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Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form]

 TNF11_MOUSE             Reviewed;         316 AA.
O35235; O35306; Q3TWY5; Q9JJK8; Q9JJK9; Q9R1Y0;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 169.
RecName: Full=Tumor necrosis factor ligand superfamily member 11;
AltName: Full=Osteoclast differentiation factor;
Short=ODF;
AltName: Full=Osteoprotegerin ligand;
Short=OPGL;
AltName: Full=Receptor activator of nuclear factor kappa-B ligand;
Short=RANKL;
AltName: Full=TNF-related activation-induced cytokine;
Short=TRANCE;
AltName: CD_antigen=CD254;
Contains:
RecName: Full=Tumor necrosis factor ligand superfamily member 11, membrane form;
Contains:
RecName: Full=Tumor necrosis factor ligand superfamily member 11, soluble form;
Name=Tnfsf11; Synonyms=Opgl, Rankl, Trance;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hybridoma;
PubMed=9312132; DOI=10.1074/jbc.272.40.25190;
Wong B.R., Rho J., Arron J., Robinson E., Orlinick J., Chao M.,
Kalachikov S., Cayani E., Bartlett F.S. III, Frankel W.N., Lee S.Y.,
Choi Y.;
"TRANCE is a novel ligand of the tumor necrosis factor receptor family
that activates c-Jun N-terminal kinase in T cells.";
J. Biol. Chem. 272:25190-25194(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Thymic lymphoma;
PubMed=9367155; DOI=10.1038/36593;
Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C.,
Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D.,
Galibert L.;
"A homologue of the TNF receptor and its ligand enhance T-cell growth
and dendritic-cell function.";
Nature 390:175-179(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=9568710; DOI=10.1016/S0092-8674(00)81569-X;
Lacey D.L., Timms E., Tan H.-L., Kelley M.J., Dunstan C.R.,
Burgess T., Elliott R., Colombero A., Elliott G., Scully S., Hsu H.,
Sullivan J., Hawkins N., Davy E., Capparelli C., Eli A., Qian Y.-X.,
Kaufman S., Sarosi I., Shalhoub V., Senaldi G., Guo J., Delaney J.,
Boyle W.J.;
"Osteoprotegerin ligand is a cytokine that regulates osteoclast
differentiation and activation.";
Cell 93:165-176(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Bone marrow stroma;
PubMed=9520411; DOI=10.1073/pnas.95.7.3597;
Yasuda H., Shima N., Nakagawa N., Yamaguchi K., Kinosaki M.,
Mochizuki S., Tomoyasu A., Yano K., Goto M., Murakami A., Tsuda E.,
Morinaga T., Higashio K., Udagawa N., Takahashi N., Suda T.;
"Osteoclast differentiation factor is a ligand for
osteoprotegerin/osteoclastogenesis-inhibitory factor and is identical
to TRANCE/RANKL.";
Proc. Natl. Acad. Sci. U.S.A. 95:3597-3602(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
STRAIN=129;
PubMed=10196481; DOI=10.1016/S0378-1119(99)00025-6;
Kodaira K., Kodaira K., Mizuno A., Yasuda H., Shima N., Murakami A.,
Ueda M., Higashio K.;
"Cloning and characterization of the gene encoding mouse osteoclast
differentiation factor.";
Gene 230:121-127(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=11250921; DOI=10.1210/endo.142.4.8070;
Ikeda T., Kasai M., Utsuyama M., Hirokawa K.;
"Determination of three isoforms of the receptor activator of nuclear
factor-kappaB ligand and their differential expression in bone and
thymus.";
Endocrinology 142:1419-1426(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
PROTEIN SEQUENCE OF 139-147, PROTEOLYTIC PROCESSING, AND
GLYCOSYLATION.
PubMed=10224132; DOI=10.1074/jbc.274.19.13613;
Lum L., Wong B.R., Josien R., Becherer J.D., Erdjument-Bromage H.,
Schloendorff J., Tempst P., Choi Y., Blobel C.P.;
"Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-
converting enzyme-like protease in shedding of TRANCE, a TNF family
member involved in osteoclastogenesis and dendritic cell survival.";
J. Biol. Chem. 274:13613-13618(1999).
[9]
FUNCTION.
PubMed=23395171; DOI=10.1016/j.cmet.2013.01.002;
Kim H., Kim T., Jeong B.C., Cho I.T., Han D., Takegahara N.,
Negishi-Koga T., Takayanagi H., Lee J.H., Sul J.Y., Prasad V.,
Lee S.H., Choi Y.;
"Tmem64 modulates calcium signaling during RANKL-mediated osteoclast
differentiation.";
Cell Metab. 17:249-260(2013).
