11 and TNFRSF11B. May also play a role in preventing arterial
calcification. May act as decoy receptor for TNFSF10/TRAIL and
protect against apoptosis. TNFSF10/TRAIL binding blocks the
inhibition of osteoclastogenesis. {ECO:0000269|PubMed:22664871,
ECO:0000269|PubMed:9168977}.
-!- SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11.
{ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9603945}.
-!- INTERACTION:
O14788:TNFSF11; NbExp=3; IntAct=EBI-15481185, EBI-7404021;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Highly expressed in adult lung, heart, kidney,
liver, spleen, thymus, prostate, ovary, small intestine, thyroid,
lymph node, trachea, adrenal gland, testis, and bone marrow.
Detected at very low levels in brain, placenta and skeletal
muscle. Highly expressed in fetal kidney, liver and lung.
-!- INDUCTION: Up-regulated by increasing calcium-concentration in the
medium and estrogens. Down-regulated by glucocorticoids.
-!- PTM: N-glycosylated. Contains sialic acid residues.
{ECO:0000269|PubMed:22664871}.
-!- PTM: The N-terminus is blocked.
-!- DISEASE: Paget disease of bone 5, juvenile-onset (PDB5)
[MIM:239000]: An autosomal recessive, juvenile-onset form of Paget
disease, a disorder of bone remodeling characterized by increased
bone turnover affecting one or more sites throughout the skeleton,
primarily the axial skeleton. Osteoclastic overactivity followed
by compensatory osteoblastic activity leads to a structurally
disorganized mosaic of bone (woven bone), which is mechanically
weaker, larger, less compact, more vascular, and more susceptible
to fracture than normal adult lamellar bone. PDB5 clinical
manifestations include short stature, progressive long bone
deformities, fractures, vertebral collapse, skull enlargement, and
hyperostosis with progressive deafness.
{ECO:0000269|PubMed:12189164}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TNFRSF11BID42610ch8q24.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tnfrsf11b/";
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EMBL; U94332; AAB53709.1; -; mRNA.
EMBL; AB002146; BAA25910.1; -; mRNA.
EMBL; AB008822; BAA32076.1; -; Genomic_DNA.
EMBL; AK313710; BAG36455.1; -; mRNA.
EMBL; AK223155; BAD96875.1; -; mRNA.
EMBL; AY466112; AAR23265.1; -; Genomic_DNA.
EMBL; AC107953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP004283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030155; AAH30155.1; -; mRNA.
EMBL; AF134187; AAF20168.1; -; mRNA.
CCDS; CCDS6326.1; -.
RefSeq; NP_002537.3; NM_002546.3.
UniGene; Hs.81791; -.
PDB; 3URF; X-ray; 2.70 A; Z=22-186.
PDBsum; 3URF; -.
ProteinModelPortal; O00300; -.
SMR; O00300; -.
BioGrid; 111028; 2.
IntAct; O00300; 2.
STRING; 9606.ENSP00000297350; -.
iPTMnet; O00300; -.
PhosphoSitePlus; O00300; -.
BioMuta; TNFRSF11B; -.
jPOST; O00300; -.
PaxDb; O00300; -.
PeptideAtlas; O00300; -.
PRIDE; O00300; -.
ProteomicsDB; 47829; -.
Ensembl; ENST00000297350; ENSP00000297350; ENSG00000164761.
GeneID; 4982; -.
KEGG; hsa:4982; -.
UCSC; uc003yon.5; human.
CTD; 4982; -.
DisGeNET; 4982; -.
EuPathDB; HostDB:ENSG00000164761.8; -.
GeneCards; TNFRSF11B; -.
H-InvDB; HIX0007748; -.
HGNC; HGNC:11909; TNFRSF11B.
HPA; CAB034939; -.
MalaCards; TNFRSF11B; -.
MIM; 239000; phenotype.
MIM; 602643; gene.
neXtProt; NX_O00300; -.
OpenTargets; ENSG00000164761; -.
Orphanet; 2801; Juvenile Paget disease.
