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TR10D_HUMAN
ID   TR10D_HUMAN             Reviewed;         386 AA.
AC   Q9UBN6; B2R8W0; Q9Y6Q4;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 187.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 10D;
DE   AltName: Full=Decoy receptor 2;
DE            Short=DcR2;
DE   AltName: Full=TNF-related apoptosis-inducing ligand receptor 4;
DE            Short=TRAIL receptor 4;
DE            Short=TRAIL-R4 {ECO:0000303|PubMed:9430226};
DE   AltName: Full=TRAIL receptor with a truncated death domain;
DE   AltName: CD_antigen=CD264;
DE   Flags: Precursor;
GN   Name=TNFRSF10D {ECO:0000312|HGNC:HGNC:11907};
GN   Synonyms=DCR2, TRAILR4, TRUNDD {ECO:0000303|PubMed:9537512};
GN   ORFNames=UNQ251/PRO288;
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], PROTEIN SEQUENCE OF N-TERMINUS, AND VARIANT
RP   SER-310.
RC   TISSUE=Fetal lung;
RX   PubMed=9382840; DOI=10.1016/s0960-9822(06)00422-2;
RA   Marsters S.A., Sheridan J.P., Pitti R.M., Huang A., Skubatch M.,
RA   Baldwin D., Yuan J., Gurney A., Goddard A.D., Godowski P., Ashkenazi A.;
RT   "A novel receptor for Apo2L/TRAIL contains a truncated death domain.";
RL   Curr. Biol. 7:1003-1006(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANTS SER-35 AND SER-310,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Foreskin fibroblast, and Peripheral blood lymphocyte;
RX   PubMed=9430226; DOI=10.1016/s1074-7613(00)80399-4;
RA   Degli-Esposti M.A., Dougall W.C., Smolak P.J., Waugh J.Y., Smith C.A.,
RA   Goodwin R.G.;
RT   "The novel receptor TRAIL-R4 induces NF-kappaB and protects against TRAIL-
RT   mediated apoptosis, yet retains an incomplete death domain.";
RL   Immunity 7:813-820(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, FUNCTION, AND VARIANT
RP   SER-310.
RX   PubMed=9537512; DOI=10.1016/s0014-5793(98)00135-5;
RA   Pan G., Ni J., Yu G.-L., Wei Y.-F., Dixit V.M.;
RT   "TRUNDD, a new member of the TRAIL receptor family that antagonizes TRAIL
RT   signalling.";
RL   FEBS Lett. 424:41-45(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-310.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-310.
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-310.
RC   TISSUE=Prostate;
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   [7]
RP   PROTEIN SEQUENCE OF 56-70.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
CC   -!- FUNCTION: Receptor for the cytotoxic ligand TRAIL (PubMed:9430226).
CC       Contains a truncated death domain and hence is not capable of inducing
CC       apoptosis but protects against TRAIL-mediated apoptosis
CC       (PubMed:9537512). Reports are contradictory with regards to its ability
CC       to induce the NF-kappa-B pathway. According to PubMed:9382840, it
CC       cannot but according to PubMed:9430226, it can induce the NF-kappa-B
CC       pathway (PubMed:9382840, PubMed:9430226). {ECO:0000269|PubMed:9382840,
CC       ECO:0000269|PubMed:9430226, ECO:0000269|PubMed:9537512}.
