TR13C_MOUSE
ID TR13C_MOUSE Reviewed; 175 AA.
AC Q9D8D0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 13C;
DE AltName: Full=B-cell maturation defect;
DE AltName: Full=B-cell-activating factor receptor;
DE AltName: Full=BAFF receptor;
DE Short=BAFF-R;
DE AltName: Full=BLyS receptor 3;
DE AltName: CD_antigen=CD268;
GN Name=Tnfrsf13c; Synonyms=Baffr, Bcmd, Br3;
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] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ; TISSUE=B-cell lymphoma;
RX PubMed=11509692; DOI=10.1126/science.1061965;
RA Thompson J.S., Bixler S.A., Qian F., Vora K., Scott M.L., Cachero T.G.,
RA Hession C., Schneider P., Sizing I.D., Mullen C., Strauch K., Zafari M.,
RA Benjamin C.D., Tschopp J., Browning J.L., Ambrose C.;
RT "BAFF-R, a newly identified TNF receptor that specifically interacts with
RT BAFF.";
RL Science 293:2108-2111(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
RC STRAIN=A/J;
RX PubMed=11591325; DOI=10.1016/s0960-9822(01)00481-x;
RA Yan M., Brady J.R., Chan B., Lee W.P., Hsu B., Harless S.M., Cancro M.P.,
RA Grewal I.S., Dixit V.M.;
RT "Identification of a novel receptor for B lymphocyte stimulator that is
RT mutated in a mouse strain with severe B cell deficiency.";
RL Curr. Biol. 11:1547-1552(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [4]
RP FUNCTION.
RX PubMed=11747827; DOI=10.1016/s0960-9822(01)00598-x;
RA Harless S.M., Lentz V.M., Sah A.P., Hsu B.L., Clise-Dwyer K., Hilbert D.M.,
RA Hayes C.E., Cancro M.P.;
RT "Competition for BLyS-mediated signaling through Bcmd/BR3 regulates
RT peripheral B lymphocyte numbers.";
RL Curr. Biol. 11:1986-1989(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS.
CC Promotes the survival of mature B-cells and the B-cell response.
CC {ECO:0000269|PubMed:11747827}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8D0-2; Sequence=VSP_006506;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and testis; detected at
CC lower levels in lung and thymus.
CC -!- DISEASE: Note=Defects in Tnfrsf13c are a cause of severe B-cell
CC deficiency. B-cell deficient strain A/WySnJ has a 4.7 kb insertion in
CC the BAFFR gene leading to an altered C-terminus. The mutant RNA is not
CC detectable. B-cell lymphopoiesis is normal, but the life span of
CC peripheral B-cells is much reduced. {ECO:0000269|PubMed:11591325}.
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DR EMBL; AF373847; AAK91827.1; -; mRNA.
DR EMBL; AK008142; BAB25490.1; -; mRNA.
DR CCDS; CCDS27684.1; -. [Q9D8D0-1]
DR RefSeq; NP_082351.1; NM_028075.2. [Q9D8D0-1]
DR AlphaFoldDB; Q9D8D0; -.
DR SMR; Q9D8D0; -.
DR BioGRID; 215117; 3.
DR GlyGen; Q9D8D0; 1 site.
DR iPTMnet; Q9D8D0; -.
DR PhosphoSitePlus; Q9D8D0; -.
DR PaxDb; Q9D8D0; -.
DR PRIDE; Q9D8D0; -.
DR ProteomicsDB; 259179; -. [Q9D8D0-1]
DR ProteomicsDB; 259180; -. [Q9D8D0-2]
DR Antibodypedia; 307; 675 antibodies from 41 providers.
DR DNASU; 72049; -.
DR Ensembl; ENSMUST00000089161; ENSMUSP00000086564; ENSMUSG00000068105. [Q9D8D0-1]
DR GeneID; 72049; -.
DR KEGG; mmu:72049; -.
DR UCSC; uc007wyj.1; mouse. [Q9D8D0-1]
DR CTD; 115650; -.
DR MGI; MGI:1919299; Tnfrsf13c.
DR VEuPathDB; HostDB:ENSMUSG00000068105; -.
DR GeneTree; ENSGT00940000154485; -.
DR InParanoid; Q9D8D0; -.
DR OMA; AQCFDPL; -.
DR PhylomeDB; Q9D8D0; -.
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; 72049; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Tnfrsf13c; mouse.
DR PRO; PR:Q9D8D0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D8D0; protein.
DR Bgee; ENSMUSG00000068105; Expressed in mesenteric lymph node and 83 other tissues.
DR ExpressionAtlas; Q9D8D0; baseline and differential.
DR Genevisible; Q9D8D0; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0031296; P:B cell costimulation; IDA:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IDA:MGI.
DR GO; GO:0002467; P:germinal center formation; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
DR GO; GO:0002636; P:positive regulation of germinal center formation; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR GO; GO:0031295; P:T cell costimulation; IDA:MGI.
DR GO; GO:0042098; P:T cell proliferation; IDA:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:InterPro.
DR InterPro; IPR022338; TNFR_13C.
DR InterPro; IPR043521; TNFR_13C/17.
DR InterPro; IPR015336; TNFR_13C_TALL-1-bd.
DR PANTHER; PTHR20437; PTHR20437; 1.
DR PANTHER; PTHR20437:SF2; PTHR20437:SF2; 1.
DR Pfam; PF09256; BaffR-Tall_bind; 1.
DR PRINTS; PR01964; TNFACTORR13C.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunity; Membrane; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..175
FT /note="Tumor necrosis factor receptor superfamily member
FT 13C"
FT /id="PRO_0000058934"
FT TOPO_DOM 1..71
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 21..38
FT /note="TNFR-Cys; truncated"
FT REGION 29..34
FT /note="Essential for TNFSF13B/TALL1/BAFF/BLyS binding"
FT /evidence="ECO:0000250"
FT REGION 124..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..35
FT /evidence="ECO:0000250"
FT DISULFID 27..38
FT /evidence="ECO:0000250"
FT VAR_SEQ 133..143
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11509692"
FT /id="VSP_006506"
SQ SEQUENCE 175 AA; 18798 MW; 28BC7C1A02FB87EF CRC64;
MGARRLRVRS QRSRDSSVPT QCNQTECFDP LVRNCVSCEL FHTPDTGHTS SLEPGTALQP
QEGSALRPDV ALLVGAPALL GLILALTLVG LVSLVSWRWR QQLRTASPDT SEGVQQESLE
NVFVPSSETP HASAPTWPPL KEDADSALPR HSVPVPATEL GSTELVTTKT AGPEQ
