TNF12_MOUSE
ID TNF12_MOUSE Reviewed; 249 AA.
AC O54907; Q9CTP2;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 12;
DE AltName: Full=TNF-related weak inducer of apoptosis;
DE Short=TWEAK;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 12, membrane form;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 12, secreted form;
GN Name=Tnfsf12;
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].
RA Chicheportiche Y., Bixler S., Tizard R., Browning J.L.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-249.
RC TISSUE=Peritoneal macrophage;
RX PubMed=9405449; DOI=10.1074/jbc.272.51.32401;
RA Chicheportiche Y., Bourdon P.R., Xu H., Hsu Y.-M., Scott H., Hession C.,
RA Garcia I., Browning J.L.;
RT "TWEAK, a new secreted ligand in the tumor necrosis factor family that
RT weakly induces apoptosis.";
RL J. Biol. Chem. 272:32401-32410(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-249.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak
CC inducer of apoptosis in some cell types. Mediates NF-kappa-B
CC activation. Promotes angiogenesis and the proliferation of endothelial
CC cells. Also involved in induction of inflammatory cytokines. Promotes
CC IL8 secretion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Interacts with the angiogenic factor AGGF1/VG5Q
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
CC 12, secreted form]: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: The soluble form is produced from the membrane form by proteolytic
CC processing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF030100; AAC53517.2; -; mRNA.
DR EMBL; AK020909; BAB32249.1; -; mRNA.
DR CCDS; CCDS24907.1; -.
DR RefSeq; NP_035744.1; NM_011614.3.
DR AlphaFoldDB; O54907; -.
DR SMR; O54907; -.
DR STRING; 10090.ENSMUSP00000137972; -.
DR GlyGen; O54907; 1 site.
DR PhosphoSitePlus; O54907; -.
DR PaxDb; O54907; -.
DR PRIDE; O54907; -.
DR ProteomicsDB; 260718; -.
DR Antibodypedia; 34916; 550 antibodies from 41 providers.
DR DNASU; 21944; -.
DR Ensembl; ENSMUST00000181810; ENSMUSP00000137972; ENSMUSG00000097328.
DR GeneID; 21944; -.
DR KEGG; mmu:21944; -.
DR UCSC; uc007jri.2; mouse.
DR CTD; 8742; -.
DR MGI; MGI:1196259; Tnfsf12.
DR VEuPathDB; HostDB:ENSMUSG00000097328; -.
DR eggNOG; ENOG502RN22; Eukaryota.
DR GeneTree; ENSGT00940000163167; -.
DR HOGENOM; CLU_090519_0_0_1; -.
DR InParanoid; O54907; -.
DR OMA; PRCELNP; -.
DR OrthoDB; 1319236at2759; -.
DR PhylomeDB; O54907; -.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR BioGRID-ORCS; 21944; 0 hits in 70 CRISPR screens.
DR PRO; PR:O54907; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O54907; protein.
DR Bgee; ENSMUSG00000097328; Expressed in retinal neural layer and 206 other tissues.
DR ExpressionAtlas; O54907; baseline and differential.
DR Genevisible; O54907; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Apoptosis; Cell membrane; Cleavage on pair of basic residues;
KW Cytokine; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..249
FT /note="Tumor necrosis factor ligand superfamily member 12,
FT membrane form"
FT /id="PRO_0000034522"
FT CHAIN 94..249
FT /note="Tumor necrosis factor ligand superfamily member 12,
FT secreted form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034523"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 52..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 93..94
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..210
FT /evidence="ECO:0000250"
SQ SEQUENCE 249 AA; 27441 MW; 08352620444EFB7B CRC64;
MAARRSQRRR GRRGEPGTAL LAPLVLSLGL ALACLGLLLV VVSLGSWATL SAQEPSQEEL
TAEDRREPPE LNPQTEESQD VVPFLEQLVR PRRSAPKGRK ARPRRAIAAH YEVHPRPGQD
GAQAGVDGTV SGWEETKINS SSPLRYDRQI GEFTVIRAGL YYLYCQVHFD EGKAVYLKLD
LLVNGVLALR CLEEFSATAA SSPGPQLRLC QVSGLLPLRP GSSLRIRTLP WAHLKAAPFL
TYFGLFQVH
