TNR6_MACMU
ID TNR6_MACMU Reviewed; 333 AA.
AC Q9BDP2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-75; LYS-89; LYS-196 AND
RP HIS-201.
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; AF344833; AAK37529.1; -; mRNA.
DR RefSeq; NP_001028105.1; NM_001032933.2.
DR AlphaFoldDB; Q9BDP2; -.
DR SMR; Q9BDP2; -.
DR STRING; 9544.ENSMMUP00000014651; -.
DR GeneID; 574332; -.
DR KEGG; mcc:574332; -.
DR CTD; 355; -.
DR eggNOG; ENOG502S0SV; Eukaryota.
DR InParanoid; Q9BDP2; -.
DR Proteomes; UP000006718; 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; 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..333
FT /note="Tumor necrosis factor receptor superfamily member 6"
FT /id="PRO_0000034565"
FT TOPO_DOM 26..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..333
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 228..312
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 211..315
FT /note="Interaction with HIPK3"
FT /evidence="ECO:0000250"
FT REGION 228..252
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25446"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25445"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P25446"
FT LIPID 198
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 75
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 89
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 196
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:11491535"
FT VARIANT 201
FT /note="R -> H"
FT /evidence="ECO:0000269|PubMed:11491535"
SQ SEQUENCE 333 AA; 37468 MW; 98C17F766762F287 CRC64;
MLGIWTLLPL VLTSVVRLLS KCVNAQVTDI SSKGFELRKI VTTIETQNLE GLHHEGQFCR
NPCPPGERKA RDCTVNEDEP DCVPCQEGEE YTDKGHFSSK CRRCRLCDEG HGLEVEINCT
RTQNTKCRCK PNFFCNSAVC EHCDPCTKCK HGIIEECTLT SNTKCKEEDS RSDLLWLCLL
LLLLLIPPIV YVVIKEPCRK RRKENQGPHE STTLNPETAI NLSDVDLSKY ITTIAGAMTL
SQVKDFVRKN GVSEAKIDEI KNDNVQDTAE QKVQLLRNWY QLHGKKDACD TLIKGLKTAD
LCTLAEKIHA VILKDITSDT ENSNFGNEVQ NLV
