TR13B_HUMAN
ID TR13B_HUMAN Reviewed; 293 AA.
AC O14836; B2R8B0; B7Z6V8; Q32LX4; Q7Z6F5;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 13B;
DE AltName: Full=Transmembrane activator and CAML interactor;
DE AltName: CD_antigen=CD267;
GN Name=TNFRSF13B; Synonyms=TACI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RX PubMed=9311921; DOI=10.1126/science.278.5335.138;
RA von Buelow G.-U., Bram R.J.;
RT "NF-AT activation induced by a CAML-interacting member of the tumor
RT necrosis factor receptor superfamily.";
RL Science 278:138-141(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Zhou G., Ke R., Li H., Zheng G., Shen C., Lin L., Yang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP LEU-251.
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-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).
RN [6]
RP FUNCTION.
RX PubMed=10956646; DOI=10.1074/jbc.m005224200;
RA Wu Y., Bressette D., Carrell J.A., Kaufman T., Feng P., Taylor K., Gan Y.,
RA Cho Y.H., Garcia A.D., Gollatz E., Dimke D., LaFleur D., Migone T.S.,
RA Nardelli B., Wei P., Ruben S.M., Ullrich S.J., Olsen H.S., Kanakaraj P.,
RA Moore P.A., Baker K.P.;
RT "Tumor necrosis factor (TNF) receptor superfamily member TACI is a high
RT affinity receptor for TNF family members APRIL and BLyS.";
RL J. Biol. Chem. 275:35478-35485(2000).
RN [7]
RP FUNCTION.
RX PubMed=10973284; DOI=10.1038/79802;
RA Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M.,
RA McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J.,
RA Sarosi I., Hsu H., Senaldi G., Theill L.E.;
RT "APRIL and TALL-I and receptors BCMA and TACI: system for regulating
RT humoral immunity.";
RL Nat. Immunol. 1:252-256(2000).
RN [8]
RP INTERACTION WITH TRAF2 AND TRAF5.
RX PubMed=10880535; DOI=10.1084/jem.192.1.137;
RA Xia X.-Z., Treanor J., Senaldi G., Khare S.D., Boone T., Kelley M.,
RA Theill L.E., Colombero A., Solovyev I., Lee F., McCabe S., Elliott R.,
RA Miner K., Hawkins N., Guo J., Stolina M., Yu G., Wang J., Delaney J.,
RA Meng S.-Y., Boyle W.J., Hsu H.;
RT "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor
RT family member involved in B cell regulation.";
RL J. Exp. Med. 192:137-143(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 68-109 IN COMPLEX WITH MOUSE
RP TNFSF13, AND STRUCTURE BY NMR OF 68-109.
RX PubMed=15542592; DOI=10.1074/jbc.m411714200;
RA Hymowitz S.G., Patel D.R., Wallweber H.J., Runyon S., Yan M., Yin J.,
RA Shriver S.K., Gordon N.C., Pan B., Skelton N.J., Kelley R.F.,
RA Starovasnik M.A.;
RT "Structures of APRIL-receptor complexes: like BCMA, TACI employs only a
RT single cysteine-rich domain for high affinity ligand binding.";
RL J. Biol. Chem. 280:7218-7227(2005).
RN [10]
RP VARIANT IGAD2 ARG-104, AND VARIANTS CVID2 ARG-104; GLY-181 AND HIS-202.
RX PubMed=16007086; DOI=10.1038/ng1601;
RA Castigli E., Wilson S.A., Garibyan L., Rachid R., Bonilla F., Schneider L.,
RA Geha R.S.;
RT "TACI is mutant in common variable immunodeficiency and IgA deficiency.";
RL Nat. Genet. 37:829-834(2005).
RN [11]
RP VARIANT ASN-56.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that
CC binds both ligands with similar high affinity. Mediates calcineurin-
CC dependent activation of NF-AT, as well as activation of NF-kappa-B and
CC AP-1. Involved in the stimulation of B- and T-cell function and the
CC regulation of humoral immunity. {ECO:0000269|PubMed:10956646,
CC ECO:0000269|PubMed:10973284}.
CC -!- SUBUNIT: Binds TRAF2, TRAF5 and TRAF6. Binds the NH2-terminal domain of
CC CAMLG with its C-terminus. {ECO:0000269|PubMed:15542592}.
