TNR19_MOUSE
ID TNR19_MOUSE Reviewed; 416 AA.
AC Q9JLL3; Q80T13; Q812G3; Q9JHF1; Q9JJH6; Q9JLL2; Q9QXW7;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 19;
DE AltName: Full=TRADE;
DE AltName: Full=Toxicity and JNK inducer;
DE Flags: Precursor;
GN Name=Tnfrsf19; Synonyms=Taj, Troy;
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] (ISOFORM 4).
RX PubMed=10585776; DOI=10.1006/geno.1999.5979;
RA Hu S., Tamada K., Ni J., Vincenz C., Chen L.;
RT "Characterization of TNFRSF19, a novel member of the tumor necrosis factor
RT receptor superfamily.";
RL Genomics 62:103-107(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Embryo, and Spleen;
RX PubMed=10809768; DOI=10.1074/jbc.275.20.15336;
RA Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.;
RT "TAJ, a novel member of the tumor necrosis factor receptor family,
RT activates the c-Jun N-terminal kinase pathway and mediates caspase-
RT independent cell death.";
RL J. Biol. Chem. 275:15336-15342(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=10764796; DOI=10.1074/jbc.m002691200;
RA Kojima T., Morikawa Y., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Senba E., Kitamura T.;
RT "TROY, a newly identified member of the tumor necrosis factor receptor
RT superfamily, exhibits a homology with Edar and is expressed in embryonic
RT skin and hair follicles.";
RL J. Biol. Chem. 275:20742-20747(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Chaudhary D., Long A.J.;
RT "TRADE, a novel TNF receptor family member associated with death
RT signaling.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Czech II; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Can mediate activation of c-Jun and NF-kappa-B. May promote
CC caspase-independent cell death (By similarity). Isoform 2 and isoform 3
CC may act as decoy receptors. {ECO:0000250}.
CC -!- SUBUNIT: Associates with TRAF1, TRAF2, TRAF3 and TRAF5. Interacts with
CC LINGO1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9JLL3; P30086: PEBP1; Xeno; NbExp=4; IntAct=EBI-20800437, EBI-716384;
CC Q9JLL3; P35232: PHB; Xeno; NbExp=3; IntAct=EBI-20800437, EBI-354213;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=TAJ-alphaL;
CC IsoId=Q9JLL3-1; Sequence=Displayed;
CC Name=2; Synonyms=TAJ-beta1;
CC IsoId=Q9JLL3-2; Sequence=VSP_006513, VSP_006514;
CC Name=3; Synonyms=TAJ-alphaS, dTROY;
CC IsoId=Q9JLL3-3; Sequence=VSP_006515, VSP_006516;
CC Name=4;
CC IsoId=Q9JLL3-4; Sequence=VSP_006517, VSP_006518;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult brain, and in embryos
CC from day 11-17, but not earlier. Detected in embryonic brain and
CC epithelium, and at lower levels in adult heart, lung and liver. In
CC neonatal mice, mainly in hair follicles and neuron-like cells in the
CC cerebellum, but not in the skin epidermis. Isoform 3 was found in
CC embryonic day 17.5 skin but not in brain and liver.
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DR EMBL; AF173166; AAF19795.1; -; mRNA.
DR EMBL; AF167552; AAF71825.1; -; mRNA.
DR EMBL; AF167554; AAF71827.1; -; mRNA.
DR EMBL; AF167553; AAF71826.1; -; mRNA.
DR EMBL; AB040432; BAB03267.1; -; mRNA.
DR EMBL; AB040433; BAB03268.1; -; mRNA.
DR EMBL; AF247000; AAK28397.1; -; mRNA.
DR EMBL; AK028146; BAC25774.1; -; mRNA.
DR EMBL; BC030062; AAH30062.1; -; mRNA.
DR CCDS; CCDS36941.1; -. [Q9JLL3-1]
DR RefSeq; NP_001157627.1; NM_001164155.1. [Q9JLL3-1]
DR RefSeq; NP_038897.4; NM_013869.5. [Q9JLL3-1]
DR AlphaFoldDB; Q9JLL3; -.
DR BioGRID; 205900; 1.
DR CORUM; Q9JLL3; -.
DR IntAct; Q9JLL3; 2.
DR MINT; Q9JLL3; -.
DR STRING; 10090.ENSMUSP00000106865; -.
DR GlyGen; Q9JLL3; 1 site.
DR PhosphoSitePlus; Q9JLL3; -.
DR PaxDb; Q9JLL3; -.
DR PRIDE; Q9JLL3; -.
DR ProteomicsDB; 260638; -. [Q9JLL3-1]
DR ProteomicsDB; 260639; -. [Q9JLL3-2]
DR ProteomicsDB; 260640; -. [Q9JLL3-3]
DR ProteomicsDB; 260641; -. [Q9JLL3-4]
DR ABCD; Q9JLL3; 1 sequenced antibody.
