ID   TNR6_MACFA              Reviewed;         331 AA.
AC   Q9TSN4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10773350; DOI=10.1016/s0198-8859(00)00100-2;
RA   Murayama Y., Terao K., Inoue-Murayama M.;
RT   "Molecular cloning and characterization of cynomolgus monkey Fas.";
RL   Hum. Immunol. 61:474-485(2000).
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; AB031420; BAA83551.1; -; mRNA.
DR   RefSeq; NP_001270444.1; NM_001283515.1.
DR   AlphaFoldDB; Q9TSN4; -.
DR   SMR; Q9TSN4; -.
DR   STRING; 9541.XP_005565956.1; -.
DR   GeneID; 102140989; -.
DR   CTD; 355; -.
DR   eggNOG; ENOG502S0SV; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; 2.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..331
FT                   /note="Tumor necrosis factor receptor superfamily member 6"
FT                   /id="PRO_0000034564"
FT   TOPO_DOM        26..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          47..83
FT                   /note="TNFR-Cys 1"
FT   REPEAT          84..127
FT                   /note="TNFR-Cys 2"
FT   REPEAT          128..166
FT                   /note="TNFR-Cys 3"
FT   DOMAIN          226..310
FT                   /note="Death"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT   REGION          209..313
FT                   /note="Interaction with HIPK3"
FT                   /evidence="ECO:0000250"
FT   REGION          226..250
FT                   /note="Interaction with CALM"
FT                   /evidence="ECO:0000250|UniProtKB:P25445"
FT   MOD_RES         211
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P25446"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P25445"
FT   MOD_RES         318
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P25446"
FT   LIPID           196
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P25445"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        63..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        85..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        104..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        107..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        129..143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        146..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        149..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ   SEQUENCE   331 AA;  37266 MW;  0C617508081B05DF CRC64;
     MLGIWTLLPL VLTSVVRLLS KCVNAQVTDI SSKGFELRKI VTTIETQNLE GLHHEGQFCR
     NPCPPGERKA RDCTVNEDEP DCVPCQEGKE YTDKGHFSSK CRRCRLCDEG HGLEVEINCT
     RTQNTKCRCK PNFFCNSAVC EHCDPCTKCE HGIIEECTLT SNTKCKEEDS RSDLPWLCLL
     LLLIPPIVYV VIKKACRKHR KENQGPHEST TLNPETAINL SDVDLSKYIT TIAGAMTLSQ
     VKDFVRKNGV SEAKIDEIKN DNVQDTAEQK VQLLRNWYQL HGKKDACDTL IKGLKTADLC
     TLAEKIHAVI LKDITSDTEN SNFRNEIQSL V