[10]
FUNCTION, AND INTERACTION WITH FBN1.
PubMed=24039232; DOI=10.1242/jcs.127571;
Tiedemann K., Boraschi-Diaz I., Rajakumar I., Kaur J., Roughley P.,
Reinhardt D.P., Komarova S.V.;
"Fibrillin-1 directly regulates osteoclast formation and function by a
dual mechanism.";
J. Cell Sci. 126:4187-4194(2013).
[11]
FUNCTION.
PubMed=26644563; DOI=10.1073/pnas.1511285112;
Decker C.E., Yang Z., Rimer R., Park-Min K.H., Macaubas C.,
Mellins E.D., Novack D.V., Faccio R.;
"Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
regulate bone mass.";
Proc. Natl. Acad. Sci. U.S.A. 112:15654-15659(2015).
[12]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 158-316, AND SUBUNIT.
PubMed=11581298; DOI=10.1172/JCI13890;
Lam J., Nelson C.A., Ross F.P., Teitelbaum S.L., Fremont D.H.;
"Crystal structure of the TRANCE/RANKL cytokine reveals determinants
of receptor-ligand specificity.";
J. Clin. Invest. 108:971-979(2001).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 137-316, AND SUBUNIT.
PubMed=11733492; DOI=10.1074/jbc.M106525200;
Ito S., Wakabayashi K., Ubukata O., Hayashi S., Okada F., Hata T.;
"Crystal structure of the extracellular domain of mouse RANK ligand at
2.2-A resolution.";
J. Biol. Chem. 277:6631-6636(2002).
[14]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 158-316 IN COMPLEX WITH
TNFRSF11A, INTERACTION WITH TNFRSF11A, AND SUBUNIT.
PubMed=20483727; DOI=10.4049/jimmunol.0904033;
Liu C., Walter T.S., Huang P., Zhang S., Zhu X., Wu Y.,
Wedderburn L.R., Tang P., Owens R.J., Stuart D.I., Ren J., Gao B.;
"Structural and functional insights of RANKL-RANK interaction and
signaling.";
J. Immunol. 184:6910-6919(2010).
[15]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 162-316 IN COMPLEX WITH
TNFRSF11B.
PubMed=23039992; DOI=10.1016/j.str.2012.08.030;
Nelson C.A., Warren J.T., Wang M.W., Teitelbaum S.L., Fremont D.H.;
"RANKL employs distinct binding modes to engage RANK and the
osteoprotegerin decoy receptor.";
Structure 20:1971-1982(2012).
-!- 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 (By similarity). Induces
osteoclastogenesis by activating multiple signaling pathways in
osteoclast precursor cells, chief among which is induction of long
lasting oscillations in the intracellular concentration of Ca (2+)
resulting in the activation of NFATC1, which translocates to the
nucleus and induces osteoclast-specific gene transcription to
allow differentiation of osteoclasts (PubMed:24039232). During
osteoclast differentiation, in a TMEM64 and ATP2A2-dependent
manner induces activation of CREB1 and mitochondrial ROS
generation necessary for proper osteoclast generation
(PubMed:23395171, PubMed:26644563). {ECO:0000250|UniProtKB:O14788,
ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:24039232,
ECO:0000269|PubMed:26644563}.
-!- SUBUNIT: Homotrimer (PubMed:11581298, PubMed:11733492,
PubMed:20483727). Interacts with TNFRSF11A and TNFRSF11B
(PubMed:20483727, PubMed:23039992). Interacts with FBN1 (via N-
terminal domain) in a Ca(+2)-dependent manner (PubMed:24039232).
{ECO:0000269|PubMed:11581298, ECO:0000269|PubMed:11733492,
ECO:0000269|PubMed:20483727, ECO:0000269|PubMed:23039992,
ECO:0000269|PubMed:24039232}.
-!- INTERACTION:
O35305:Tnfrsf11a; NbExp=6; IntAct=EBI-15890886, EBI-647362;
O08712:Tnfrsf11b; NbExp=4; IntAct=EBI-15890886, EBI-16015871;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type
II membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type
II membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily
member 11, soluble form: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O35235-1; Sequence=Displayed;
Name=2;
IsoId=O35235-2; Sequence=VSP_006449;
Name=3;
IsoId=O35235-3; Sequence=VSP_006448;
-!- TISSUE SPECIFICITY: Highly expressed in thymus and lymph nodes,
but not in non-lymphoid tissues and is abundantly expressed in T-
cells but not in B-cells. A high level expression is also seen in
the trabecular bone and lung.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10224132}.
-!- PTM: The soluble form of isoform 1 derives from the membrane form
by proteolytic processing. The cleavage may be catalyzed by
ADAM17. A further shorter soluble form was observed.
{ECO:0000269|PubMed:10224132}.
-!- DISEASE: Note=Deficiency in Tnfsf11 results in failure to form
lobulo-alveolar mammary structures during pregnancy, resulting in
death of newborns. Trance-deficient mice show severe
osteopetrosis, with no osteoclasts, marrow spaces, or tooth
eruption, and exhibit profound growth retardation at several
skeletal sites, including the limbs, skull, and vertebrae and have
marked chondrodysplasia, with thick, irregular growth plates and a
relative increase in hypertrophic chondrocytes.
-!- SIMILARITY: Belongs to the tumor necrosis factor family.
{ECO:0000305}.
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EMBL; AF013170; AAC71061.1; -; mRNA.
EMBL; AF019048; AAB86812.1; -; mRNA.
EMBL; AF053713; AAC40113.1; -; mRNA.
EMBL; AB008426; BAA25425.1; -; mRNA.
EMBL; AB022039; BAA36970.1; -; Genomic_DNA.
EMBL; AB032771; BAA97257.1; -; mRNA.
EMBL; AB032772; BAA97258.1; -; mRNA.
EMBL; AB036798; BAA97259.1; -; mRNA.
EMBL; AK159498; BAE35131.1; -; mRNA.
CCDS; CCDS27294.1; -. [O35235-1]
RefSeq; NP_035743.2; NM_011613.3. [O35235-1]
UniGene; Mm.249221; -.
PDB; 1IQA; X-ray; 2.20 A; A/B/C=157-316.
PDB; 1JTZ; X-ray; 2.60 A; X/Y/Z=156-316.
PDB; 1S55; X-ray; 1.90 A; A/B/C=161-316.
PDB; 3ME2; X-ray; 2.80 A; A=158-316.
PDB; 3QBQ; X-ray; 2.50 A; A/C=157-316.
PDB; 4E4D; X-ray; 2.70 A; X=162-316.
PDB; 4GIQ; X-ray; 2.70 A; A=158-316.
PDBsum; 1IQA; -.
PDBsum; 1JTZ; -.
PDBsum; 1S55; -.
PDBsum; 3ME2; -.
PDBsum; 3QBQ; -.
PDBsum; 4E4D; -.
PDBsum; 4GIQ; -.
ProteinModelPortal; O35235; -.
SMR; O35235; -.
DIP; DIP-59480N; -.
IntAct; O35235; 2.
STRING; 10090.ENSMUSP00000022592; -.
BindingDB; O35235; -.
ChEMBL; CHEMBL3596084; -.
PhosphoSitePlus; O35235; -.
PaxDb; O35235; -.
PRIDE; O35235; -.
Ensembl; ENSMUST00000022592; ENSMUSP00000022592; ENSMUSG00000022015. [O35235-1]
GeneID; 21943; -.
KEGG; mmu:21943; -.
UCSC; uc007ush.1; mouse. [O35235-1]
CTD; 8600; -.
MGI; MGI:1100089; Tnfsf11.
eggNOG; ENOG410IEIS; Eukaryota.
eggNOG; ENOG410YGCE; LUCA.
GeneTree; ENSGT00530000063443; -.
HOGENOM; HOG000132981; -.
HOVERGEN; HBG054257; -.
InParanoid; O35235; -.
KO; K05473; -.
OMA; QDATYFG; -.
OrthoDB; EOG091G0F3S; -.
TreeFam; TF332169; -.
Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
ChiTaRS; Tnfsf11; mouse.
EvolutionaryTrace; O35235; -.
PMAP-CutDB; Q3TWY5; -.
PRO; PR:O35235; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022015; -.
Genevisible; O35235; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IPI:BHF-UCL.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:DFLAT.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0045453; P:bone resorption; IDA:MGI.
GO; GO:0055074; P:calcium ion homeostasis; IGI:MGI.
GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:DFLAT.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0048535; P:lymph node development; TAS:MGI.
GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
GO; GO:0002548; P:monocyte chemotaxis; ISO:MGI.
GO; GO:0001503; P:ossification; IMP:MGI.
GO; GO:0036035; P:osteoclast development; IDA:MGI.
GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
GO; GO:0002158; P:osteoclast proliferation; IDA:MGI.
