TNR3_HUMAN
ID TNR3_HUMAN Reviewed; 435 AA.
AC P36941; B7Z1D2; D3DUR2; F5GXE7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 3;
DE AltName: Full=Lymphotoxin-beta receptor;
DE AltName: Full=Tumor necrosis factor C receptor;
DE AltName: Full=Tumor necrosis factor receptor 2-related protein;
DE AltName: Full=Tumor necrosis factor receptor type III;
DE Short=TNF-RIII;
DE Short=TNFR-III;
DE Flags: Precursor;
GN Name=LTBR; Synonyms=D12S370, TNFCR, TNFR3, TNFRSF3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8486360; DOI=10.1006/geno.1993.1161;
RA Baens M., Chaffanet M., Cassiman J.-J., van den Berghe H., Marynen P.;
RT "Construction and evaluation of a hncDNA library of human 12p transcribed
RT sequences derived from a somatic cell hybrid.";
RL Genomics 16:214-218(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adrenal gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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).
RN [6]
RP FUNCTION.
RX PubMed=8171323; DOI=10.1126/science.8171323;
RA Crowe P.D., VanArsdale T.L., Walter B.N., Ware C.F., Hession C.,
RA Ehrenfels B., Browning J.L., Din W.S., Goodwin R.G., Smith C.A.;
RT "A lymphotoxin-beta-specific receptor.";
RL Science 264:707-710(1994).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10207006; DOI=10.1074/jbc.274.17.11868;
RA Wu M.-Y., Wang P.-Y., Han S.-H., Hsieh S.-L.;
RT "The cytoplasmic domain of the lymphotoxin-beta receptor mediates cell
RT death in HeLa cells.";
RL J. Biol. Chem. 274:11868-11873(1999).
RN [8]
RP FUNCTION.
RX PubMed=10799510; DOI=10.1074/jbc.275.19.14307;
RA Rooney I.A., Butrovich K.D., Glass A.A., Borboroglu S., Benedict C.A.,
RA Whitbeck J.C., Cohen G.H., Eisenberg R.J., Ware C.F.;
RT "The lymphotoxin-beta receptor is necessary and sufficient for LIGHT-
RT mediated apoptosis of tumor cells.";
RL J. Biol. Chem. 275:14307-14315(2000).
RN [9]
RP INTERACTION WITH TRAF3.
RX PubMed=8663299; DOI=10.1074/jbc.271.25.14661;
RA Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H.,
RA Okumura K.;
RT "TRAF5, an activator of NF-kappaB and putative signal transducer for the
RT lymphotoxin-beta receptor.";
RL J. Biol. Chem. 271:14661-14664(1996).
RN [10]
RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
RX PubMed=8995654; DOI=10.1128/jvi.71.2.1301-1309.1997;
RA Matsumoto M., Hsieh T.-Y., Zhu N., VanArsdale T., Hwang S.B., Jeng K.-S.,
RA Gorbalenya A.E., Lo S.-Y., Ou J.-H., Ware C.F., Lai M.M.C.;
RT "Hepatitis C virus core protein interacts with the cytoplasmic tail of
RT lymphotoxin-beta receptor.";
RL J. Virol. 71:1301-1309(1997).
RN [11]
RP INTERACTION WITH TRAF4.
RX PubMed=9626059;
RA Krajewska M., Krajewski S., Zapata J.M., VanArsdale T., Gascoyne R.D.,
RA Berern K., McFadden D., Shabaik A., Hugh J., Reynolds A., Clevenger C.V.,
RA Reed J.C.;
RT "TRAF-4 expression in epithelial progenitor cells. Analysis in normal
RT adult, fetal, and tumor tissues.";
RL Am. J. Pathol. 152:1549-1561(1998).
RN [12]
RP INTERACTION WITH TRAF5.
RX PubMed=9511754; DOI=10.1016/s0378-1119(97)00616-1;
RA Mizushima S., Fujita M., Ishida T., Azuma S., Kato K., Hirai M., Otsuka M.,
RA Yamamoto T., Inoue J.;
RT "Cloning and characterization of a cDNA encoding the human homolog of tumor
RT necrosis factor receptor-associated factor 5 (TRAF5).";
RL Gene 207:135-140(1998).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Receptor for the heterotrimeric lymphotoxin containing LTA
CC and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3 and TRAF5.