CC   -!- INTERACTION:
CC       Q9UBN6; O95236-2: APOL3; NbExp=3; IntAct=EBI-1044859, EBI-11976321;
CC       Q9UBN6; P53367: ARFIP1; NbExp=3; IntAct=EBI-1044859, EBI-2808808;
CC       Q9UBN6; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-1044859, EBI-752069;
CC       Q9UBN6; Q5VYK3: ECPAS; NbExp=3; IntAct=EBI-1044859, EBI-521451;
CC       Q9UBN6; Q8IWE2: FAM114A1; NbExp=3; IntAct=EBI-1044859, EBI-2686288;
CC       Q9UBN6; Q05329: GAD2; NbExp=3; IntAct=EBI-1044859, EBI-9304251;
CC       Q9UBN6; C9JCN9: HSBP1L1; NbExp=3; IntAct=EBI-1044859, EBI-2685549;
CC       Q9UBN6; Q9BT40: INPP5K; NbExp=3; IntAct=EBI-1044859, EBI-749162;
CC       Q9UBN6; O43561-2: LAT; NbExp=3; IntAct=EBI-1044859, EBI-8070286;
CC       Q9UBN6; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-1044859, EBI-740987;
CC       Q9UBN6; Q7Z6M4: MTERF4; NbExp=3; IntAct=EBI-1044859, EBI-948435;
CC       Q9UBN6; P49585: PCYT1A; NbExp=3; IntAct=EBI-1044859, EBI-2563309;
CC       Q9UBN6; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-1044859, EBI-14223623;
CC       Q9UBN6; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-1044859, EBI-11721828;
CC       Q9UBN6; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-1044859, EBI-10320765;
CC       Q9UBN6; P09455: RBP1; NbExp=3; IntAct=EBI-1044859, EBI-2623483;
CC       Q9UBN6; Q96LZ7: RMDN2; NbExp=3; IntAct=EBI-1044859, EBI-2806908;
CC       Q9UBN6; Q9NTN9-2: SEMA4G; NbExp=3; IntAct=EBI-1044859, EBI-12913124;
CC       Q9UBN6; Q9HC62: SENP2; NbExp=3; IntAct=EBI-1044859, EBI-714881;
CC       Q9UBN6; Q92504: SLC39A7; NbExp=3; IntAct=EBI-1044859, EBI-1051105;
CC       Q9UBN6; Q9P2R7: SUCLA2; NbExp=3; IntAct=EBI-1044859, EBI-2269898;
CC       Q9UBN6; Q9BW92: TARS2; NbExp=3; IntAct=EBI-1044859, EBI-1045099;
CC       Q9UBN6; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-1044859, EBI-702328;
CC       Q9UBN6; Q8WY91: THAP4; NbExp=3; IntAct=EBI-1044859, EBI-726691;
CC       Q9UBN6; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-1044859, EBI-12261790;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, in particular in fetal kidney,
CC       lung and liver, and in adult testis and liver. Also expressed in
CC       peripheral blood leukocytes, colon and small intestine, ovary,
CC       prostate, thymus, spleen, pancreas, kidney, lung, placenta and heart.
CC       {ECO:0000269|PubMed:9430226}.
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DR   EMBL; AF029761; AAD03477.1; -; mRNA.
DR   EMBL; AF021232; AAC32765.1; -; mRNA.
DR   EMBL; AF021233; AAC32766.1; -; mRNA.
DR   EMBL; AF023849; AAC52053.1; -; mRNA.
DR   EMBL; AY358285; AAQ88652.1; -; mRNA.
DR   EMBL; AK313528; BAG36307.1; -; mRNA.
DR   EMBL; BC052270; AAH52270.1; -; mRNA.
DR   CCDS; CCDS6038.1; -.
DR   RefSeq; NP_003831.2; NM_003840.4.
DR   AlphaFoldDB; Q9UBN6; -.
DR   BioGRID; 114321; 45.
DR   DIP; DIP-6231N; -.
DR   IntAct; Q9UBN6; 31.
DR   MINT; Q9UBN6; -.
DR   STRING; 9606.ENSP00000310263; -.
DR   GlyGen; Q9UBN6; 2 sites.
DR   iPTMnet; Q9UBN6; -.
DR   PhosphoSitePlus; Q9UBN6; -.
DR   SwissPalm; Q9UBN6; -.
DR   BioMuta; TNFRSF10D; -.
DR   DMDM; 18203495; -.
DR   EPD; Q9UBN6; -.
DR   jPOST; Q9UBN6; -.
DR   MassIVE; Q9UBN6; -.
DR   MaxQB; Q9UBN6; -.
DR   PaxDb; Q9UBN6; -.
DR   PeptideAtlas; Q9UBN6; -.
DR   PRIDE; Q9UBN6; -.
DR   ProteomicsDB; 84018; -.
DR   Antibodypedia; 9716; 778 antibodies from 43 providers.
DR   DNASU; 8793; -.
DR   Ensembl; ENST00000312584.4; ENSP00000310263.3; ENSG00000173530.6.
DR   GeneID; 8793; -.
DR   KEGG; hsa:8793; -.
DR   MANE-Select; ENST00000312584.4; ENSP00000310263.3; NM_003840.5; NP_003831.2.
DR   UCSC; uc003xcz.4; human.
DR   CTD; 8793; -.
DR   DisGeNET; 8793; -.
DR   GeneCards; TNFRSF10D; -.
DR   HGNC; HGNC:11907; TNFRSF10D.
