Tumor necrosis factor ligand superfamily member 10

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Reviewed, UniProtKB/Swiss-Prot P50591 (TNF10_HUMAN)

Last modified November 25, 2008. Version 86. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Tumor necrosis factor ligand superfamily member 10
Alternative name(s):
    TNF-related apoptosis-inducing ligand
      Short name=Protein TRAIL
    Apo-2 ligand
      Short name=Apo-2L
    CD_antigen=CD253

Gene names

Name:	TNFSF10
Synonyms:	APO2L, TRAIL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis.
Cofactor	Binds 1 zinc ion per trimer.
Subunit structure	Homotrimer.
Subcellular location	Membrane; Single-pass type II membrane proteinPotential.
Tissue specificity	Widespread; most predominant in spleen, lung and prostate.
Sequence similarities	Belongs to the tumor necrosis factor family.

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Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane
Domain	Signal-anchor Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Cytokine
Technical term	3D-structure
Gene Ontology (GO)
Biological process	activation of pro-apoptotic gene products Inferred from Experiment. Source: Reactome cell-cell signaling Ref.1 Traceable author statement. Source: ProtInc immune response Inferred from electronic annotation. Source: InterPro induction of apoptosis Ref.2 Traceable author statement. Source: ProtInc positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern. Source: UniProtKB
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW integral to plasma membrane Ref.2 Traceable author statement. Source: ProtInc soluble fraction Ref.2 Traceable author statement. Source: ProtInc
Molecular function	tumor necrosis factor receptor binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 281

281

Tumor necrosis factor ligand superfamily member 10

PRO_0000185503

Regions

Topological domain

1 – 17

Cytoplasmic Potential

Transmembrane

18 – 38

Signal-anchor for type II membrane protein Potential

Topological domain

39 – 281

243

Extracellular Potential

Sites

Metal binding

230

Zinc

Secondary structure

281

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P50591-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DDAAAF78DAAB2F6D
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FASTA

281

32,509

        10         20         30         40         50         60 
MAMMEVQGGP SLGQTCVLIV IFTVLLQSLC VAVTYVYFTN ELKQMQDKYS KSGIACFLKE 

        70         80         90        100        110        120 
DDSYWDPNDE ESMNSPCWQV KWQLRQLVRK MILRTSEETI STVQEKQQNI SPLVRERGPQ 

       130        140        150        160        170        180 
RVAAHITGTR GRSNTLSSPN SKNEKALGRK INSWESSRSG HSFLSNLHLR NGELVIHEKG 

       190        200        210        220        230        240 
FYYIYSQTYF RFQEEIKENT KNDKQMVQYI YKYTSYPDPI LLMKSARNSC WSKDAEYGLY 

       250        260        270        280 
SIYQGGIFEL KENDRIFVSV TNEHLIDMDH EASFFGAFLV G

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a new member of the TNF family that induces apoptosis." Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K., Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G. Immunity 3:673-682(1995) [PubMed: 8777713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family." Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A. J. Biol. Chem. 271:12687-12690(1996) [PubMed: 8663110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[3]	"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]. Tissue: Lymph.
[4]	"Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5." Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., Kelley R.F., Ashkenazi A., de Vos A.M. Mol. Cell 4:563-571(1999) [PubMed: 10549288] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 114-281.
[5]	"Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation." Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y., Screaton G.R. Nat. Struct. Biol. 6:1048-1053(1999) [PubMed: 10542098] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 119-281.
[6]	"2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity." Cha S.-S., Kim M.S., Choi Y.H., Sung B.J., Shin N.K., Shin H.C., Sung Y.C., Oh B.-H. Immunity 11:253-261(1999) [PubMed: 10485660] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-281.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U37518 mRNA. Translation: AAC50332.1.
U57059 mRNA. Translation: AAB01233.1.
BC032722 mRNA. Translation: AAH32722.1.

RefSeq

NP_003801.1.

UniGene

Hs.478275

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D0G	X-ray	2.40	A/B/D	114-281	[»]
1D2Q	X-ray	2.80	A	114-281	[»]
1D4V	X-ray	2.20	B	119-281	[»]
1DG6	X-ray	1.30	A	91-281	[»]
1DU3	X-ray	2.20	D/E/F/J/K/L	114-281	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6230N.

IntAct

P50591.

PTM databases

PhosphoSite

P50591.

Genome annotation databases

Ensembl

ENSG00000121858. Homo sapiens. [Contig view]

GeneID

8743.

KEGG

hsa:8743.

Organism-specific databases

H-InvDB

HIX0003863.

HGNC

HGNC:11925. TNFSF10.

HPA

CAB002446.

MIM

603598. gene.

PharmGKB

PA36618.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P50591.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P50591.

CleanEx

HS_TNFSF10.

GermOnline

ENSG00000121858. Homo sapiens.

Family and domain databases

InterPro

IPR017355. TNF10_TNF11.
IPR006052. TNF_family.
IPR008983. Tumour_necrosis_fac-like.
[Graphical view]

Gene3D

G3DSA:2.60.120.40. Tumour_necrosis_fac-like. 1 hit.

Pfam

PF00229. TNF. 1 hit.
[Graphical view]

PIRSF

PIRSF038013. TNF10_TNF11. 1 hit.

ProDom

PD002012. TNF_subf. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00207. TNF. 1 hit.
[Graphical view]

PROSITE

PS00251. TNF_1. 1 hit.
PS50049. TNF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

32805.

SOURCE

Search...

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Entry information

Entry name

TNF10_HUMAN

Accession

Primary (citable) accession number: P50591

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents