Reviewed, UniProtKB/Swiss-Prot O14798 (TR10C_HUMAN)

Names and origin

Protein names

Recommended name:
    Tumor necrosis factor receptor superfamily member 10C
Alternative name(s):
    Decoy receptor 1
      Short name=DcR1
    Decoy TRAIL receptor without death domain
    TNF-related apoptosis-inducing ligand receptor 3
      Short name=TRAIL receptor 3
      Short name=TRAIL-R3
    Trail receptor without an intracellular domain
    Lymphocyte inhibitor of TRAIL
    Antagonist decoy receptor for TRAIL/Apo-2L
    CD_antigen=CD263

Gene names

Name:	TNFRSF10C
Synonyms:	DCR1, LIT, TRAILR3, TRID
ORF Names:	UNQ321/PRO366

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	259 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Tissue specificity	Higher expression in normal tissues than in tumor cell lines. Highly expressed in peripheral blood lymphocytes, spleen, skeletal muscle, placenta, lung and heart.
Post-translational modification	N-glycosylated and O-glycosylated.
Sequence similarities	Contains 3 TNFR-Cys repeats.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Molecular function	Receptor
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Ref.2 Traceable author statement. Source: ProtInc
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc
Molecular function	transmembrane receptor activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Ref.10
	Chain	24 – 236	213	Tumor necrosis factor receptor superfamily member 10C		PRO_0000034582
	Propeptide	237 – 259	23	Removed in mature form Potential		PRO_0000034583
Regions
	Repeat	29 – 66	38	TNFR-Cys 1
	Repeat	69 – 109	41	TNFR-Cys 2
	Repeat	110 – 149	40	TNFR-Cys 3
	Repeat	162 – 176	15	1
	Repeat	177 – 191	15	2
	Repeat	192 – 206	15	3
	Repeat	207 – 221	15	4
	Repeat	222 – 236	15	5
	Region	162 – 236	75	5 X 15 AA tandem TAPE repeats
Amino acid modifications
	Lipidation	236	1	GPI-anchor amidated alanine Potential
	Glycosylation	77	1	N-linked (GlcNAc...) (high mannose) Potential
	Glycosylation	140	1	N-linked (GlcNAc...) (high mannose) Potential
	Glycosylation	156	1	N-linked (GlcNAc...) (high mannose) Potential
	Disulfide bond	53 ↔ 66		By similarity
	Disulfide bond	69 ↔ 85		By similarity
	Disulfide bond	88 ↔ 101		By similarity
	Disulfide bond	91 ↔ 109		By similarity
	Disulfide bond	111 ↔ 125		By similarity
	Disulfide bond	128 ↔ 141		By similarity
	Disulfide bond	131 ↔ 149		By similarity
Natural variations
	Natural variant	199	1	T → N: dbSNP rs12550828.		VAR_046534
	Natural variant	229	1	T → I: dbSNP rs9644063. Ref.8		VAR_046535
Experimental info
	Sequence conflict	119	1	E → V in AAB81181. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O14798-1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: FE3BF7FCEEAE50B8	FASTA	259	27,395
	10 20 30 40 50 60 MARIPKTLKF VVVIVAVLLP VLAYSATTAR QEEVPQQTVA PQQQRHSFKG EECPAGSHRS 70 80 90 100 110 120 EHTGACNPCT EGVDYTNASN NEPSCFPCTV CKSDQKHKSS CTMTRDTVCQ CKEGTFRNEN 130 140 150 160 170 180 SPEMCRKCSR CPSGEVQVSN CTSWDDIQCV EEFGANATVE TPAAEETMNT SPGTPAPAAE 190 200 210 220 230 240 ETMNTSPGTP APAAEETMTT SPGTPAPAAE ETMTTSPGTP APAAEETMTT SPGTPASSHY 250 LSCTIVGIIV LIVLLIVFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL." MacFarlane M., Ahmad M., Srinivasula S.M., Fernandes-Alnemri T., Cohen G.M., Alnemri E.S. J. Biol. Chem. 272:25417-25420(1997) [PubMed: 9325248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family." Degli-Esposti M.A., Smolak P.J., Walczak H., Waugh J., Huang C.-P., DuBose R.F., Goodwin R.G., Smith C.A. J. Exp. Med. 186:1165-1170(1997) [PubMed: 9314565] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Foreskin fibroblast.