DR   HPA; ENSG00000173530; Low tissue specificity.
DR   MIM; 603614; gene.
DR   neXtProt; NX_Q9UBN6; -.
DR   OpenTargets; ENSG00000173530; -.
DR   PharmGKB; PA36600; -.
DR   VEuPathDB; HostDB:ENSG00000173530; -.
DR   eggNOG; ENOG502RBEC; Eukaryota.
DR   GeneTree; ENSGT00940000164831; -.
DR   HOGENOM; CLU_038161_0_0_1; -.
DR   InParanoid; Q9UBN6; -.
DR   OrthoDB; 1448442at2759; -.
DR   PhylomeDB; Q9UBN6; -.
DR   TreeFam; TF333916; -.
DR   PathwayCommons; Q9UBN6; -.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
DR   Reactome; R-HSA-75158; TRAIL signaling.
DR   SignaLink; Q9UBN6; -.
DR   SIGNOR; Q9UBN6; -.
DR   BioGRID-ORCS; 8793; 8 hits in 1073 CRISPR screens.
DR   ChiTaRS; TNFRSF10D; human.
DR   GeneWiki; TNFRSF10D; -.
DR   GenomeRNAi; 8793; -.
DR   Pharos; Q9UBN6; Tbio.
DR   PRO; PR:Q9UBN6; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9UBN6; protein.
DR   Bgee; ENSG00000173530; Expressed in cartilage tissue and 145 other tissues.
DR   Genevisible; Q9UBN6; HS.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045569; F:TRAIL binding; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd10580; TNFRSF10; 1.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020465; TNFR_10.
DR   InterPro; IPR034024; TNFRSF10_N.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PRINTS; PR01956; TNFACTORR10.
DR   SMART; SM00208; TNFR; 2.
DR   PROSITE; PS00652; TNFR_NGFR_1; 2.
DR   PROSITE; PS50050; TNFR_NGFR_2; 2.
PE   1: Evidence at protein level;
KW   Apoptosis; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..55
FT                   /evidence="ECO:0000269|PubMed:15340161,
FT                   ECO:0000269|PubMed:9382840"
FT   CHAIN           56..386
FT                   /note="Tumor necrosis factor receptor superfamily member
FT                   10D"
FT                   /id="PRO_0000034584"
FT   TOPO_DOM        56..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..386
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          58..97
FT                   /note="TNFR-Cys 1"
FT   REPEAT          98..139
FT                   /note="TNFR-Cys 2"
FT   REPEAT          140..180
FT                   /note="TNFR-Cys 3"
FT   DOMAIN          340..366
FT                   /note="Death; truncated"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        99..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        118..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        121..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        141..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        158..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        162..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   VARIANT         35
FT                   /note="P -> S (in dbSNP:rs11135703)"
FT                   /evidence="ECO:0000269|PubMed:9430226"
FT                   /id="VAR_011417"
FT   VARIANT         276
FT                   /note="R -> H (in dbSNP:rs55636833)"
FT                   /id="VAR_061854"
FT   VARIANT         310
FT                   /note="L -> S (in dbSNP:rs1133782)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9382840, ECO:0000269|PubMed:9430226,
FT                   ECO:0000269|PubMed:9537512"
FT                   /id="VAR_011418"
FT   VARIANT         345
FT                   /note="T -> P (in dbSNP:rs34622674)"
FT                   /id="VAR_057288"
SQ   SEQUENCE   386 AA;  41849 MW;  8D15E577D214852A CRC64;
     MGLWGQSVPT ASSARAGRYP GARTASGTRP WLLDPKILKF VVFIVAVLLP VRVDSATIPR
     QDEVPQQTVA PQQQRRSLKE EECPAGSHRS EYTGACNPCT EGVDYTIASN NLPSCLLCTV
     CKSGQTNKSS CTTTRDTVCQ CEKGSFQDKN SPEMCRTCRT GCPRGMVKVS NCTPRSDIKC
     KNESAASSTG KTPAAEETVT TILGMLASPY HYLIIIVVLV IILAVVVVGF SCRKKFISYL
     KGICSGGGGG PERVHRVLFR RRSCPSRVPG AEDNARNETL SNRYLQPTQV SEQEIQGQEL
     AELTGVTVEL PEEPQRLLEQ AEAEGCQRRR LLVPVNDADS ADISTLLDAS ATLEEGHAKE
     TIQDQLVGSE KLFYEEDEAG SATSCL
 
 
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