TR11B_MOUSE
ID TR11B_MOUSE Reviewed; 401 AA.
AC O08712; O70202;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 166.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; 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 [GENOMIC DNA / MRNA], AND VARIANTS PRO-138; ARG-161;
RP ASP-165; ALA-288 AND ARG-296.
RC STRAIN=129/Ola, and NIH Swiss; TISSUE=Fibroblast;
RX PubMed=9714833; DOI=10.1016/s0378-1119(98)00295-9;
RA Mizuno A., Murakami A., Nakagawa N., Yasuda H., Tsuda E., Morinaga T.,
RA Higashio K.;
RT "Structure of the mouse osteoclastogenesis inhibitory factor (OCIF) gene
RT and its expression in embryogenesis.";
RL Gene 215:339-343(1998).
RN [3]
RP FUNCTION.
RX PubMed=10952716; DOI=10.1084/jem.192.4.463;
RA Min H., Morony S., Sarosi I., Dunstan C.R., Capparelli C., Scully S.,
RA Van G., Kaufman S., Kostenuik P.J., Lacey D.L., Boyle W.J., Simonet W.S.;
RT "Osteoprotegerin reverses osteoporosis by inhibiting endosteal osteoclasts
RT and prevents vascular calcification by blocking a process resembling
RT osteoclastogenesis.";
RL J. Exp. Med. 192:463-474(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-197 IN COMPLEX WITH
RP TNFSF11/RANKL, AND DISULFIDE BONDS.
RX PubMed=23039992; DOI=10.1016/j.str.2012.08.030;
RA Nelson C.A., Warren J.T., Wang M.W., Teitelbaum S.L., Fremont D.H.;
RT "RANKL employs distinct binding modes to engage RANK and the
RT osteoprotegerin decoy receptor.";
RL Structure 20:1971-1982(2012).
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:10952716}.
CC -!- SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11.
CC {ECO:0000269|PubMed:23039992}.
CC -!- INTERACTION:
CC O08712; O35235-1: Tnfsf11; NbExp=4; IntAct=EBI-16015871, EBI-15890886;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, lung, stomach,
CC intestines and calvaria. Highly expressed in decidua and placenta, and
CC in embryo.
CC -!- DEVELOPMENTAL STAGE: Detected in embryo at high levels on day 7,
CC whereas expression decreases at day 11 and increases from day 15 to 17.
CC On day 15 found in developing bone primordia, brachiocephalic artery
CC and ductus arteriosus, left main bronchus, abdominal aorta and midgut.
CC -!- INDUCTION: Up-regulated by TGF-beta and estrogens. Down-regulated by
CC 1,25-dihdroxyvitamin D3 and parathyroid hormone.
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DR EMBL; U94331; AAB53708.1; -; mRNA.
DR EMBL; AB013898; BAA28269.1; -; mRNA.
DR EMBL; AB013903; BAA33388.1; -; Genomic_DNA.
DR CCDS; CCDS27468.1; -.
DR RefSeq; NP_032790.3; NM_008764.3.
DR PDB; 4E4D; X-ray; 2.70 A; R=22-197.
DR PDBsum; 4E4D; -.
DR AlphaFoldDB; O08712; -.
DR SMR; O08712; -.
DR ComplexPortal; CPX-4763; Osteoprotegerin complex.
DR DIP; DIP-59980N; -.
DR IntAct; O08712; 1.
DR STRING; 10090.ENSMUSP00000078705; -.
DR GlyGen; O08712; 4 sites.
DR PhosphoSitePlus; O08712; -.
DR PaxDb; O08712; -.
DR PRIDE; O08712; -.
DR ProteomicsDB; 258833; -.
DR Antibodypedia; 13632; 795 antibodies from 43 providers.
DR DNASU; 18383; -.
DR Ensembl; ENSMUST00000079772; ENSMUSP00000078705; ENSMUSG00000063727.
DR GeneID; 18383; -.
DR KEGG; mmu:18383; -.
DR UCSC; uc007vrk.1; mouse.
DR CTD; 4982; -.
DR MGI; MGI:109587; Tnfrsf11b.
DR VEuPathDB; HostDB:ENSMUSG00000063727; -.
DR eggNOG; ENOG502QVRT; Eukaryota.
DR GeneTree; ENSGT00940000155167; -.
DR HOGENOM; CLU_057708_0_0_1; -.
DR InParanoid; O08712; -.
DR OMA; KFLCCTL; -.
DR OrthoDB; 869160at2759; -.
DR PhylomeDB; O08712; -.
DR TreeFam; TF331157; -.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR BioGRID-ORCS; 18383; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tnfrsf11b; mouse.
DR PRO; PR:O08712; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O08712; protein.
DR Bgee; ENSMUSG00000063727; Expressed in decidua and 158 other tissues.
DR ExpressionAtlas; O08712; baseline and differential.
DR Genevisible; O08712; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IC:ComplexPortal.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISO:MGI.
DR GO; GO:0042489; P:negative regulation of odontogenesis of dentin-containing tooth; IDA:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA: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; IEA:InterPro.
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; 2.
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; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Disulfide bond; Glycoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..401
FT /note="Tumor necrosis factor receptor superfamily member
FT 11B"
FT /id="PRO_0000034588"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT DOMAIN 283..365
FT /note="Death 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT SITE 400
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT CARBOHYD 98
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:0000255"
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:23039992"
FT DISULFID 44..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 65..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 83..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 87..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 107..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 124..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 145..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT DISULFID 166..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0000269|PubMed:23039992"
FT VARIANT 138
FT /note="R -> P (in strain: 129/Ola and NIH Swiss)"
FT /evidence="ECO:0000269|PubMed:9714833"
FT VARIANT 161
FT /note="I -> R (in strain: 129/Ola and NIH Swiss)"
FT /evidence="ECO:0000269|PubMed:9714833"
FT VARIANT 165
FT /note="N -> D (in strain: 129/Ola and NIH Swiss)"
FT /evidence="ECO:0000269|PubMed:9714833"
FT VARIANT 288
FT /note="S -> A (in strain: 129/Ola and NIH Swiss)"
FT /evidence="ECO:0000269|PubMed:9714833"
FT VARIANT 296
FT /note="L -> R (in strain: 129/Ola and NIH Swiss)"
FT /evidence="ECO:0000269|PubMed:9714833"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4E4D"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:4E4D"
SQ SEQUENCE 401 AA; 45923 MW; CAA6102D3B312470 CRC64;
MNKWLCCALL VLLDIIEWTT QETLPPKYLH YDPETGHQLL CDKCAPGTYL KQHCTVRRKT
LCVPCPDHSY TDSWHTSDEC VYCSPVCKEL QSVKQECNRT HNRVCECEEG RYLEIEFCLK
HRSCPPGSGV VQAGTPERNT VCKKCPDGFF SGETSSKAPC IKHTNCSTFG LLLIQKGNAT
HDNVCSGNRE ATQKCGIDVT LCEEAFFRFA VPTKIIPNWL SVLVDSLPGT KVNAESVERI
KRRHSSQEQT FQLLKLWKHQ NRDQEMVKKI IQDIDLCESS VQRHLGHSNL TTEQLLALME
SLPGKKISPE EIERTRKTCK SSEQLLKLLS LWRIKNGDQD TLKGLMYALK HLKTSHFPKT
VTHSLRKTMR FLHSFTMYRL YQKLFLEMIG NQVQSVKISC L
