Q9ESE2 (TNF11_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor necrosis factor ligand superfamily member 11

Alternative name(s):
Osteoclast differentiation factor
Short name=ODF
Osteoprotegerin ligand
Short name=OPGL
Receptor activator of nuclear factor kappa-B ligand
Short name=RANKL
TNF-related activation-induced cytokine
Short name=TRANCE
CD_antigen=CD254

Cleaved into the following 2 chains:

1. Tumor necrosis factor ligand superfamily member 11, membrane form
2. Tumor necrosis factor ligand superfamily member 11, soluble form

Gene names

Name:	Tnfsf11
Synonyms:	Opgl, Rankl, Trance

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
Subunit structure	Homotrimer. Interacts with TNFRSF11A and TNFRSF11B By similarity.
Subcellular location	Cell membrane; Single-pass type II membrane protein By similarity. Tumor necrosis factor ligand superfamily member 11, soluble form: Secreted By similarity.
Tissue specificity	Highly expressed in thymus and bone tissues.
Post-translational modification	The soluble form derives from the membrane form by proteolytic processing By similarity.
Sequence similarities	Belongs to the tumor necrosis factor family.

Ontologies

Keywords
Biological process	Differentiation
Cellular component	Cell membrane Membrane Secreted
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Cytokine Developmental protein Receptor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW immune response Inferred from electronic annotation. Source: InterPro multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of bone resorption Inferred from mutant phenotype Ref.1. Source: RGD positive regulation of osteoclast differentiation Inferred from mutant phenotype Ref.1. Source: RGD response to radiation Inferred from expression pattern PubMed 16752412. Source: RGD response to stress Inferred from expression pattern PubMed 18380564. Source: RGD
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 318	318	Tumor necrosis factor ligand superfamily member 11, membrane form		PRO_0000034518
	Chain	141 – 318	178	Tumor necrosis factor ligand superfamily member 11, soluble form		PRO_0000034519
Regions
	Topological domain	1 – 47	47	Cytoplasmic Potential
	Transmembrane	48 – 68	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	69 – 318	250	Extracellular Potential
Sites
	Site	140 – 141	2	Cleavage By similarity
Amino acid modifications
	Glycosylation	199	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	317	1	I → M in AAL23963. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9ESE2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4B87A4D706AD098F	FASTA	318	35,370
	10 20 30 40 50 60 MRRANRDYGK YLRGSEEMGS CPGVPHEGPL HPAPSAPAPA PPPAASRFMF LALLGLGLGQ 70 80 90 100 110 120 VVCSIALFLY FRAQMDPNRI SEDSTRCFYR ILRLRENTGL QDSTLESEDT EALPDSCRRM 130 140 150 160 170 180 KQAFQGAVQR ELQHIVGPQR FSGVPAMMEG SWLDVARRGK PEAQPFAHLT INAADIPSGS 190 200 210 220 230 240 HKVSLSSWYH DRGWAKISNM TLSNGKLRVN QDGFYYLYAN ICFRHHETSG SVPADYLQLM 250 260 270 280 290 300 VYVVKTSIKI PSSHNLMKGG STKNWSGNSE FHFYSINVGG FFKLRAGEEI SVQVSNPSLL 310 DPDQDATYFG AFKVQDID

References

[1]	"Cloning, sequence and functional characterization of the rat homologue of receptor activator of NF-kB ligand." Xu J.K., Tan J.K., Huang L., Gao X.H., Laird R., Liu D., Wysocki S., Zheng M.H. J. Bone Miner. Res. 15:2178-2186(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Tibial bone.
[2]	"Evidence that the rat osteopetrotic mutation toothless (tl) is not in the TNFSF11 (TRANCE, RANKL, ODF, OPGL) gene." Odgren P.R., Kim N., van Wesenbeeck L., MacKay C., Mason-Savas A., Safadi F.F., Popoff S.N., Lengner C., van-Hul W., Choi Y., Marks S.C. Jr. Int. J. Dev. Biol. 45:853-859(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 266-318. Strain: Fischer 344.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF187319 mRNA. Translation: AAG17031.1. AF425669 mRNA. Translation: AAL23963.1.
IPI	IPI00191877.
RefSeq	NP_476490.1. NM_057149.1.
UniGene	Rn.217570. Rn.64517.
3D structure databases
ProteinModelPortal	Q9ESE2.
SMR	Q9ESE2. Positions 163-318.
ModBase	Search...
Proteomic databases
PaxDb	Q9ESE2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	117516.
KEGG	rno:117516.
UCSC	RGD:620784. rat.
Organism-specific databases
CTD	8600.
RGD	620784. Tnfsf11.
Phylogenomic databases
eggNOG	NOG40842.
HOGENOM	HOG000132981.
HOVERGEN	HBG054257.
InParanoid	Q9ESE2.
KO	K05473.
OrthoDB	EOG4FTW12.
Gene expression databases
ArrayExpress	Q9ESE2.
Genevestigator	Q9ESE2.
GermOnline	ENSRNOG00000009559. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.120.40. 1 hit.
InterPro	IPR006052. TNF. IPR017355. TNF_ligand_10/11. IPR008983. Tumour_necrosis_fac-like_dom. [Graphical view]
Pfam	PF00229. TNF. 1 hit. [Graphical view]
PIRSF	PIRSF038013. TNF10_TNF11. 1 hit.
SMART	SM00207. TNF. 1 hit. [Graphical view]
SUPFAM	SSF49842. TNF_like. 1 hit.
PROSITE	PS00251. TNF_1. False negative. PS50049. TNF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	620273.

Entry information

Entry name

TNF11_RAT

Accession

Primary (citable) accession number: Q9ESE2
Secondary accession number(s): Q91ZI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program