GO; GO:0038001; P:paracrine signaling; IDA:MGI.
GO; GO:0045780; P:positive regulation of bone resorption; ISO:MGI.
GO; GO:0051466; P:positive regulation of corticotropin-releasing hormone secretion; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0071848; P:positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling; ISO:MGI.
GO; GO:0071812; P:positive regulation of fever generation by positive regulation of prostaglandin secretion; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; IGI:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:2001206; P:positive regulation of osteoclast development; IDA:MGI.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:DFLAT.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:MGI.
GO; GO:0050870; P:positive regulation of T cell activation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0045670; P:regulation of osteoclast differentiation; IDA:MGI.
GO; GO:0071847; P:TNFSF11-mediated signaling pathway; IDA:MGI.
GO; GO:0044691; P:tooth eruption; IMP:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IGI:BHF-UCL.
Gene3D; 2.60.120.40; -; 1.
InterPro; IPR006052; TNF_dom.
InterPro; IPR017355; TNF_ligand_10/11.
InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
Pfam; PF00229; TNF; 1.
PIRSF; PIRSF038013; TNF10_TNF11; 1.
SMART; SM00207; TNF; 1.
SUPFAM; SSF49842; SSF49842; 1.
PROSITE; PS50049; TNF_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytokine; Cytoplasm; Developmental protein; Differentiation;
Direct protein sequencing; Glycoprotein; Membrane; Receptor;
Reference proteome; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 316 Tumor necrosis factor ligand superfamily
member 11, membrane form.
/FTId=PRO_0000034516.
CHAIN 139 316 Tumor necrosis factor ligand superfamily
member 11, soluble form.
/FTId=PRO_0000034517.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000255}.
TRANSMEM 49 69 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 70 316 Extracellular. {ECO:0000255}.
SITE 138 139 Cleavage.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 117 Missing (in isoform 3).
{ECO:0000303|PubMed:11250921}.
/FTId=VSP_006448.
VAR_SEQ 14 44 SSEEMGSGPGVPHEGPLHPAPSAPAPAPPPA -> TP (in
isoform 2).
{ECO:0000303|PubMed:11250921}.
/FTId=VSP_006449.
CONFLICT 99 99 D -> G (in Ref. 1; AAC71061, 3; AAC40113,
4; BAA25425, 5; BAA36970 and 6; BAA97257/
BAA97259). {ECO:0000305}.
CONFLICT 141 143 Missing (in Ref. 5; BAA36970).
{ECO:0000305}.
STRAND 164 169 {ECO:0000244|PDB:1S55}.
HELIX 171 173 {ECO:0000244|PDB:3ME2}.
STRAND 177 179 {ECO:0000244|PDB:1S55}.
STRAND 181 183 {ECO:0000244|PDB:1JTZ}.
STRAND 186 190 {ECO:0000244|PDB:1S55}.
STRAND 194 201 {ECO:0000244|PDB:1S55}.
STRAND 204 207 {ECO:0000244|PDB:1S55}.
STRAND 211 224 {ECO:0000244|PDB:1S55}.
HELIX 225 227 {ECO:0000244|PDB:1S55}.
STRAND 233 248 {ECO:0000244|PDB:1S55}.
STRAND 251 262 {ECO:0000244|PDB:1S55}.
STRAND 265 282 {ECO:0000244|PDB:1S55}.
STRAND 286 293 {ECO:0000244|PDB:1S55}.
HELIX 295 297 {ECO:0000244|PDB:1S55}.
TURN 302 304 {ECO:0000244|PDB:1S55}.
STRAND 305 313 {ECO:0000244|PDB:1S55}.
SEQUENCE 316 AA; 35003 MW; 8AF3825F92E0A786 CRC64;
MRRASRDYGK YLRSSEEMGS GPGVPHEGPL HPAPSAPAPA PPPAASRSMF LALLGLGLGQ
VVCSIALFLY FRAQMDPNRI SEDSTHCFYR ILRLHENADL QDSTLESEDT LPDSCRRMKQ
AFQGAVQKEL QHIVGPQRFS GAPAMMEGSW LDVAQRGKPE AQPFAHLTIN AASIPSGSHK
VTLSSWYHDR GWAKISNMTL SNGKLRVNQD GFYYLYANIC FRHHETSGSV PTDYLQLMVY
VVKTSIKIPS SHNLMKGGST KNWSGNSEFH FYSINVGGFF KLRAGEEISI QVSNPSLLDP
DQDATYFGAF KVQDID


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