TNR1A_PIG
ID TNR1A_PIG Reviewed; 461 AA.
AC P50555;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 1A;
DE AltName: Full=Tumor necrosis factor receptor 1;
DE Short=TNF-R1;
DE AltName: Full=Tumor necrosis factor receptor type I;
DE Short=TNF-RI;
DE Short=TNFR-I;
DE AltName: Full=p55;
DE AltName: Full=p60;
DE AltName: CD_antigen=CD120a;
DE Flags: Precursor;
GN Name=TNFRSF1A; Synonyms=TNFR1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=7590278; DOI=10.1016/0378-1119(95)00423-4;
RA Suter B., Pauli U.H.;
RT "Cloning of the cDNA encoding the porcine p55 tumor necrosis factor
RT receptor.";
RL Gene 163:263-266(1995).
CC -!- FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric
CC TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8
CC to the activated receptor. The resulting death-inducing signaling
CC complex (DISC) performs caspase-8 proteolytic activation which
CC initiates the subsequent cascade of caspases (aspartate-specific
CC cysteine proteases) mediating apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binding of TNF to the extracellular domain leads to
CC homotrimerization. The aggregated death domains provide a novel
CC molecular interface that interacts specifically with the death domain
CC of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and
CC possibly FADD, are recruited to the complex by their association with
CC TRADD. This complex activates at least two distinct signaling cascades,
CC apoptosis and NF-kappa-B signaling. Interacts with BAG4, BABAM2, FEM1B,
CC GRB2, SQSTM1 and TRPC4AP. Interacts with DAB2IP. Interacts directly
CC with NOL3 (via CARD domain); inhibits TNF-signaling pathway. Interacts
CC with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of
CC RIPK1 and TRADD to TNFRSF1A in a TNF-alpha-dependent process. Interacts
CC with PGLYRP1; this interaction is important for cell death induction.
CC Interacts (via death domain) with MADD (via death domain) (By
CC similarity). {ECO:0000250|UniProtKB:P19438,
CC ECO:0000250|UniProtKB:P25118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: Both the cytoplasmic membrane-proximal region and the C-
CC terminal region containing the death domain are involved in the
CC interaction with TRPC4AP. {ECO:0000250}.
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DR EMBL; U19994; AAC48499.1; -; mRNA.
DR PIR; JC4302; JC4302.
DR RefSeq; NP_999134.1; NM_213969.1.
DR AlphaFoldDB; P50555; -.
DR SMR; P50555; -.
DR STRING; 9823.ENSSSCP00000000755; -.
DR PaxDb; P50555; -.
DR GeneID; 397020; -.
DR KEGG; ssc:397020; -.
DR CTD; 7132; -.
DR eggNOG; ENOG502S050; Eukaryota.
DR InParanoid; P50555; -.
DR OrthoDB; 726174at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:InterPro.
DR CDD; cd08313; Death_TNFR1; 1.
DR CDD; cd10576; TNFRSF1A; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020419; TNFR_1A.
DR InterPro; IPR033994; TNFRSF1A_death.
DR InterPro; IPR033993; TNFRSF1A_N.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 3.
DR PRINTS; PR01918; TNFACTORR1A.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 4.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 3.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell membrane; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000250|UniProtKB:P19438"
FT CHAIN 30..461
FT /note="Tumor necrosis factor receptor superfamily member
FT 1A"
FT /id="PRO_0000034546"
FT TOPO_DOM 30..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 43..82
FT /note="TNFR-Cys 1"
FT REPEAT 83..125
FT /note="TNFR-Cys 2"
FT REPEAT 126..166
FT /note="TNFR-Cys 3"
FT REPEAT 167..195
FT /note="TNFR-Cys 4"
FT DOMAIN 362..447
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 340..350
FT /note="N-SMase activation domain (NSD)"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 59..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 62..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 84..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 102..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 105..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 127..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 146..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 149..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 168..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 182..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 185..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 461 AA; 50696 MW; CD72361EC60C9D43 CRC64;
MGLSTVPGLL LPLVLRALLV DVYPAGVHGL VLHPGDREKR ESLCPQGKYS HPQNRSICCT
KCHKGTYLHN DCLGPGLDTD CRECDNGTFT ASENHLTQCL SCSKCRSEMS QVEISPCTVD
RDTVCGCRKN QYRKYWSETL FQCLNCSLCP NGTVQLPCLE KQDTICNCHS GFFLRDKECV
SCVNCKNADC KNLCPATSET RNDFQDTGTT VLLPLVIFFG LCLAFFLFVG LACRYQRWKP
KLYSIICGKS TPVKEGEPEP LATAPSFGPI TTFSPIPSFS PTTTFSPVPS FSPISSPTFT
PCDWSNIKVT SPPKEIAPPP QGAGPILPMP PASTPVPTPL PKWGGSAHSA HSAPAQLADA
DPATLYAVVD GVPPTRWKEF VRRLGLSEHE IERLELQNGR CLREAQYSML AEWRRRTSRR
EATLELLGSV LRDMDLLGCL EDIEEALRGP ARLAPAPHLL R