[3]	"An antagonist decoy receptor and a death domain-containing receptor for TRAIL." Pan G., Ni J., Wei Y.-F., Yu G.-L., Gentz R., Dixit V.M. Science 277:815-818(1997) [PubMed: 9242610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors." Sheridan J.P., Marsters S.A., Pitti R.M., Gurney A., Skubatch M., Baldwin D.T., Ramakrishnan L., Gray C.L., Baker K., Wood W.I., Goddard A.D., Godowski P.J., Ashkenazi A. Science 277:818-821(1997) [PubMed: 9242611] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS.
[5]	"Characterization of two receptors for TRAIL." Schneider P., Bodmer J.-L., Thome M., Hofmann K., Holler N., Tschopp J. FEBS Lett. 416:329-334(1997) [PubMed: 9373179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Liver and Spleen.
[6]	"Lymphocyte inhibitor of TRAIL (TNF-related apoptosis-inducing ligand): a new receptor protecting lymphocytes from the death ligand TRAIL." Mongkolsapaya J., Cowper A.E., Xu X.-N., Morris G., McMichael A.J., Bell J.I., Screaton G.R. J. Immunol. 160:3-6(1998) [PubMed: 9551946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-229.
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-38.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF020502 mRNA. Translation: AAB71413.1. Different initiation. AF014794 mRNA. Translation: AAC05593.1. Different initiation. AF012629 mRNA. Translation: AAB67110.1. AF012536 mRNA. Translation: AAB67104.1. AF016267 mRNA. Translation: AAB81181.1. AF033854 mRNA. Translation: AAB87506.1. AY358281 mRNA. Translation: AAQ88648.1. Different initiation. CR541857 mRNA. Translation: CAG46655.1. BC125041 mRNA. Translation: AAI25042.1. BC125042 mRNA. Translation: AAI25043.1.
IPI	IPI00021970.
RefSeq	NP_003832.2.
UniGene	Hs.655801
3D structure databases
HSSP	HSSP built from PDB template 1D4V based on UniProtKB O14763.
ModBase	Search...
Protein-protein interaction databases
IntAct	O14798. 5 interactions.
Proteomic databases
PRIDE	O14798.
Genome annotation databases
Ensembl	ENSG00000173535. Homo sapiens. [Contig view]
GeneID	8794.
KEGG	hsa:8794.
Organism-specific databases
GeneCards	GC08P022997.
H-InvDB	HIX0019534.
HGNC	HGNC:11906. TNFRSF10C.
MIM	603613. gene.
PharmGKB	PA36599.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O14798.
HOVERGEN	O14798.
Enzyme and pathway databases
Pathway_Interaction_DB	trail_pathway. TRAIL signaling pathway.
Gene expression databases
ArrayExpress	O14798.
Bgee	O14798.
CleanEx	HS_TNFRSF10C.
GermOnline	ENSG00000173535. Homo sapiens.
Family and domain databases
InterPro	IPR001368. TNFR_Cys_rich_reg. [Graphical view]
Pfam	PF00020. TNFR_c6. 2 hits. [Graphical view]
SMART	SM00208. TNFR. 2 hits. [Graphical view]
PROSITE	PS00652. TNFR_NGFR_1. 2 hits. PS50050. TNFR_NGFR_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	32980.
SOURCE	Search...

Entry information

Entry name

TR10C_HUMAN

Accession

Primary (citable) accession number: O14798
Secondary accession number(s): O14755 , Q08AS6, Q6FH98, Q6UXM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	March 3, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)