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Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (CD antigen CD95)

 TNR6_CERAT              Reviewed;         331 AA.
Q9BDN4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-MAR-2018, entry version 86.
RecName: Full=Tumor necrosis factor receptor superfamily member 6;
AltName: Full=Apo-1 antigen;
AltName: Full=Apoptosis-mediating surface antigen FAS;
AltName: Full=FASLG receptor;
AltName: CD_antigen=CD95;
Flags: Precursor;
Name=FAS; Synonyms=APT1, TNFRSF6;
Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Cercocebus.
NCBI_TaxID=9531;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-44; GLN-47; ASP-55;
HIS-60; SER-61; GLY-77; ALA-95; GLY-282 AND ASP-298.
PubMed=11491535; DOI=10.1007/s002510100322;
Villinger F.J., Bostik P., Mayne A.E., King C.L., Genain C.P.,
Weiss W.R., Ansari A.A.;
"Cloning, sequencing, and homology analysis of nonhuman primate
Fas/Fas-ligand and co-stimulatory molecules.";
Immunogenetics 53:315-328(2001).
-!- FUNCTION: Receptor for TNFSF6/FASLG. The adapter molecule FADD
recruits caspase-8 to the activated receptor. The resulting death-
inducing signaling complex (DISC) performs caspase-8 proteolytic
activation which initiates the subsequent cascade of caspases
(aspartate-specific cysteine proteases) mediating apoptosis. FAS-
mediated apoptosis may have a role in the induction of peripheral
tolerance, in the antigen-stimulated suicide of mature T-cells, or
both (By similarity). {ECO:0000250}.
-!- SUBUNIT: Binds DAXX. Interacts with HIPK3. Part of a complex
containing HIPK3 and FADD (By similarity). Binds RIPK1 and FAIM2.
Interacts with BABAM2 and FEM1B. Interacts with FADD (By
similarity). Interacts directly (via DED domain) with NOL3 (via
CARD domain); inhibits death-inducing signaling complex (DISC)
assembly by inhibiting the increase in FAS-FADD binding induced by
FAS activation (By similarity). Interacts with CALM (By
similarity). {ECO:0000250|UniProtKB:P25445,
ECO:0000250|UniProtKB:Q63199}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- DOMAIN: Contains a death domain involved in the binding of FADD,
and maybe to other cytosolic adapter proteins.
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EMBL; AF344843; AAK37602.1; -; mRNA.
RefSeq; NP_001292900.1; NM_001305971.1.
ProteinModelPortal; Q9BDN4; -.
SMR; Q9BDN4; -.
GeneID; 105587157; -.
CTD; 355; -.
HOVERGEN; HBG004091; -.
OrthoDB; EOG091G0DU6; -.
Proteomes; UP000233060; Whole Genome Shotgun Assembly.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; IEA:InterPro.
CDD; cd08316; Death_FAS_TNFRSF6; 1.
CDD; cd10579; TNFRSF6; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR008063; Fas_rcpt.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR033998; TNFRSF6_death.
InterPro; IPR033999; TNFRSF6_N.
PANTHER; PTHR23097:SF114; PTHR23097:SF114; 2.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 2.
PRINTS; PR01680; TNFACTORR6.
SMART; SM00005; DEATH; 1.
SMART; SM00208; TNFR; 2.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 2.
PROSITE; PS50050; TNFR_NGFR_2; 2.
2: Evidence at transcript level;
Apoptosis; Calmodulin-binding; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 331 Tumor necrosis factor receptor
superfamily member 6.
/FTId=PRO_0000034562.
TOPO_DOM 26 171 Extracellular. {ECO:0000255}.
TRANSMEM 172 192 Helical. {ECO:0000255}.
TOPO_DOM 193 331 Cytoplasmic. {ECO:0000255}.
REPEAT 47 83 TNFR-Cys 1.
REPEAT 84 127 TNFR-Cys 2.
REPEAT 128 166 TNFR-Cys 3.
DOMAIN 226 310 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 209 313 Interaction with HIPK3. {ECO:0000250}.
REGION 226 250 Interaction with CALM.
{ECO:0000250|UniProtKB:P25445}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000250|UniProtKB:P25446}.
MOD_RES 221 221 Phosphoserine.
{ECO:0000250|UniProtKB:P25445}.
MOD_RES 318 318 Phosphothreonine.
{ECO:0000250|UniProtKB:P25446}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 59 73 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 63 82 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 85 101 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 104 119 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 107 127 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 129 143 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 146 157 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 149 165 {ECO:0000255|PROSITE-ProRule:PRU00206}.
VARIANT 44 44 I -> V. {ECO:0000269|PubMed:11491535}.
VARIANT 47 47 R -> Q. {ECO:0000269|PubMed:11491535}.
VARIANT 55 55 E -> D. {ECO:0000269|PubMed:11491535}.
VARIANT 60 60 R -> H. {ECO:0000269|PubMed:11491535}.
VARIANT 61 61 N -> S. {ECO:0000269|PubMed:11491535}.
VARIANT 77 77 E -> G. {ECO:0000269|PubMed:11491535}.
VARIANT 95 95 G -> A. {ECO:0000269|PubMed:11491535}.
VARIANT 282 282 E -> G. {ECO:0000269|PubMed:11491535}.
VARIANT 298 298 G -> D. {ECO:0000269|PubMed:11491535}.
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


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