TNR8_RAT
ID TNR8_RAT Reviewed; 492 AA.
AC P97525; A0A0G2K7Z6;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 125.
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|RGD:3879};
GN Synonyms=Cd30 {ECO:0000250|UniProtKB:P28908};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=WKAH; TISSUE=T-cell lymphoma;
RX PubMed=8982082; DOI=10.1016/s0378-1119(96)00542-2;
RA Aizawa S., Satoh H., Horie R., Ito K., Choi S.H., Takeuchi H., Watanabe T.;
RT "Cloning and characterization of a cDNA for rat CD30 homolog and
RT chromosomal assignment of the genomic gene.";
RL Gene 182:155-162(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Receptor for TNFSF8/CD30L. May play a role in the regulation
CC of cellular growth and transformation of activated lymphoblasts (By
CC similarity). Regulates gene expression through activation of NF-kappa-B
CC (PubMed:8982082). {ECO:0000250|UniProtKB:P28908,
CC ECO:0000269|PubMed:8982082}.
CC -!- SUBUNIT: Interacts with TRAF1, TRAF2, TRAF3 and TRAF5.
CC {ECO:0000250|UniProtKB:P28908}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P28908};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Very low level of expression. Detected in spleen,
CC thymus and lung. Highly expressed in HTLV-1 infected T-cell lines.
CC {ECO:0000269|PubMed:8982082}.
CC -!- INDUCTION: By phytohemagglutinin (PHA) in spleen T-cells.
CC {ECO:0000269|PubMed:8982082}.
CC -!- SIMILARITY: Belongs to the TNFR8 family. {ECO:0000305}.
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DR EMBL; D42117; BAA07699.1; -; mRNA.
DR EMBL; AC127855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC5486; JC5486.
DR RefSeq; NP_062008.1; NM_019135.1.
DR AlphaFoldDB; P97525; -.
DR BioGRID; 247144; 2.
DR STRING; 10116.ENSRNOP00000022967; -.
DR GlyGen; P97525; 3 sites.
DR PaxDb; P97525; -.
DR PRIDE; P97525; -.
DR GeneID; 25069; -.
DR KEGG; rno:25069; -.
DR UCSC; RGD:3879; rat.
DR CTD; 943; -.
DR RGD; 3879; Tnfrsf8.
DR eggNOG; ENOG502SNQ9; Eukaryota.
DR InParanoid; P97525; -.
DR OMA; PHTDCAK; -.
DR OrthoDB; 630149at2759; -.
DR PhylomeDB; P97525; -.
DR Reactome; R-RNO-5669034; TNFs bind their physiological receptors.
DR PRO; PR:P97525; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016782; Expressed in thymus and 4 other tissues.
DR ExpressionAtlas; P97525; baseline and differential.
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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
DR GO; GO:0032759; P:positive regulation of TRAIL production; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020416; TNFR_8.
DR PRINTS; PR01923; TNFACTORR8.
DR SMART; SM00208; TNFR; 3.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
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..492
FT /note="Tumor necrosis factor receptor superfamily member 8"
FT /id="PRO_0000034576"
FT TOPO_DOM 19..282
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 57..104
FT /note="TNFR-Cys 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT REPEAT 105..141
FT /note="TNFR-Cys 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT REGION 141..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28908"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28908"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 83..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 86..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 123..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT CONFLICT 67
FT /note="S -> N (in Ref. 1; BAA07699)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..78
FT /note="NEDR -> SNEDG (in Ref. 1; BAA07699)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="D -> E (in Ref. 1; BAA07699)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="S -> T (in Ref. 1; BAA07699)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="R -> W (in Ref. 1; BAA07699)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="V -> A (in Ref. 1; BAA07699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 52613 MW; 1D4A80FA1A247950 CRC64;
MSILLKAAGL LFLGMLQAFP KDRPLDTTCT GDLSYYPGEA ARNCCYQCPS GLSPTQPCPQ
GPATARSSVI LTTTNEDRKC TACVTCLPGL VEKAPCSGNS PRICECQPGM YCSTPAVNSC
ARCSEKTVVK FPDTAEKNTI CDLPSPGSGP NGSNPDDCKT LTSHTTPQAI PTLESPANDS
VRSLLPKQVT DFVNEGATKL VKVPESSSSK ASMPSPDPGN AEMNMTLKLP PPGTVPDIST
SENSMEPAST ASTLSLLVDA RTSSRMQPTS PLSTGTPFLD PGSMLFWVAM VVLLVGSASF
LLCYWKACRR RFQRKFHLNY LQQTFQPKME QVDSCPTEKL TQLQRSGSVT DSSAGHTLSP
LSPPAVETGA SVGTACLETL PLLDDSITGN SFAPREPPEP RVSTEHTNNR IEKIYIMKAD
TVIVGSVKTE VPEGRAPVGS TESELEAELE VDHTPHYPEQ ETEPPLGSCT EVMFSVEEGG
KEDHEPTTVS EK
