TNR8_MOUSE
ID TNR8_MOUSE Reviewed; 498 AA.
AC Q60846; A1L3C9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 8 {ECO:0000250|UniProtKB:P28908};
DE AltName: Full=CD30L receptor;
DE AltName: Full=Lymphocyte activation antigen CD30;
DE AltName: CD_antigen=CD30 {ECO:0000250|UniProtKB:P28908};
DE Flags: Precursor;
GN Name=Tnfrsf8 {ECO:0000312|MGI:MGI:99908};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Splenocyte;
RX PubMed=8543792;
RA Bowen M.A., Lee R.K., Miragliotta G., Nam S.Y., Podack E.R.;
RT "Structure and expression of murine CD30 and its role in cytokine
RT production.";
RL J. Immunol. 156:442-449(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Receptor for TNFSF8/CD30L (PubMed:8543792). May play a role
CC in the regulation of cellular growth and transformation of activated
CC lymphoblasts. Regulates gene expression through activation of NF-kappa-
CC B (By similarity). {ECO:0000250|UniProtKB:P28908,
CC ECO:0000269|PubMed:8543792}.
CC -!- SUBUNIT: Interacts with TRAF1, TRAF2, TRAF3 and TRAF5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8543792};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in thymus and in activated splenocytes.
CC {ECO:0000269|PubMed:8543792}.
CC -!- INDUCTION: By concanavalin A and pokeweed mitogen in splenocytes.
CC {ECO:0000269|PubMed:8543792}.
CC -!- SIMILARITY: Belongs to the TNFR8 family. {ECO:0000305}.
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DR EMBL; U25416; AAA92887.1; -; mRNA.
DR EMBL; BC130026; AAI30027.1; -; mRNA.
DR CCDS; CCDS18915.1; -.
DR RefSeq; NP_033427.1; NM_009401.2.
DR AlphaFoldDB; Q60846; -.
DR STRING; 10090.ENSMUSP00000030339; -.
DR GlyGen; Q60846; 3 sites.
DR iPTMnet; Q60846; -.
DR PhosphoSitePlus; Q60846; -.
DR EPD; Q60846; -.
DR PaxDb; Q60846; -.
DR PRIDE; Q60846; -.
DR ProteomicsDB; 259484; -.
DR Antibodypedia; 3659; 2367 antibodies from 45 providers.
DR DNASU; 21941; -.
DR Ensembl; ENSMUST00000030339; ENSMUSP00000030339; ENSMUSG00000028602.
DR GeneID; 21941; -.
DR KEGG; mmu:21941; -.
DR UCSC; uc008vrv.1; mouse.
DR CTD; 943; -.
DR MGI; MGI:99908; Tnfrsf8.
DR VEuPathDB; HostDB:ENSMUSG00000028602; -.
DR eggNOG; ENOG502SNQ9; Eukaryota.
DR GeneTree; ENSGT00510000049215; -.
DR HOGENOM; CLU_043282_0_0_1; -.
DR InParanoid; Q60846; -.
DR OMA; PHTDCAK; -.
DR OrthoDB; 630149at2759; -.
DR PhylomeDB; Q60846; -.
DR TreeFam; TF331157; -.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR BioGRID-ORCS; 21941; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q60846; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q60846; protein.
DR Bgee; ENSMUSG00000028602; Expressed in retinal neural layer and 21 other tissues.
DR ExpressionAtlas; Q60846; baseline and differential.
DR Genevisible; Q60846; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0032759; P:positive regulation of TRAIL production; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13409; TNFRSF8; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020416; TNFR_8.
DR InterPro; IPR034002; TNFRSF8_N.
DR PRINTS; PR01923; TNFACTORR8.
DR SMART; SM00208; TNFR; 3.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..498
FT /note="Tumor necrosis factor receptor superfamily member 8"
FT /id="PRO_0000034575"
FT TOPO_DOM 19..287
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 68..105
FT /note="TNFR-Cys 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT REPEAT 106..146
FT /note="TNFR-Cys 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT REGION 142..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28908"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28908"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 84..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 87..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 107..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 128..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 498 AA; 53216 MW; 98CA2A05B38AFA71 CRC64;
MSALLTAAGL LFLGMLQAFP TDRPLKTTCA GDLSHYPGEA ARNCCYQCPS GLSPTQPCPR
GPAHCRKQCA PDYYVNEDGK CTACVTCLPG LVEKAPCSGN SPRICECQPG MHCCTPAVNS
CARCKLHCSG EEVVKSPGTA KKDTICELPS SGSGPNCSNP GDRKTLTSHA TPQAMPTLES
PANDSARSLL PMRVTNLVQE DATELVKVPE SSSSKAREPS PDPGNAEKNM TLELPSPGTL
PDISTSENSK EPASTASTLS LVVDAWTSSR MQPTSPLSTG TPFLDPGPVL FWVAMVVLLV
GSGSFLLCYW KACRRRFQQK FHLDYLVQTF QPKMEQTDSC PTEKLTQPQR SGSVTDPSTG
HKLSPVSPPP AVETCASVGA TYLENLPLLD DSPAGNPFSP REPPEPRVST EHTNNRIEKI
YIMKADTVIV GSVKTEVPEG RAPAGSTESE LEAELEVDHA PHYPEQETEP PLGSCTEVMF
SVEEGGKEDH GPTTVSEK
