TNR6_PIG
ID TNR6_PIG Reviewed; 332 AA.
AC O77736;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bartling B., Hoffmann J., Holtz J., Schulz R., Heusch G., Darmer D.;
RT "Expression of apoptosis-associated genes in hibernating and stunned
RT myocardium of pig.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P51867};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P51867}.
CC Membrane raft {ECO:0000250|UniProtKB:P25445}.
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; AJ001202; CAA04596.1; -; mRNA.
DR RefSeq; NP_999004.1; NM_213839.1.
DR AlphaFoldDB; O77736; -.
DR SMR; O77736; -.
DR STRING; 9823.ENSSSCP00000011136; -.
DR PaxDb; O77736; -.
DR PeptideAtlas; O77736; -.
DR PRIDE; O77736; -.
DR Ensembl; ENSSSCT00030039189; ENSSSCP00030018041; ENSSSCG00030028016.
DR Ensembl; ENSSSCT00040069888; ENSSSCP00040029785; ENSSSCG00040051682.
DR Ensembl; ENSSSCT00045044622; ENSSSCP00045030948; ENSSSCG00045026098.
DR Ensembl; ENSSSCT00050030167; ENSSSCP00050012547; ENSSSCG00050022352.
DR Ensembl; ENSSSCT00060029683; ENSSSCP00060012745; ENSSSCG00060021879.
DR GeneID; 396826; -.
DR KEGG; ssc:396826; -.
DR CTD; 355; -.
DR eggNOG; ENOG502S0SV; Eukaryota.
DR InParanoid; O77736; -.
DR OrthoDB; 993446at2759; -.
DR Reactome; R-SSC-3371378; Regulation by c-FLIP.
DR Reactome; R-SSC-5218900; CASP8 activity is inhibited.
DR Reactome; R-SSC-69416; Dimerization of procaspase-8.
DR Reactome; R-SSC-75157; FasL/ CD95L signaling.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; 2.
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; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..332
FT /note="Tumor necrosis factor receptor superfamily member 6"
FT /id="PRO_0000034568"
FT TOPO_DOM 17..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 45..81
FT /note="TNFR-Cys 1"
FT REPEAT 82..125
FT /note="TNFR-Cys 2"
FT REPEAT 126..164
FT /note="TNFR-Cys 3"
FT DOMAIN 227..311
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 210..314
FT /note="Interaction with HIPK3"
FT /evidence="ECO:0000250"
FT REGION 227..251
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25446"
FT LIPID 200
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 58..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 61..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 83..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 102..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 105..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 127..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 144..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 147..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 332 AA; 37593 MW; 5B8B03682756BF1B CRC64;
MSGIWVLLSL VFTCIAGPLS KGDDAQVTDP DSEMVKLNIT KRESECPEGQ HREGQFCCQP
CPPGKRKHAD CTSPGGAPQC VPCSEGEDYT DKNHHSSKCR RCRVCDGEHG LEVEKNCTRT
QNTKCRCKPN FFCHTSQCEH CNPCTTCEHG VIENCTPTSN TKCREVFQSA GSRSNLHWLW
ALLILIPVPA LVYREVKRRC RRKENGYQKP ITSNAEEVPM IKDVDLGKYI TRIAEQMKIT
EVKDFVRKNG IEETKIDEIM HDNPKDTAEQ KVQLLRNWYL YHGKKDAYCT LIQGLRKAKL
SALADKINDI VQKDVTSEQE NANSQNENES LT
