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UniProtKB/Swiss-Prot entry O00220


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TR10A_HUMAN
Primary accession number O00220
Secondary accession numbers A8K5I4 Q53Y72 Q96E62
Integrated into Swiss-Prot on September 26, 2001
Sequence was last modified on May 27, 2002 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 84)
Name and origin of the protein
Protein name Tumor necrosis factor receptor superfamily member 10A [Precursor]
Synonyms Death receptor 4
TNF-related apoptosis-inducing ligand receptor 1
TRAIL receptor 1
TRAIL-R1
CD261 antigen
Gene name
Name: TNFRSF10A
Synonyms: APO2, DR4, TRAILR1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-141 AND THR-209.
DOI=10.1126/science.276.5309.111; PubMed=9082980 [NCBI, ExPASy, EBI, Israel, Japan]
Pan G., O'Rourke K., Chinnaiyan A.M., Gentz R., Ebner R., Ni J., Dixit V.M.;
"The receptor for the cytotoxic ligand TRAIL.";
Science 276:111-113(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-141 AND THR-209.
TISSUE=Tongue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.;
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
DOI=10.1016/S1074-7613(00)80400-8; PubMed=9430227 [NCBI, ExPASy, EBI, Israel, Japan]
Chaudhary P.M., Eby M., Jasmin A., Bookwalter A., Murray J., Hood L.;
"Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway.";
Immunity 7:821-830(1997).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-463 AND SER-466, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
INTERACTION WITH ARAP1.
DOI=10.1007/s10495-007-0171-8; PubMed=18165900 [NCBI, ExPASy, EBI, Israel, Japan]
Simova S., Klima M., Cermak L., Sourkova V., Andera L.;
"Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane.";
Apoptosis 13:423-436(2008).
Comments
  • FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.
  • SUBUNIT: Can interact with TRADD and RIP. Interacts with ARAP1.
  • INTERACTION:
    Q96P48:ARAP1; NbExp=3; IntAct=EBI-518861, EBI-710003;
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
  • TISSUE SPECIFICITY: Widely expressed. High levels are found in spleen, peripheral blood leukocytes, small intestine and thymus, but also in K562 erythroleukemia cells, MCF7 breast carcinoma cells and activated T-cells.
  • SIMILARITY: Contains 1 death domain.
  • SIMILARITY: Contains 3 TNFR-Cys repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U90875; AAC51226.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291299; BAF83988.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006906; AAP35552.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EF064713; ABK41896.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012866; AAH12866.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00021975; -.
RefSeq NP_003835.2; -.
UniGene Hs.591834
3D structure databases
HSSP O14763; 1D0G. [HSSP ENTRY / PDB]
ModBase O00220.
Protein-protein interaction databases
IntAct O00220; 2.
PTM databases
PhosphoSite O00220; -.
Enzyme and pathway databases
Pathway_Interaction_DB trail_pathway; TRAIL signaling pathway.
Organism-specific databases
GeneCards GC08M023104; -.
H-InvDB HIX0022944; -.
HGNC HGNC:11904; TNFRSF10A.
GenAtlas TNFRSF10A.
MIM 603611; gene. [NCBI / EBI]
PharmGKB PA36597; -.
Gene expression databases
ArrayExpress O00220; -.
Bgee O00220; -.
CleanEx HS_TNFRSF10A; -.
GermOnline ENSG00000104689; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred by curator from UniProtKB).
GO:0008656; Molecular function: caspase activator activity (non-traceable author statement from UniProtKB).
GO:0005035; Molecular function: death receptor activity (traceable author statement from ProtInc).
GO:0045569; Molecular function: TRAIL binding (non-traceable author statement from UniProtKB).
GO:0008134; Molecular function: transcription factor binding (inferred from physical interaction from UniProtKB).
GO:0006919; Biological process: activation of caspase activity (non-traceable author statement from UniProtKB).
