TNF15_RAT
ID TNF15_RAT Reviewed; 252 AA.
AC Q8K3Y7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 15;
DE AltName: Full=TNF ligand-related molecule 1;
DE AltName: Full=Vascular endothelial cell growth inhibitor;
GN Name=Tnfsf15; Synonyms=Tl1, Vegi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=11911831; DOI=10.1016/s1074-7613(02)00283-2;
RA Migone T.-S., Zhang J., Luo X., Zhuang L., Chen C., Hu B., Hong J.S.,
RA Perry J.W., Chen S.-F., Zhou J.X.H., Cho Y.H., Ullrich S., Kanakaraj P.,
RA Carrell J., Boyd E., Olsen H.S., Hu G., Pukac L., Liu D., Ni J., Kim S.,
RA Gentz R., Feng P., Moore P.A., Ruben S.M., Wei P.;
RT "TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell
RT costimulator.";
RL Immunity 16:479-492(2002).
CC -!- FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of
CC NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in
CC vitro). Promotes activation of caspases and apoptosis. Promotes
CC splenocyte alloactivation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF520787; AAM77368.1; -; mRNA.
DR RefSeq; NP_665708.1; NM_145765.1.
DR AlphaFoldDB; Q8K3Y7; -.
DR SMR; Q8K3Y7; -.
DR STRING; 10116.ENSRNOP00000011845; -.
DR GlyGen; Q8K3Y7; 2 sites.
DR PaxDb; Q8K3Y7; -.
DR GeneID; 252878; -.
DR KEGG; rno:252878; -.
DR UCSC; RGD:628735; rat.
DR CTD; 9966; -.
DR RGD; 628735; Tnfsf15.
DR eggNOG; ENOG502S4Q1; Eukaryota.
DR HOGENOM; CLU_070352_3_0_1; -.
DR InParanoid; Q8K3Y7; -.
DR OrthoDB; 1154153at2759; -.
DR PhylomeDB; Q8K3Y7; -.
DR TreeFam; TF332169; -.
DR Reactome; R-RNO-5669034; TNFs bind their physiological receptors.
DR PRO; PR:Q8K3Y7; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005123; F:death receptor binding; IDA:RGD.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:RGD.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:RGD.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR006053; TNF.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008064; TNFSF15.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR PANTHER; PTHR11471:SF24; PTHR11471:SF24; 1.
DR Pfam; PF00229; TNF; 1.
DR PRINTS; PR01234; TNECROSISFCT.
DR SMART; SM00207; TNF; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..252
FT /note="Tumor necrosis factor ligand superfamily member 15"
FT /id="PRO_0000333233"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 188
FT /note="Important for binding TNFRSF6B"
FT /evidence="ECO:0000250"
FT SITE 191
FT /note="Important for binding TNFRSF6B"
FT /evidence="ECO:0000250"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..203
FT /evidence="ECO:0000250"
SQ SEQUENCE 252 AA; 28029 MW; 7789E6556D46F293 CRC64;
MAEELGLGFG EAVPVEMLPE GCRHRREART GLAARSKACL ALTCCLLSFP ILAGLSTLLM
TGQLRIPGKD CMFPTVTEER SAPSAQPVYT PSRDKPKAHL TIMRQTPVPH LKNELAALHW
ENNLGMAFTK NRMNYTNKFL VIPESGDYFI YSQITFRGTT SECGDISRVR RPKKPDSITV
VITKVADSYP EPAHLLTGTK SVCEISSNWF QPIYLGAMFS LEEGDRLMVN VSDISLVDYT
KEDKTFFGAF LI