PharmGKB; PA36602; -.
eggNOG; ENOG410IFEM; Eukaryota.
eggNOG; ENOG4111PUQ; LUCA.
GeneTree; ENSGT00940000155167; -.
HOGENOM; HOG000273896; -.
HOVERGEN; HBG061495; -.
InParanoid; O00300; -.
KO; K05148; -.
OMA; SRQLMCD; -.
OrthoDB; 358120at2759; -.
PhylomeDB; O00300; -.
TreeFam; TF331157; -.
Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
SIGNOR; O00300; -.
ChiTaRS; TNFRSF11B; human.
GeneWiki; Osteoprotegerin; -.
GenomeRNAi; 4982; -.
PRO; PR:O00300; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164761; Expressed in 159 organ(s), highest expression level in tendon of biceps brachii.
ExpressionAtlas; O00300; baseline and differential.
Genevisible; O00300; HS.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:ProtInc.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005125; F:cytokine activity; TAS:ProtInc.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
GO; GO:0042489; P:negative regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR022323; TNFR_11.
InterPro; IPR017371; TNFR_11B.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 3.
PIRSF; PIRSF038065; TNFR_11B; 1.
PRINTS; PR01961; TNFACTORR11.
PRINTS; PR01975; TNFACTORR11B.
SMART; SM00005; DEATH; 1.
SMART; SM01411; Ephrin_rec_like; 2.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 2.
PROSITE; PS00652; TNFR_NGFR_1; 1.
PROSITE; PS50050; TNFR_NGFR_2; 2.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:9571159}.
CHAIN 22 401 Tumor necrosis factor receptor
superfamily member 11B.
/FTId=PRO_0000034587.
REPEAT 24 62 TNFR-Cys 1.
REPEAT 65 105 TNFR-Cys 2.
REPEAT 107 142 TNFR-Cys 3.
REPEAT 145 185 TNFR-Cys 4.
DOMAIN 198 269 Death 1.
DOMAIN 270 365 Death 2.
SITE 400 400 Involved in dimerization.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22664871}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 41 54 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 44 62 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 65 80 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 83 97 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 87 105 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 107 118 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 124 142 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 145 160 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
DISULFID 166 185 {ECO:0000255|PROSITE-ProRule:PRU00206,
ECO:0000269|PubMed:22664871}.
VARIANT 3 3 N -> K (in dbSNP:rs2073618).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:9108485,
ECO:0000269|PubMed:9492069,
ECO:0000269|PubMed:9688283,
ECO:0000269|Ref.6}.
/FTId=VAR_013439.
VARIANT 104 104 V -> M (in dbSNP:rs11573906).
{ECO:0000269|Ref.6}.
/FTId=VAR_018957.
VARIANT 182 182 Missing (in PDB5).
{ECO:0000269|PubMed:12189164}.
/FTId=VAR_019413.
MUTAGEN 78 79 DE->AA: Decreases inhibition of
osteoclast differentiation.
{ECO:0000269|PubMed:22664871}.
MUTAGEN 116 116 E->A: Reduces affinity for TNFSF11.
Decreases inhibition of osteoclast
differentiation.
{ECO:0000269|PubMed:22664871}.
MUTAGEN 400 401 Missing: Abolishes dimerization.
MUTAGEN 400 400 C->S: Abolishes dimerization.
{ECO:0000269|PubMed:9478964}.
CONFLICT 263 263 D -> A (in Ref. 1; AAB53709).
{ECO:0000305}.
STRAND 29 31 {ECO:0000244|PDB:3URF}.
STRAND 35 37 {ECO:0000244|PDB:3URF}.
STRAND 40 42 {ECO:0000244|PDB:3URF}.
STRAND 48 52 {ECO:0000244|PDB:3URF}.
STRAND 56 58 {ECO:0000244|PDB:3URF}.
STRAND 61 64 {ECO:0000244|PDB:3URF}.
STRAND 91 95 {ECO:0000244|PDB:3URF}.
STRAND 99 101 {ECO:0000244|PDB:3URF}.
STRAND 104 107 {ECO:0000244|PDB:3URF}.
