TNR6_BOVIN
ID TNR6_BOVIN Reviewed; 323 AA.
AC P51867;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 6;
DE AltName: Full=Apo-1 antigen;
DE AltName: Full=Apoptosis-mediating surface antigen FAS;
DE AltName: Full=FASLG receptor;
DE AltName: CD_antigen=CD95;
DE Flags: Precursor;
GN Name=FAS; Synonyms=APT1, TNFRSF6;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8634151; DOI=10.1089/dna.1996.15.227;
RA Yoo J., Stone R.T., Beattie C.W.;
RT "Cloning and characterization of the bovine Fas.";
RL DNA Cell Biol. 15:227-234(1996).
CC -!- FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits
CC caspase-8 to the activated receptor. The resulting death-inducing
CC signaling complex (DISC) performs caspase-8 proteolytic activation
CC which initiates the subsequent cascade of caspases (aspartate-specific
CC cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may
CC have a role in the induction of peripheral tolerance, in the antigen-
CC stimulated suicide of mature T-cells, or both (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds DAXX. Interacts with HIPK3 (By similarity). Part of a
CC complex containing HIPK3 and FADD (By similarity). Binds RIPK1 and
CC FAIM2. Interacts with BABAM2 and FEM1B. Interacts with FADD (By
CC similarity). Interacts directly (via DED domain) with NOL3 (via CARD
CC domain); inhibits death-inducing signaling complex (DISC) assembly by
CC inhibiting the increase in FAS-FADD binding induced by FAS activation
CC (By similarity). Interacts with CALM (By similarity). In the absence of
CC stimulation, interacts with BIRC2, DDX3X and GSK3B. The interaction
CC with BIRC2 and DDX3X is further enhanced upon receptor stimulation and
CC accompanied by DDX3X and BIRC2 cleavage (By similarity).
CC {ECO:0000250|UniProtKB:P25445, ECO:0000250|UniProtKB:P25446}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8634151};
CC Single-pass type I membrane protein {ECO:0000305}. Membrane raft
CC {ECO:0000250|UniProtKB:P25445}.
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood lymphocytes, thymus,
CC spleen, lung and ovary. {ECO:0000269|PubMed:8634151}.
CC -!- DOMAIN: Contains a death domain involved in the binding of FADD, and
CC maybe to other cytosolic adapter proteins.
CC -!- PTM: Palmitoylated. Palmitoylation by ZDHHC7 prevents the lysosomal
CC degradation of FAS regulating its expression at the plasma membrane.
CC {ECO:0000250|UniProtKB:P25445}.
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DR EMBL; U34794; AAC48546.1; -; mRNA.
DR RefSeq; NP_777087.1; NM_174662.2.
DR AlphaFoldDB; P51867; -.
DR SMR; P51867; -.
DR STRING; 9913.ENSBTAP00000014282; -.
DR PaxDb; P51867; -.
DR PRIDE; P51867; -.
DR GeneID; 282488; -.
DR KEGG; bta:282488; -.
DR CTD; 355; -.
DR eggNOG; ENOG502S0SV; Eukaryota.
DR HOGENOM; CLU_067123_1_0_1; -.
DR InParanoid; P51867; -.
DR OrthoDB; 993446at2759; -.
DR TreeFam; TF333916; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IBA:GO_Central.
DR GO; GO:0006924; P:activation-induced cell death of T cells; IBA:GO_Central.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0097049; P:motor neuron apoptotic process; IBA:GO_Central.
DR GO; GO:0097527; P:necroptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IBA:GO_Central.
DR CDD; cd08316; Death_FAS_TNFRSF6; 1.
DR CDD; cd10579; TNFRSF6; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR008063; Fas_rcpt.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR033998; TNFRSF6_death.
DR InterPro; IPR033999; TNFRSF6_N.
DR PANTHER; PTHR46874; PTHR46874; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01680; TNFACTORR6.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 3.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 2: Evidence at transcript level;
KW Apoptosis; Calmodulin-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..323
FT /note="Tumor necrosis factor receptor superfamily member 6"
FT /id="PRO_0000034561"
FT TOPO_DOM 23..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 45..80
FT /note="TNFR-Cys 1"
FT REPEAT 81..124
FT /note="TNFR-Cys 2"
FT REPEAT 125..163
FT /note="TNFR-Cys 3"
FT DOMAIN 238..306
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 204..305
FT /note="Interaction with HIPK3"
FT /evidence="ECO:0000250"
FT REGION 222..246
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 57..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 60..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 82..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 101..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 104..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 126..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 143..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 146..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 323 AA; 36445 MW; 4D88A90E9E1F4892 CRC64;
MSGIWVHLSL IFISVSGPLS KGENAHMAGI NSEGLKLNIT EANSCQEGLY REHQFCCQPC
PPGKRKNGDC KRDGDTPECV LCSEGNEYTD KSHHSDKCIR CSICDEEHGL EVEQNCTRTR
NTKCRCKSNF FCNSSPCEHC NPCTTCEHGI IEKCTPTSNT KCKGSRSHAN SLWALLILLI
PIVLIIYKVV KSRERNKKND YCNSAASNDE GRQLNLTDVD LGKYIPSIAE QMRITEVKEF
VRKNGMEEAK IDDIMHDNVH ETAEQKVQLL RNWYQSHGKK NAYCTLTKSL PKALAEKICD
IVMKDITNER ENANLQNENE NLV
