TR11B_BOVIN
ID TR11B_BOVIN Reviewed; 402 AA.
AC A5D7R1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 11B;
DE AltName: Full=Osteoprotegerin;
DE Flags: Precursor;
GN Name=TNFRSF11B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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. Bone homeostasis
CC seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May
CC also play a role in preventing arterial calcification. May act as decoy
CC receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL
CC binding blocks the inhibition of osteoclastogenesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with TNFSF10 and TNFSF11 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: N-glycosylated. Contains sialic acid residues (By similarity).
CC {ECO:0000250}.
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DR EMBL; BC140651; AAI40652.1; -; mRNA.
DR RefSeq; NP_001091525.1; NM_001098056.2.
DR AlphaFoldDB; A5D7R1; -.
DR SMR; A5D7R1; -.
DR STRING; 9913.ENSBTAP00000009759; -.
DR PaxDb; A5D7R1; -.
DR PRIDE; A5D7R1; -.
DR Ensembl; ENSBTAT00000009759; ENSBTAP00000009759; ENSBTAG00000007423.
DR GeneID; 523822; -.
DR KEGG; bta:523822; -.
DR CTD; 4982; -.
DR VEuPathDB; HostDB:ENSBTAG00000007423; -.
DR VGNC; VGNC:36161; TNFRSF11B.
DR eggNOG; ENOG502QVRT; Eukaryota.
DR GeneTree; ENSGT00940000155167; -.
DR HOGENOM; CLU_057708_0_0_1; -.
DR InParanoid; A5D7R1; -.
DR OMA; KFLCCTL; -.
DR OrthoDB; 869160at2759; -.
DR TreeFam; TF331157; -.
DR Reactome; R-BTA-5669034; TNFs bind their physiological receptors.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000007423; Expressed in intramuscular adipose tissue and 79 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; 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:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.533.10; -; 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 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 2: Evidence at transcript level;
KW Apoptosis; Disulfide bond; Glycoprotein; Receptor; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..402
FT /note="Tumor necrosis factor receptor superfamily member
FT 11B"
FT /id="PRO_0000394512"
FT REPEAT 24..62
FT /note="TNFR-Cys 1"
FT REPEAT 64..105
FT /note="TNFR-Cys 2"
FT REPEAT 106..142
FT /note="TNFR-Cys 3"
FT REPEAT 144..185
FT /note="TNFR-Cys 4"
FT DOMAIN 198..269
FT /note="Death 1"
FT DOMAIN 270..365
FT /note="Death 2"
FT SITE 401
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
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 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 402 AA; 46418 MW; A0F6FDC15A355270 CRC64;
MNKLLCCALV FLDISIKWTT QETFPPKYLH YDPESSRQLM CDKCPPGTFL KQPCTARRKT
VCAPCPDHYY TDTWHTSDEC LYCSPVCKEL QYVKQECSRT HNRVCECEEG RYLELEFCLK
HRSCPPGFGV LHPGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSAFG LLLTQKGNAT
HDNICSGSSE SSTHKCGIDM TLCEEAFFRF AVPTKLTPNW LSVLVDNLPG TKVNAESIER
IKQRHNSREQ TFQLLKLWKH QNKDQDMVKK IIQDIDLCEN SVRRHIGHLN LTFEQLLKLM
ESLPGKKVTT EDVEKTVKTC KSSEQLLKLL SLWRIKNGDQ DTRKGLLHAL KHLKTYHFPK
TVIQSLKKTI RFLHSFTMYR LYRKLFLEMI GNQVQSLKIS CL