GO:0007250; Biological process: activation of NF-kappaB-inducing kinase activity (non-traceable author statement from UniProtKB).
GO:0008625; Biological process: induction of apoptosis via death domain receptors (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000488; Death.
IPR011029; DEATH-like.
IPR017301; TNF-rel_apoptosis-ind_lig_rcpt.
IPR001368; TNFR_Cys_rich_reg.
Graphical view of domain structure.
Gene3D G3DSA:1.10.533.10; DEATH_like; 1.
Pfam PF00531; Death; 1.
PF00020; TNFR_c6; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF037867; CD261_antigen; 1.
SMART SM00005; DEATH; 1.
SM00208; TNFR; 2.
SMART graphical view of domain structure.
PROSITE PS50017; DEATH_DOMAIN; 1.
PS00652; TNFR_NGFR_1; 2.
PS50050; TNFR_NGFR_2; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O00220; -.
Genome annotation databases
Ensembl ENSG00000104689; Homo sapiens. [Contig view]
GeneID 8797; -.
KEGG hsa:8797; -.
Phylogenomic databases
HOGENOM O00220; -.
HOVERGEN O00220; -.
Other
NextBio 32996; -.
SOURCE TNFRSF10A; Homo sapiens.
ProtoNet O00220.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    23  23     Potential. 
CHAIN   24   468  445     Tumor necrosis factor receptor superfamily member 10A. PRO_0000034579
TOPO_DOM   24   239  216     Extracellular (Potential). 
TRANSMEM   240   262  23     Potential. 
TOPO_DOM   263   468  206     Cytoplasmic (Potential). 
REPEAT   107   145  39     TNFR-Cys 1. 
REPEAT   147   188  42     TNFR-Cys 2. 
REPEAT   189   229  41     TNFR-Cys 3. 
DOMAIN   365   448  84     Death. 
COMPBIAS   29    32  4     Poly-Ala. 
MOD_RES   83    83        Phosphoserine. 
MOD_RES   463   463        Phosphoserine. 
MOD_RES   466   466        Phosphoserine. 
CARBOHYD   156   156        N-linked (GlcNAc...) (Potential). 
DISULFID   132   145        By similarity. 
DISULFID   148   164        By similarity. 
DISULFID   167   180        By similarity. 
DISULFID   170   188        By similarity. 
DISULFID   190   204        By similarity. 
DISULFID   207   221        By similarity. 
DISULFID   211   229        By similarity. 
VARIANT   11    11  1     G -> V (in dbSNP:rs34737614 [NCBI]). VAR_052349 
VARIANT   33    33  1     T -> I (in dbSNP:rs20577 [NCBI]). VAR_016149 
VARIANT   105   105  1     P -> R (in dbSNP:rs11986840 [NCBI]). VAR_052350 
VARIANT   141   141  1     H -> R (in dbSNP:rs6557634 [NCBI]). VAR_016150 
VARIANT   209   209  1     R -> T (in dbSNP:rs20575 [NCBI]). VAR_016151 
VARIANT   228   228  1     E -> A (in dbSNP:rs20576 [NCBI]). VAR_016152 
VARIANT   297   297  1     N -> H (in dbSNP:rs17088980 [NCBI]). VAR_052351 
VARIANT   441   441  1     K -> R (in dbSNP:rs2230229 [NCBI]). VAR_052352 
CONFLICT   281   281        W -> C (in Ref. 2; BAF83988). 
Sequence information
Length: 468 AA [This is the length of the unprocessed precursor] Molecular weight: 50061 Da [This is the MW of the unprocessed precursor] CRC64: 7E9661859A550CD4 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPPPARVHL GAFLAVTPNP GSAASGTEAA AATPSKVWGS SAGRIEPRGG GRGALPTSMG 

        70         80         90        100        110        120 
QHGPSARARA GRAPGPRPAR EASPRLRVHK TFKFVVVGVL LQVVPSSAAT IKLHDQSIGT 

       130        140        150        160        170        180 
QQWEHSPLGE LCPPGSHRSE HPGACNRCTE GVGYTNASNN LFACLPCTAC KSDEEERSPC 

       190        200        210        220        230        240 
TTTRNTACQC KPGTFRNDNS AEMCRKCSRG CPRGMVKVKD CTPWSDIECV HKESGNGHNI 

       250        260        270        280        290        300 
WVILVVTLVV PLLLVAVLIV CCCIGSGCGG DPKCMDRVCF WRLGLLRGPG AEDNAHNEIL 

       310        320        330        340        350        360 
SNADSLSTFV SEQQMESQEP ADLTGVTVQS PGEAQCLLGP AEAEGSQRRR LLVPANGADP 

       370        380        390        400        410        420 
TETLMLFFDK FANIVPFDSW DQLMRQLDLT KNEIDVVRAG TAGPGDALYA MLMKWVNKTG 

       430        440        450        460 
RNASIHTLLD ALERMEERHA KEKIQDLLVD SGKFIYLEDG TGSAVSLE 

O00220 in FASTA format

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