STRAND 111 114 {ECO:0000244|PDB:3URF}.
STRAND 117 120 {ECO:0000244|PDB:3URF}.
STRAND 128 132 {ECO:0000244|PDB:3URF}.
STRAND 136 138 {ECO:0000244|PDB:3URF}.
STRAND 141 144 {ECO:0000244|PDB:3URF}.
STRAND 155 157 {ECO:0000244|PDB:3URF}.
STRAND 167 171 {ECO:0000244|PDB:3URF}.
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


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Pathways :
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1983: Splicing factor NOVA regulated synpatic proteins
WP2148: Brain derived neurotrophic factor
WP272: Blood Clotting Cascade
WP1004: Kit Receptor Signaling Pathway
WP1011: T Cell Receptor Signaling Pathway
WP1014: Androgen receptor signaling pathway
WP1025: B Cell Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1067: Toll-like receptor signaling pathway
WP1112: EPO Receptor Signaling
WP1121: Kit Receptor Signaling Pathway
WP1130: T Cell Receptor Signaling Pathway

Related Genes :
[TNFRSF11B OCIF OPG] Tumor necrosis factor receptor superfamily member 11B (Osteoclastogenesis inhibitory factor) (Osteoprotegerin)
[Tnfsf11 Opgl Rankl Trance] Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form]
[TNFSF11 OPGL RANKL TRANCE] Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form]
[ZFP36L1 BERG36 BRF1 ERF1 RNF162B TIS11B] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-response factor 1) (ERF-1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[Zfp36l1 Brf1 Tis11b] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[Zfp36l1 Brf1 Cmg1 Tis11b] mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-inducible protein CMG1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)
[Faslg Apt1Lg1 Cd95l Fasl Tnfsf6] Tumor necrosis factor ligand superfamily member 6 (CD95 ligand) (CD95-L) (Fas antigen ligand) (Fas ligand) (FasL) (CD antigen CD178) [Cleaved into: Tumor necrosis factor ligand superfamily member 6, membrane form; Tumor necrosis factor ligand superfamily member 6, soluble form (Receptor-binding FasL ectodomain) (Soluble Fas ligand) (sFasL); ADAM10-processed FasL form (APL); FasL intracellular domain (FasL ICD) (SPPL2A-processed FasL form) (SPA)]
[PEX11B] Peroxisomal membrane protein 11B (Peroxin-11B) (Peroxisomal biogenesis factor 11B) (Protein PEX11 homolog beta) (PEX11-beta)
[TNFSF13B BAFF BLYS TALL1 TNFSF20 ZTNF4 UNQ401/PRO738] Tumor necrosis factor ligand superfamily member 13B (B lymphocyte stimulator) (BLyS) (B-cell-activating factor) (BAFF) (Dendritic cell-derived TNF-like molecule) (TNF- and APOL-related leukocyte expressed ligand 1) (TALL-1) (CD antigen CD257) [Cleaved into: Tumor necrosis factor ligand superfamily member 13b, membrane form; Tumor necrosis factor ligand superfamily member 13b, soluble form]
[ITGAM CD11B CR3A] Integrin alpha-M (CD11 antigen-like family member B) (CR-3 alpha chain) (Cell surface glycoprotein MAC-1 subunit alpha) (Leukocyte adhesion receptor MO1) (Neutrophil adherence receptor) (CD antigen CD11b)
[TNFRSF14 HVEA HVEM UNQ329/PRO509] Tumor necrosis factor receptor superfamily member 14 (Herpes virus entry mediator A) (Herpesvirus entry mediator A) (HveA) (Tumor necrosis factor receptor-like 2) (TR2) (CD antigen CD270)
[TNFSF14 HVEML LIGHT UNQ391/PRO726] Tumor necrosis factor ligand superfamily member 14 (Herpes virus entry mediator ligand) (HVEM-L) (Herpesvirus entry mediator ligand) (CD antigen CD258) [Cleaved into: Tumor necrosis factor ligand superfamily member 14, membrane form; Tumor necrosis factor ligand superfamily member 14, soluble form]
