TN13B_MOUSE
ID TN13B_MOUSE Reviewed; 309 AA.
AC Q9WU72; Q7TQ58;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 13B;
DE AltName: Full=B-cell-activating factor;
DE AltName: Full=BAFF;
DE AltName: CD_antigen=CD257;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 13b, membrane form;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 13b, soluble form;
GN Name=Tnfsf13b; Synonyms=Baff;
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 1).
RX PubMed=10359578; DOI=10.1084/jem.189.11.1747;
RA Schneider P., MacKay F., Steiner V., Hofmann K., Bodmer J.-L., Holler N.,
RA Ambrose C., Lawton P., Bixler S., Acha-Orbea H., Valmori D., Romero P.,
RA Werner-Favre C., Zubler R.H., Browning J.L., Tschopp J.;
RT "BAFF, a novel ligand of the tumor necrosis factor family, stimulates B
RT cell growth.";
RL J. Exp. Med. 189:1747-1756(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-79.
RC STRAIN=NZB;
RX PubMed=11862414; DOI=10.1007/s00251-001-0396-6;
RA Jiang Y., Ohtsuji M., Abe M., Li N., Xiu Y., Wen X.S., Shirai T.,
RA Hirose S.;
RT "Polymorphism and chromosomal mapping of the mouse gene for B-cell
RT activating factor belonging to the tumor necrosis factor family (Baff) and
RT association with the autoimmune phenotype.";
RL Immunogenetics 53:810-813(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION,
RP POST-TRANSLATIONAL MODIFICATION, AND SUBUNIT.
RC STRAIN=BALB/cJ;
RX PubMed=12867412; DOI=10.1074/jbc.m306852200;
RA Gavin A.L., Ait-Azzouzene D., Ware C.F., Nemazee D.;
RT "DeltaBAFF, an alternate splice isoform that regulates receptor binding and
RT biopresentation of the B cell survival cytokine, BAFF.";
RL J. Biol. Chem. 278:38220-38228(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA.
CC TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2
CC ligands -2 receptors pathway involved in the stimulation of B- and T-
CC cell function and the regulation of humoral immunity. A third B-cell
CC specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-
CC cells and the B-cell response. {ECO:0000269|PubMed:12867412}.
CC -!- FUNCTION: Isoform 2 seems to inhibit isoform 1 secretion and
CC bioactivity. {ECO:0000269|PubMed:12867412}.
CC -!- SUBUNIT: Homotrimer. Isoform 2 heteromultimerizes with isoform 1,
CC probably limiting the amount of functional isoform 1 on the cell
CC surface. {ECO:0000269|PubMed:12867412}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
CC 13b, soluble form]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WU72-1; Sequence=Displayed;
CC Name=2; Synonyms=DeltaBAFF;
CC IsoId=Q9WU72-2; Sequence=VSP_041184;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in many myeloid cell lines.
CC {ECO:0000269|PubMed:12867412}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- PTM: Isoform 2 is not efficiently shed from the membrane unlike isoform
CC 1.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF119383; AAD22475.1; -; mRNA.
DR EMBL; AF352245; AAL83939.1; -; mRNA.
DR EMBL; AY290823; AAP82036.1; -; mRNA.
DR EMBL; CH466566; EDL22044.1; -; Genomic_DNA.
DR EMBL; BC106840; AAI06841.1; -; mRNA.
DR CCDS; CCDS22094.1; -. [Q9WU72-1]
DR CCDS; CCDS85498.1; -. [Q9WU72-2]
DR RefSeq; NP_001334238.1; NM_001347309.1. [Q9WU72-2]
DR RefSeq; NP_296371.1; NM_033622.1. [Q9WU72-1]
DR AlphaFoldDB; Q9WU72; -.
DR SMR; Q9WU72; -.
DR BioGRID; 204896; 2.
DR STRING; 10090.ENSMUSP00000033892; -.
DR GlyGen; Q9WU72; 2 sites.
DR iPTMnet; Q9WU72; -.
DR PhosphoSitePlus; Q9WU72; -.
DR MaxQB; Q9WU72; -.
DR PaxDb; Q9WU72; -.
DR PRIDE; Q9WU72; -.
DR ProteomicsDB; 260715; -. [Q9WU72-1]
DR ProteomicsDB; 260716; -. [Q9WU72-2]
DR ABCD; Q9WU72; 24 sequenced antibodies.
DR Antibodypedia; 3364; 1511 antibodies from 47 providers.
DR DNASU; 24099; -.
DR Ensembl; ENSMUST00000033892; ENSMUSP00000033892; ENSMUSG00000031497. [Q9WU72-2]
DR Ensembl; ENSMUST00000207792; ENSMUSP00000146694; ENSMUSG00000031497. [Q9WU72-1]
DR GeneID; 24099; -.
DR KEGG; mmu:24099; -.
DR UCSC; uc009kup.1; mouse. [Q9WU72-1]
DR UCSC; uc009kuq.1; mouse. [Q9WU72-2]
DR CTD; 10673; -.
DR MGI; MGI:1344376; Tnfsf13b.
DR VEuPathDB; HostDB:ENSMUSG00000031497; -.
DR eggNOG; ENOG502RX35; Eukaryota.
DR GeneTree; ENSGT00940000157536; -.
DR HOGENOM; CLU_063693_0_0_1; -.
DR InParanoid; Q9WU72; -.
DR OMA; ARGECTS; -.
DR PhylomeDB; Q9WU72; -.
DR TreeFam; TF332331; -.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
DR Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR BioGRID-ORCS; 24099; 1 hit in 60 CRISPR screens.
DR ChiTaRS; Tnfsf13b; mouse.
DR PRO; PR:Q9WU72; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9WU72; protein.
DR Bgee; ENSMUSG00000031497; Expressed in granulocyte and 128 other tissues.
DR ExpressionAtlas; Q9WU72; baseline and differential.
DR Genevisible; Q9WU72; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0031296; P:B cell costimulation; IDA:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP: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: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; IGI: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 SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50049; TNF_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW Cytokine; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..309
FT /note="Tumor necrosis factor ligand superfamily member 13b,
FT membrane form"
FT /id="PRO_0000034530"
FT CHAIN 127..309
FT /note="Tumor necrosis factor ligand superfamily member 13b,
FT soluble form"
FT /id="PRO_0000034531"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..309
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 110..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 126..127
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256..269
FT /evidence="ECO:0000250"
FT VAR_SEQ 166..185
FT /note="IIQDCLQLIADSDTPTIRKG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12867412,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_041184"
FT VARIANT 79
FT /note="N -> S (in strain: NZB)"
FT /evidence="ECO:0000269|PubMed:11862414"
SQ SEQUENCE 309 AA; 34192 MW; F3DE6056E66034B4 CRC64;
MDESAKTLPP PCLCFCSEKG EDMKVGYDPI TPQKEEGAWF GICRDGRLLA ATLLLALLSS
SFTAMSLYQL AALQADLMNL RMELQSYRGS ATPAAAGAPE LTAGVKLLTP AAPRPHNSSR
GHRNRRAFQG PEETEQDVDL SAPPAPCLPG CRHSQHDDNG MNLRNIIQDC LQLIADSDTP
TIRKGTYTFV PWLLSFKRGN ALEEKENKIV VRQTGYFFIY SQVLYTDPIF AMGHVIQRKK
VHVFGDELSL VTLFRCIQNM PKTLPNNSCY SAGIARLEEG DEIQLAIPRE NAQISRNGDD
TFFGALKLL
