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Database: UniProt
Entry: Q9PW79_CHICK
LinkDB: Q9PW79_CHICK
Original site: Q9PW79_CHICK 
ID   Q9PW79_CHICK            Unreviewed;       368 AA.
AC   Q9PW79;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=TvbS3 {ECO:0000313|EMBL:AAD47256.1};
GN   Name=tvb {ECO:0000313|EMBL:AAD47256.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:AAD47256.1};
RN   [1] {ECO:0000313|EMBL:AAD47256.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8945512; DOI=10.1016/S0092-8674(00)81992-3;
RA   Brojatsch J., Naughton J., Rolls M.M., Zingler K., Young J.A.;
RT   "CAR1, a TNFR-related protein, is a cellular receptor for cytopathic avian
RT   leukosis-sarcoma viruses and mediates apoptosis.";
RL   Cell 87:845-855(1996).
RN   [2] {ECO:0000313|EMBL:AAD47256.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Brojatsch J., Naughton J., Young J.A.T.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter
CC       molecule FADD recruits caspase-8 to the activated receptor. The
CC       resulting death-inducing signaling complex (DISC) performs caspase-8
CC       proteolytic activation which initiates the subsequent cascade of
CC       caspases (aspartate-specific cysteine proteases) mediating apoptosis.
CC       {ECO:0000256|PIRNR:PIRNR037867}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00206}.
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DR   EMBL; AF161712; AAD47256.1; -; mRNA.
DR   AlphaFoldDB; Q9PW79; -.
DR   VEuPathDB; HostDB:geneid_373904; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0045569; F:TRAIL binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IEA:UniProtKB-UniRule.
DR   CDD; cd08315; Death_TRAILR_DR4_DR5; 1.
DR   CDD; cd10580; TNFRSF10; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020465; TNFR_10.
DR   InterPro; IPR034024; TNFRSF10_N.
DR   InterPro; IPR034029; TNFRSF10A/B_death.
DR   PANTHER; PTHR46330:SF16; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 10A; 1.
DR   PANTHER; PTHR46330; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 10B; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PIRSF; PIRSF037867; CD261_antigen; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00208; TNFR; 2.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF57586; TNF receptor-like; 2.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 2.
PE   2: Evidence at transcript level;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|PIRNR:PIRNR037867};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00206}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR037867};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037867};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR037867};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR037867};
KW   Transmembrane helix {ECO:0000256|PIRNR:PIRNR037867}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|PIRNR:PIRNR037867"
FT   CHAIN           25..368
FT                   /evidence="ECO:0000256|PIRNR:PIRNR037867"
FT                   /id="PRO_5024528107"
FT   TRANSMEM        156..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR037867"
FT   DOMAIN          58..101
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          58..101
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          102..143
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000259|PROSITE:PS50050"
FT   REPEAT          102..143
FT                   /note="TNFR-Cys"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DOMAIN          288..357
FT                   /note="Death"
FT                   /evidence="ECO:0000259|PROSITE:PS50017"
FT   DISULFID        80..93
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        83..101
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        103..118
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT   DISULFID        125..143
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
SQ   SEQUENCE   368 AA;  41516 MW;  F558C225AB3750BB CRC64;
     MRSAALRLCP VLLLLFAEVQ LGSAAAVKKR ADRSDLQKPD LYRRKCPMGT YEANDSIQCL
     PSKKDEYTEY PNDFPKCLGC RTCREDQVEV SPCIPTRNTQ CACKNGTFCL PDHPCEMCQK
     CQTECPKGQV RLAPCTQHSD LLCGPPLEIS SSSSTLWIII TFTVLLAVIL GLVLVFWKRC
     SSRHHGAGDD GELSWKPSAV VNRLLQRLGI QDNRCNEQIY QNQQQQELLF TAQGSEVPHG
     VEMEGTERRT PDPKVETQRK LVPVLGENPI ALLHRSFNTF VDYVPFPEWK RFGRALDLQE
     NDLYLAEQHD RVSCEPFYQM LNTWLNQQGS KASVNTLLET LPRIGLSGVA DIIASELISK
     GYFQYEVS
//
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