TR11B_RAT
ID TR11B_RAT Reviewed; 401 AA.
AC O08727;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 11B;
DE AltName: Full=Osteoprotegerin;
DE Flags: Precursor;
GN Name=Tnfrsf11b; Synonyms=Opg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic intestine;
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by osteopontin.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U94330; AAB53707.1; -; mRNA.
DR EMBL; BC081830; AAH81830.1; -; mRNA.
DR RefSeq; NP_037002.1; NM_012870.2.
DR AlphaFoldDB; O08727; -.
DR SMR; O08727; -.
DR STRING; 10116.ENSRNOP00000011344; -.
DR GlyGen; O08727; 4 sites.
DR PaxDb; O08727; -.
DR Ensembl; ENSRNOT00000011344; ENSRNOP00000011344; ENSRNOG00000008336.
DR GeneID; 25341; -.
DR KEGG; rno:25341; -.
DR UCSC; RGD:619802; rat.
DR CTD; 4982; -.
DR RGD; 619802; Tnfrsf11b.
DR eggNOG; ENOG502QVRT; Eukaryota.
DR GeneTree; ENSGT00940000155167; -.
DR HOGENOM; CLU_057708_0_0_1; -.
DR InParanoid; O08727; -.
DR OMA; KFLCCTL; -.
DR OrthoDB; 869160at2759; -.
DR PhylomeDB; O08727; -.
DR TreeFam; TF331157; -.
DR Reactome; R-RNO-5669034; TNFs bind their physiological receptors.
DR PRO; PR:O08727; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008336; Expressed in esophagus and 17 other tissues.
DR Genevisible; O08727; RN.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0045779; P:negative regulation of bone resorption; IDA:RGD.
DR GO; GO:0042489; P:negative regulation of odontogenesis of dentin-containing tooth; IEP:RGD.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytokine; Disulfide bond; Glycoprotein; Reference proteome;
KW 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_0000034589"
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 /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 DISULFID 44..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 65..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 83..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 87..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 107..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 124..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 145..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 166..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 401 AA; 46192 MW; FEC6A31F1D4E573A CRC64;
MNKWLCCALL VFLDIIEWTT QETFPPKYLH YDPETGRQLL CDKCAPGTYL KQHCTVRRKT
LCVPCPDYSY TDSWHTSDEC VYCSPVCKEL QTVKQECNRT HNRVCECEEG RYLELEFCLK
HRSCPPGLGV LQAGTPERNT VCKRCPDGFF SGETSSKAPC RKHTNCSSLG LLLIQKGNAT
HDNVCSGNRE ATQNCGIDVT LCEEAFFRFA VPTKIIPNWL SVLVDSLPGT KVNAESVERI
KRRHSSQEQT FQLLKLWKHQ NRDQEMVKKI IQDIDLCESS VQRHIGHANL TTEQLRILME
SLPGKKISPD EIERTRKTCK PSEQLLKLLS LWRIKNGDQD TLKGLMYALK HLKAYHFPKT
VTHSLRKTIR FLHSFTMYRL YQKLFLEMIG NQVQSVKISC L