CC -!- INTERACTION:
CC O14836; Q99836: MYD88; NbExp=12; IntAct=EBI-519160, EBI-447677;
CC O14836; O43765: SGTA; NbExp=3; IntAct=EBI-519160, EBI-347996;
CC O14836; Q9Y275: TNFSF13B; NbExp=7; IntAct=EBI-519160, EBI-519169;
CC O14836-2; O43765: SGTA; NbExp=8; IntAct=EBI-12023110, EBI-347996;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14836-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14836-2; Sequence=VSP_013798;
CC Name=3;
CC IsoId=O14836-3; Sequence=VSP_054184, VSP_054185;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen, thymus, small intestine
CC and peripheral blood leukocytes. Expressed in resting B-cells and
CC activated T-cells, but not in resting T-cells.
CC -!- DISEASE: Immunodeficiency, common variable, 2 (CVID2) [MIM:240500]: A
CC primary immunodeficiency characterized by antibody deficiency,
CC hypogammaglobulinemia, recurrent bacterial infections and an inability
CC to mount an antibody response to antigen. The defect results from a
CC failure of B-cell differentiation and impaired secretion of
CC immunoglobulins; the numbers of circulating B-cells is usually in the
CC normal range, but can be low. {ECO:0000269|PubMed:16007086}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Immunoglobulin A deficiency 2 (IGAD2) [MIM:609529]: Selective
CC deficiency of immunoglobulin A (IGAD) is the most common form of
CC primary immunodeficiency, with an incidence of approximately 1 in 600
CC individuals in the western world. Individuals with symptomatic IGAD
CC often have deficiency of IgG subclasses or decreased antibody response
CC to carbohydrate antigens such as pneumococcal polysaccharide vaccine.
CC Individuals with IGAD also suffer from recurrent sinopulmonary and
CC gastrointestinal infections and have an increased incidence of
CC autoimmune disorders and of lymphoid and non-lymphoid malignancies. In
CC vitro studies have suggested that some individuals with IGAD have
CC impaired isotype class switching to IgA and others may have a post-
CC switch defect. IGAD and CVID have been known to coexist in families.
CC Some individuals initially present with IGAD1 and then develop CVID.
CC These observations suggest that some cases of IGAD and CVID may have a
CC common etiology. {ECO:0000269|PubMed:16007086}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=TNFRSF13Bbase; Note=TNFRSF13B mutation db;
CC URL="http://structure.bmc.lu.se/idbase/TNFRSF13Bbase/";
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DR EMBL; AF023614; AAC51790.1; -; mRNA.
DR EMBL; AY302137; AAP57629.1; -; mRNA.
DR EMBL; AK301032; BAH13394.1; -; mRNA.
DR EMBL; AK313302; BAG36107.1; -; mRNA.
DR EMBL; CH471196; EAW55729.1; -; Genomic_DNA.
DR EMBL; BC109392; AAI09393.1; -; mRNA.
DR CCDS; CCDS11181.1; -. [O14836-1]
DR RefSeq; NP_036584.1; NM_012452.2. [O14836-1]
DR PDB; 1XU1; X-ray; 1.90 A; R/S/T=68-109.
DR PDB; 1XUT; NMR; -; A=68-109.
DR PDBsum; 1XU1; -.
DR PDBsum; 1XUT; -.
DR AlphaFoldDB; O14836; -.
DR SMR; O14836; -.
DR BioGRID; 117046; 48.
DR DIP; DIP-6224N; -.
DR IntAct; O14836; 35.
DR STRING; 9606.ENSP00000261652; -.
DR GlyGen; O14836; 1 site.
DR iPTMnet; O14836; -.
DR PhosphoSitePlus; O14836; -.
DR SwissPalm; O14836; -.
DR BioMuta; TNFRSF13B; -.
DR MassIVE; O14836; -.
DR MaxQB; O14836; -.
DR PaxDb; O14836; -.
DR PeptideAtlas; O14836; -.
DR PRIDE; O14836; -.
DR ProteomicsDB; 48270; -. [O14836-1]
DR ProteomicsDB; 48271; -. [O14836-2]
DR Antibodypedia; 35076; 657 antibodies from 44 providers.
DR DNASU; 23495; -.
DR Ensembl; ENST00000261652.7; ENSP00000261652.2; ENSG00000240505.9. [O14836-1]
DR Ensembl; ENST00000583789.1; ENSP00000462952.1; ENSG00000240505.9. [O14836-2]
DR GeneID; 23495; -.
DR KEGG; hsa:23495; -.
DR MANE-Select; ENST00000261652.7; ENSP00000261652.2; NM_012452.3; NP_036584.1.
DR UCSC; uc002gqt.2; human. [O14836-1]
DR CTD; 23495; -.
DR DisGeNET; 23495; -.
DR GeneCards; TNFRSF13B; -.