[CDK11B CDC2L1 CDK11 PITSLREA PK58] Cyclin-dependent kinase 11B (EC 2.7.11.22) (Cell division cycle 2-like protein kinase 1) (CLK-1) (Cell division protein kinase 11B) (Galactosyltransferase-associated protein kinase p58/GTA) (PITSLRE serine/threonine-protein kinase CDC2L1) (p58 CLK-1)
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[TNFRSF11A RANK] Tumor necrosis factor receptor superfamily member 11A (Osteoclast differentiation factor receptor) (ODFR) (Receptor activator of NF-KB) (CD antigen CD265)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[Tnfrsf14 hvem] Tumor necrosis factor receptor superfamily member 14 (Herpes virus entry mediator A) (Herpesvirus entry mediator A) (HveA) (Tumor necrosis factor receptor-like 2) (TR2) (CD antigen CD270)
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[dop Acel_1186] Depupylase (EC 3.4.-.-)
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[] Bradykinin-potentiating and C-type natriuretic peptides (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide 6a (BPP-6a); Bradykinin-potentiating peptide 10a (BPP-10a) (Bradykinin-potentiating peptide IV-1-A) (BPPIV-1-A) (Bradykinin-potentiating peptide V-8); Bradykinin-potentiating peptide 13a+QQWA (BPP-13a+QQWA); Bradykinin-potentiating peptide 13a+QWA (BPP-13a+QWA); Bradykinin-potentiating peptide 13a (BPP-13a) (Bradykinin-potentiating peptide III-1-A) (III-1-A) (Bradykinin-potentiating peptide V-9); Bradykinin-potentiating peptide 10c+QQWA (BPP-10c+QQWA); Bradykinin-potentiating peptide 10c (BPP-10c) (BPP-2) (Bradykinin-potentiating peptide IV-1-Bbeta) (BPP IV-1-Bbeta) (Bradykinin-potentiating peptide V-7); Bradykinin-potentiating peptide 10c-F (BPP-10c-F); Bradykinin-potentiating peptide 11b (BPP-11b) (Bradykinin-potentiating peptide IIa) (BPP-IIa); Bradykinin-potentiating peptide IIb (BPP-IIb); Bradykinin-potentiating peptide 5a (BPP-5a) (Bradykinin-potentiating peptide Va) (BPPVa) (Proline-rich peptide 5a) (Bj-PRO-5a) (PRO-5a); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (Bj-CNP)]
[Tnf Tnfa Tnfsf2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]
[TIF1 TIF41A YKR059W; TIF2 TIF41B YJL138C J0660] ATP-dependent RNA helicase eIF4A (EC 3.6.4.13) (Eukaryotic initiation factor 4A) (eIF-4A) (Stimulator factor I 37 kDa component) (Translation initiation factor 1/2) (p37)
[TNF TNFA TNFSF2] Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form]

Bibliography :
[29962255] Defective autophagy in osteoblasts induces endoplasmic reticulum stress and causes remarkable bone loss.
[29749489] Effects of osteoprotegerin/TNFRSF11B in two models of abdominal aortic aneurysms.
[29111093] Biomarkers of cerebral microembolic signals.
[27922673] Effects of miR-145 on the inhibition of chondrocyte proliferation and fibrosis by targeting TNFRSF11B in human osteoarthritis.
[27493142] Genetic determinants and postorthodontic external apical root resorption in Czech children.
[26841162] Elevated serum osteoprotegerin levels in women: friend or foe?
[24615483] Raloxifene pharmacodynamics is influenced by genetic variants in the RANKL/RANK/OPG system and in the Wnt signaling pathway.
[25520884] Rab25 Small GTPase Mediates Secretion of Tumor Necrosis Factor Receptor Superfamily Member 11b (osteoprotegerin) Protecting Cancer Cells from Effects of TRAIL.
[22296645] Tumour necrosis factor receptor superfamily member 11B polymorphisms and association with knee osteoarthritis in women.
[22079369] TNFRSF11B gene haplotype and its association with bone mineral density variations in postmenopausal Mexican-Mestizo women.
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