TNF10_MOUSE
ID TNF10_MOUSE Reviewed; 291 AA.
AC P50592;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 10;
DE AltName: Full=TNF-related apoptosis-inducing ligand;
DE Short=Protein TRAIL;
DE AltName: CD_antigen=CD253;
GN Name=Tnfsf10; Synonyms=Trail;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8777713; DOI=10.1016/1074-7613(95)90057-8;
RA Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K.,
RA Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G.;
RT "Identification and characterization of a new member of the TNF family that
RT induces apoptosis.";
RL Immunity 3:673-682(1995).
CC -!- FUNCTION: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2,
CC TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to
CC TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by
CC binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and
CC TNFRSF11B/OPG that cannot induce apoptosis.
CC {ECO:0000250|UniProtKB:P50591}.
CC -!- SUBUNIT: Homotrimer. One TNFSF10 homotrimer interacts with three
CC TNFSF10A mononers. One TNFSF10 homotrimer interacts with three TNFSF10B
CC mononers. {ECO:0000250|UniProtKB:P50591}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P50591};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P50591}.
CC Secreted {ECO:0000250|UniProtKB:P50591}. Note=Exists both as membrane-
CC bound and soluble form. {ECO:0000250|UniProtKB:P50591}.
CC -!- TISSUE SPECIFICITY: Widespread.
CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC {ECO:0000250|UniProtKB:P50591}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; U37522; AAC52345.1; -; mRNA.
DR CCDS; CCDS17272.1; -.
DR RefSeq; NP_033451.1; NM_009425.2.
DR AlphaFoldDB; P50592; -.
DR SMR; P50592; -.
DR STRING; 10090.ENSMUSP00000040271; -.
DR GlyGen; P50592; 1 site.
DR iPTMnet; P50592; -.
DR PhosphoSitePlus; P50592; -.
DR PaxDb; P50592; -.
DR PRIDE; P50592; -.
DR ProteomicsDB; 259272; -.
DR Antibodypedia; 3728; 1327 antibodies from 51 providers.
DR DNASU; 22035; -.
DR Ensembl; ENSMUST00000046383; ENSMUSP00000040271; ENSMUSG00000039304.
DR GeneID; 22035; -.
DR KEGG; mmu:22035; -.
DR UCSC; uc008otm.1; mouse.
DR CTD; 8743; -.
DR MGI; MGI:107414; Tnfsf10.
DR VEuPathDB; HostDB:ENSMUSG00000039304; -.
DR eggNOG; ENOG502QQ3R; Eukaryota.
DR GeneTree; ENSGT01050000244878; -.
DR HOGENOM; CLU_070352_1_0_1; -.
DR InParanoid; P50592; -.
DR OMA; CVAVTYM; -.
DR OrthoDB; 1404113at2759; -.
DR PhylomeDB; P50592; -.
DR TreeFam; TF332169; -.
DR Reactome; R-MMU-3371378; Regulation by c-FLIP.
DR Reactome; R-MMU-5218900; CASP8 activity is inhibited.
DR Reactome; R-MMU-69416; Dimerization of procaspase-8.
DR Reactome; R-MMU-75158; TRAIL signaling.
DR BioGRID-ORCS; 22035; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Tnfsf10; mouse.
DR PRO; PR:P50592; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P50592; protein.
DR Bgee; ENSMUSG00000039304; Expressed in small intestine Peyer's patch and 102 other tissues.
DR ExpressionAtlas; P50592; baseline and differential.
DR Genevisible; P50592; MM.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0045569; F:TRAIL binding; IDA:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0032813; F:tumor necrosis factor receptor superfamily binding; IPI:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR021184; TNF_CS.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR017355; TNF_ligand_10/11.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR PIRSF; PIRSF038013; TNF10_TNF11; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS00251; TNF_1; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell membrane; Cytokine; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..291
FT /note="Tumor necrosis factor ligand superfamily member 10"
FT /id="PRO_0000185504"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between all trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P50591"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 291 AA; 33477 MW; 3FEACAB9F0D7D802 CRC64;
MPSSGALKDL SFSQHFRMMV ICIVLLQVLL QAVSVAVTYM YFTNEMKQLQ DNYSKIGLAC
FSKTDEDFWD STDGEILNRP CLQVKRQLYQ LIEEVTLRTF QDTISTVPEK QLSTPPLPRG
GRPQKVAAHI TGITRRSNSA LIPISKDGKT LGQKIESWES SRKGHSFLNH VLFRNGELVI
EQEGLYYIYS QTYFRFQEAE DASKMVSKDK VRTKQLVQYI YKYTSYPDPI VLMKSARNSC
WSRDAEYGLY SIYQGGLFEL KKNDRIFVSV TNEHLMDLDQ EASFFGAFLI N