CC May play a role in the development of lymphoid organs.
CC {ECO:0000269|PubMed:10799510, ECO:0000269|PubMed:8171323}.
CC -!- SUBUNIT: Self-associates. Associates with TRAF3, TRAF4 and TRAF5.
CC {ECO:0000269|PubMed:8663299, ECO:0000269|PubMed:9511754,
CC ECO:0000269|PubMed:9626059}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
CC {ECO:0000269|PubMed:8995654}.
CC -!- INTERACTION:
CC P36941; Q08426: EHHADH; NbExp=3; IntAct=EBI-3509981, EBI-2339219;
CC P36941; P36941: LTBR; NbExp=2; IntAct=EBI-3509981, EBI-3509981;
CC P36941; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-3509981, EBI-712367;
CC P36941; O43557: TNFSF14; NbExp=3; IntAct=EBI-3509981, EBI-524131;
CC P36941; Q13114: TRAF3; NbExp=2; IntAct=EBI-3509981, EBI-357631;
CC P36941; Q15326: ZMYND11; NbExp=5; IntAct=EBI-3509981, EBI-2623509;
CC P36941; PRO_0000037666 [P29846]; Xeno; NbExp=5; IntAct=EBI-3509981, EBI-8847394;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P36941-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36941-2; Sequence=VSP_047533;
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DR EMBL; L04270; AAA36757.1; -; mRNA.
DR EMBL; AK293187; BAH11468.1; -; mRNA.
DR EMBL; AC005840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88801.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88802.1; -; Genomic_DNA.
DR EMBL; BC026262; AAH26262.1; -; mRNA.
DR CCDS; CCDS59233.1; -. [P36941-2]
DR CCDS; CCDS8544.1; -. [P36941-1]
DR PIR; I54182; I54182.
DR RefSeq; NP_001257916.1; NM_001270987.1. [P36941-2]
DR RefSeq; NP_002333.1; NM_002342.2. [P36941-1]
DR PDB; 1RF3; X-ray; 3.50 A; B=385-408.
DR PDB; 4MXW; X-ray; 3.60 A; R/S=41-211.
DR PDBsum; 1RF3; -.
DR PDBsum; 4MXW; -.
DR AlphaFoldDB; P36941; -.
DR SMR; P36941; -.
DR BioGRID; 110233; 94.
DR CORUM; P36941; -.
DR DIP; DIP-2928N; -.
DR ELM; P36941; -.
DR IntAct; P36941; 74.
DR MINT; P36941; -.
DR STRING; 9606.ENSP00000228918; -.
DR ChEMBL; CHEMBL1250360; -.
DR GlyGen; P36941; 2 sites.
DR iPTMnet; P36941; -.
DR PhosphoSitePlus; P36941; -.
DR BioMuta; LTBR; -.
DR DMDM; 549090; -.
DR CPTAC; CPTAC-2234; -.
DR EPD; P36941; -.
DR jPOST; P36941; -.
DR MassIVE; P36941; -.
DR MaxQB; P36941; -.
DR PaxDb; P36941; -.
DR PeptideAtlas; P36941; -.
DR PRIDE; P36941; -.
DR ProteomicsDB; 24401; -.
DR ProteomicsDB; 55239; -. [P36941-1]
DR ABCD; P36941; 7 sequenced antibodies.
DR Antibodypedia; 10740; 909 antibodies from 37 providers.
DR DNASU; 4055; -.
DR Ensembl; ENST00000228918.9; ENSP00000228918.4; ENSG00000111321.11. [P36941-1]
DR Ensembl; ENST00000539925.5; ENSP00000440875.1; ENSG00000111321.11. [P36941-2]
DR GeneID; 4055; -.
DR KEGG; hsa:4055; -.
DR MANE-Select; ENST00000228918.9; ENSP00000228918.4; NM_002342.3; NP_002333.1.
DR UCSC; uc001qny.3; human. [P36941-1]
DR CTD; 4055; -.