DR Antibodypedia; 2432; 379 antibodies from 33 providers.
DR DNASU; 29820; -.
DR Ensembl; ENSMUST00000111234; ENSMUSP00000106865; ENSMUSG00000060548. [Q9JLL3-1]
DR Ensembl; ENSMUST00000111236; ENSMUSP00000106867; ENSMUSG00000060548. [Q9JLL3-1]
DR Ensembl; ENSMUST00000224371; ENSMUSP00000153577; ENSMUSG00000060548. [Q9JLL3-3]
DR Ensembl; ENSMUST00000225730; ENSMUSP00000152920; ENSMUSG00000060548. [Q9JLL3-3]
DR GeneID; 29820; -.
DR KEGG; mmu:29820; -.
DR UCSC; uc007ufi.2; mouse. [Q9JLL3-1]
DR UCSC; uc007ufl.2; mouse. [Q9JLL3-3]
DR UCSC; uc007ufn.2; mouse. [Q9JLL3-2]
DR CTD; 55504; -.
DR MGI; MGI:1352474; Tnfrsf19.
DR VEuPathDB; HostDB:ENSMUSG00000060548; -.
DR eggNOG; ENOG502QQHI; Eukaryota.
DR GeneTree; ENSGT00940000153259; -.
DR HOGENOM; CLU_050058_0_0_1; -.
DR InParanoid; Q9JLL3; -.
DR OMA; SHSCAFH; -.
DR PhylomeDB; Q9JLL3; -.
DR TreeFam; TF331385; -.
DR BioGRID-ORCS; 29820; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tnfrsf19; mouse.
DR PRO; PR:Q9JLL3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JLL3; protein.
DR Bgee; ENSMUSG00000060548; Expressed in presomitic mesoderm and 278 other tissues.
DR Genevisible; Q9JLL3; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0001942; P:hair follicle development; IGI:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
DR CDD; cd13418; TNFRSF19; 1.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR022342; TNFR_19.
DR InterPro; IPR034047; TNFRSF19_N.
DR PANTHER; PTHR12120:SF1; PTHR12120:SF1; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR PRINTS; PR01969; TNFACTORR19.
DR SMART; SM00208; TNFR; 2.
DR PROSITE; PS00652; TNFR_NGFR_1; 2.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..416
FT /note="Tumor necrosis factor receptor superfamily member
FT 19"
FT /id="PRO_0000034598"
FT TOPO_DOM 30..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 33..72
FT /note="TNFR-Cys 1"
FT REPEAT 74..114
FT /note="TNFR-Cys 2"
FT REPEAT 116..149
FT /note="TNFR-Cys 3; truncated"
FT REGION 321..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 49..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 52..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 75..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 92..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 95..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 117..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 138..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 150
FT /note="T -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10809768"
FT /id="VSP_006513"
FT VAR_SEQ 151..416
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10809768"
FT /id="VSP_006514"
FT VAR_SEQ 204..214
FT /note="WSLRSQDIQYN -> CKLPSLCLTVK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10764796,
FT ECO:0000303|PubMed:10809768, ECO:0000303|PubMed:15489334"
FT /id="VSP_006515"
FT VAR_SEQ 215..416
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10764796,
FT ECO:0000303|PubMed:10809768, ECO:0000303|PubMed:15489334"
FT /id="VSP_006516"
FT VAR_SEQ 340..348
FT /note="NESAASLDS -> MLCFRFRDL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585776"
FT /id="VSP_006517"
FT VAR_SEQ 349..416
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10585776"
FT /id="VSP_006518"
FT CONFLICT 31
FT /note="T -> A (in Ref. 1; AAF19795)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> P (in Ref. 1; AAF19795)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> N (in Ref. 1; AAF19795 and 2; AAF71825)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> T (in Ref. 2; AAF71825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 45265 MW; 9BDC7C7A2D6A9C47 CRC64;
MALKVLPLHR TVLFAAILFL LHLACKVSCE TGDCRQQEFK DRSGNCVLCK QCGPGMELSK
ECGFGYGEDA QCVPCRPHRF KEDWGFQKCK PCADCALVNR FQRANCSHTS DAVCGDCLPG
FYRKTKLVGF QDMECVPCGD PPPPYEPHCT SKVNLVKISS TVSSPRDTAL AAVICSALAT
VLLALLILCV IYCKRQFMEK KPSWSLRSQD IQYNGSELSC FDQPRLRHCA HRACCQYHRD
SAPMYGPVHL IPSLCCEEAR SSARAVLGCG LRSPTTLQER NPASVGDTMP AFFGSVSRSI
CAEFSDAWPL MQNPLGGDSS LCDSYPELTG EDTNSLNPEN ESAASLDSSG GQDLAGTAAL
ESSGNVSEST DSPRHGDTGT VWEQTLAQDA QRTPSQGGWE DRENLNLAMP TAFQDA
