TNR6_CERAT
ID TNR6_CERAT Reviewed; 331 AA.
AC Q9BDN4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 98.
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 Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-44; GLN-47; ASP-55; HIS-60;
RP SER-61; GLY-77; ALA-95; GLY-282 AND ASP-298.
RX PubMed=11491535; DOI=10.1007/s002510100322;
RA Villinger F.J., Bostik P., Mayne A.E., King C.L., Genain C.P., Weiss W.R.,
RA Ansari A.A.;
RT "Cloning, sequencing, and homology analysis of nonhuman primate Fas/Fas-
RT ligand and co-stimulatory molecules.";
RL Immunogenetics 53:315-328(2001).
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; AF344843; AAK37602.1; -; mRNA.
DR RefSeq; NP_001292900.1; NM_001305971.1.
DR AlphaFoldDB; Q9BDN4; -.
DR SMR; Q9BDN4; -.
DR STRING; 9531.ENSCATP00000040382; -.
DR GeneID; 105587157; -.
DR CTD; 355; -.
DR Proteomes; UP000233060; Whole Genome Shotgun Assembly.
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_0000034562"
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"
FT VARIANT 44
FT /note="I -> V"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 47
FT /note="R -> Q"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 55
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 60
FT /note="R -> H"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 61
FT /note="N -> S"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 77
FT /note="E -> G"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 95
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 282
FT /note="E -> G"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 298
FT /note="G -> D"
FT /evidence="ECO:0000269|PubMed:11491535"
SQ SEQUENCE 331 AA; 37278 MW; 1D843C4DE1D343F4 CRC64;
MLGIWTLLPL VLTSVVRLLS KCVNAQVTDI NSKGFELRKI VTTIETRNLE GLHHEGQFCR
NPCPPGERKA RDCTVNEDEP DCVPCQEGKE YTDKGHFSSK CRRCRLCDEG HGLEVEINCT
RTQNTKCRCK PNFFCNSAVC EHCDPCTKCK HGIIEECTLT SNTKCKEEDS RSDLLWLCLL
LLLIPPIVYV VIKKACRKHR KENQGPHEST TLNPETAINL SDVDLSKYIT TIAGGMTLSQ
VRDFVRKNGV SEAKIDEIKN DNVQDTAEQK VQLLRNWYQL HEKKDACDTL IKGLKTAGLC
TLAEKIHAVI LKDITSDTEN SNFGNEVQNL V