DR DisGeNET; 4055; -.
DR GeneCards; LTBR; -.
DR HGNC; HGNC:6718; LTBR.
DR HPA; ENSG00000111321; Low tissue specificity.
DR MIM; 600979; gene.
DR neXtProt; NX_P36941; -.
DR OpenTargets; ENSG00000111321; -.
DR PharmGKB; PA30481; -.
DR VEuPathDB; HostDB:ENSG00000111321; -.
DR eggNOG; ENOG502S4WF; Eukaryota.
DR GeneTree; ENSGT00940000162178; -.
DR HOGENOM; CLU_052594_0_0_1; -.
DR InParanoid; P36941; -.
DR OMA; SPCGLAW; -.
DR OrthoDB; 1104669at2759; -.
DR PhylomeDB; P36941; -.
DR TreeFam; TF331157; -.
DR PathwayCommons; P36941; -.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR SignaLink; P36941; -.
DR SIGNOR; P36941; -.
DR BioGRID-ORCS; 4055; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; LTBR; human.
DR EvolutionaryTrace; P36941; -.
DR GeneWiki; Lymphotoxin_beta_receptor; -.
DR GenomeRNAi; 4055; -.
DR Pharos; P36941; Tbio.
DR PRO; PR:P36941; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P36941; protein.
DR Bgee; ENSG00000111321; Expressed in lower esophagus mucosa and 169 other tissues.
DR ExpressionAtlas; P36941; baseline and differential.
DR Genevisible; P36941; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd10578; TNFRSF3; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR017349; TNFR_3_LTBR.
DR InterPro; IPR033997; TNFRSF3_N.
DR PANTHER; PTHR47607; PTHR47607; 1.
DR Pfam; PF00020; TNFR_c6; 3.
DR PIRSF; PIRSF037999; TNFR_3_LTBR; 1.
DR PRINTS; PR01920; TNFACTORR3.
DR SMART; SM00208; TNFR; 4.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Disulfide bond;
KW Glycoprotein; Host-virus interaction; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..435
FT /note="Tumor necrosis factor receptor superfamily member 3"
FT /id="PRO_0000034552"
FT TOPO_DOM 31..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 42..81
FT /note="TNFR-Cys 1"
FT REPEAT 82..124
FT /note="TNFR-Cys 2"
FT REPEAT 125..168
FT /note="TNFR-Cys 3"
FT REPEAT 169..211
FT /note="TNFR-Cys 4"
FT REGION 373..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 59..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 62..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 83..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 101..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 104..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 126..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 139..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 142..167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 170..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 1..32
FT /note="MLLPWATSAPGLAWGPLVLGLFGLLAASQPQA -> MEATGISLASQLK
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047533"
FT VARIANT 274
FT /note="V -> I (in dbSNP:rs35681405)"
FT /id="VAR_052346"
FT CONFLICT 76
FT /note="R -> W (in Ref. 2; BAH11468)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="W -> R (in Ref. 2; BAH11468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 46709 MW; 624626E6022F656F CRC64;
MLLPWATSAP GLAWGPLVLG LFGLLAASQP QAVPPYASEN QTCRDQEKEY YEPQHRICCS
RCPPGTYVSA KCSRIRDTVC ATCAENSYNE HWNYLTICQL CRPCDPVMGL EEIAPCTSKR
KTQCRCQPGM FCAAWALECT HCELLSDCPP GTEAELKDEV GKGNNHCVPC KAGHFQNTSS
PSARCQPHTR CENQGLVEAA PGTAQSDTTC KNPLEPLPPE MSGTMLMLAV LLPLAFFLLL
ATVFSCIWKS HPSLCRKLGS LLKRRPQGEG PNPVAGSWEP PKAHPYFPDL VQPLLPISGD
VSPVSTGLPA APVLEAGVPQ QQSPLDLTRE PQLEPGEQSQ VAHGTNGIHV TGGSMTITGN
IYIYNGPVLG GPPGPGDLPA TPEPPYPIPE EGDPGPPGLS TPHQEDGKAW HLAETEHCGA
TPSNRGPRNQ FITHD