DR HGNC; HGNC:18153; TNFRSF13B.
DR HPA; ENSG00000240505; Group enriched (intestine, lymphoid tissue, skeletal muscle).
DR MalaCards; TNFRSF13B; -.
DR MIM; 240500; phenotype.
DR MIM; 604907; gene.
DR MIM; 609529; phenotype.
DR neXtProt; NX_O14836; -.
DR OpenTargets; ENSG00000240505; -.
DR Orphanet; 1572; Common variable immunodeficiency.
DR Orphanet; 69127; NON RARE IN EUROPE: Immunoglobulin A deficiency.
DR PharmGKB; PA38509; -.
DR VEuPathDB; HostDB:ENSG00000240505; -.
DR eggNOG; ENOG502SANG; Eukaryota.
DR GeneTree; ENSGT00390000013910; -.
DR HOGENOM; CLU_086237_0_0_1; -.
DR InParanoid; O14836; -.
DR OMA; CHCREDP; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; O14836; -.
DR TreeFam; TF337993; -.
DR PathwayCommons; O14836; -.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR SignaLink; O14836; -.
DR SIGNOR; O14836; -.
DR BioGRID-ORCS; 23495; 10 hits in 1063 CRISPR screens.
DR ChiTaRS; TNFRSF13B; human.
DR EvolutionaryTrace; O14836; -.
DR GeneWiki; TNFRSF13B; -.
DR GenomeRNAi; 23495; -.
DR Pharos; O14836; Tbio.
DR PRO; PR:O14836; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O14836; protein.
DR Bgee; ENSG00000240505; Expressed in spleen and 124 other tissues.
DR ExpressionAtlas; O14836; baseline and differential.
DR Genevisible; O14836; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0001782; P:B cell homeostasis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IBA:GO_Central.
DR CDD; cd13415; TNFRSF13B; 1.
DR InterPro; IPR015384; TACI_Cys-rich-dom.
DR InterPro; IPR022317; TNFR_13B.
DR PANTHER; PTHR15511; PTHR15511; 1.
DR Pfam; PF09305; TACI-CRD2; 2.
DR PRINTS; PR01963; TNFACTORR13B.
DR PROSITE; PS00652; TNFR_NGFR_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Disease variant;
KW Disulfide bond; Glycoprotein; Immunity; Membrane; Receptor;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..293
FT /note="Tumor necrosis factor receptor superfamily member
FT 13B"
FT /id="PRO_0000058931"
FT TOPO_DOM 1..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 33..67
FT /note="TNFR-Cys 1"
FT REPEAT 70..104
FT /note="TNFR-Cys 2"
FT REGION 115..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..47
FT /evidence="ECO:0000250"
FT DISULFID 50..62
FT /evidence="ECO:0000250"
FT DISULFID 54..66
FT /evidence="ECO:0000250"
FT DISULFID 71..86
FT DISULFID 89..100
FT DISULFID 93..104
FT VAR_SEQ 21..67
FT /note="FPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCR -> W
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_013798"
FT VAR_SEQ 150..176
FT /note="LPGLKLSADQVALVYSTLGLCLCAVLC -> PRGCPAPGTRKSFWDKENFQG
FT EGFHLG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054184"
FT VAR_SEQ 177..293
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054185"
FT VARIANT 56
FT /note="H -> N (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064758"
FT VARIANT 104
FT /note="C -> R (in CVID2 and IGAD2; dbSNP:rs34557412)"
FT /evidence="ECO:0000269|PubMed:16007086"
FT /id="VAR_024027"
FT VARIANT 181
FT /note="A -> G (in CVID2)"
FT /evidence="ECO:0000269|PubMed:16007086"
FT /id="VAR_024028"
FT VARIANT 202
FT /note="R -> H (in CVID2; dbSNP:rs104894649)"
FT /evidence="ECO:0000269|PubMed:16007086"
FT /id="VAR_024029"
FT VARIANT 251
FT /note="P -> L (in dbSNP:rs34562254)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_052353"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1XU1"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1XU1"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1XU1"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1XU1"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1XU1"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1XU1"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1XU1"
SQ SEQUENCE 293 AA; 31816 MW; 411799F3DE17A5EB CRC64;
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR
TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR
QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV ALVYSTLGLC LCAVLCCFLV
AVACFLKKRG DPCSCQPRSR PRQSPAKSSQ DHAMEAGSPV STSPEPVETC SFCFPECRAP
TQESAVTPGT PDPTCAGRWG CHTRTTVLQP CPHIPDSGLG IVCVPAQEGG PGA
