TN13B_HUMAN
ID TN13B_HUMAN Reviewed; 285 AA.
AC Q9Y275; E0ADT7; Q6FHD6; Q7Z5J2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 13B;
DE AltName: Full=B lymphocyte stimulator;
DE Short=BLyS;
DE AltName: Full=B-cell-activating factor;
DE AltName: Full=BAFF;
DE AltName: Full=Dendritic cell-derived TNF-like molecule;
DE AltName: Full=TNF- and APOL-related leukocyte expressed ligand 1;
DE Short=TALL-1;
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, BLYS, TALL1, TNFSF20, ZTNF4;
GN ORFNames=UNQ401/PRO738;
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).
RX PubMed=10331498; DOI=10.1002/jlb.65.5.680;
RA Shu H.-B., Hu W.-H., Johnson H.;
RT "TALL-1 is a novel member of the TNF family that is down-regulated by
RT mitogens.";
RL J. Leukoc. Biol. 65:680-683(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 134-148.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Monocyte, and Neutrophil;
RX PubMed=10398604; DOI=10.1126/science.285.5425.260;
RA Moore P.A., Belvedere O., Orr A., Pieri K., LaFleur D.W., Feng P.,
RA Soppet D., Charters M., Gentz R., Parmelee D., Li Y., Galperina O.,
RA Giri J., Roschke V., Nardelli B., Carrell J., Sosnovtseva S.,
RA Greenfield W., Ruben S.M., Olsen H.S., Fikes J., Hilbert D.M.;
RT "BLyS: member of the tumor necrosis factor family and B lymphocyte
RT stimulator.";
RL Science 285:260-263(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND SUBUNIT.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORM 3), SUBUNIT, AND
RP ALTERNATIVE SPLICING.
RX PubMed=22749832; DOI=10.1016/j.jaut.2012.05.009;
RA Lahiri A., Pochard P., Le Pottier L., Tobon G.J., Bendaoud B., Youinou P.,
RA Pers J.O.;
RT "The complexity of the BAFF TNF-family members: implications for
RT autoimmunity.";
RL J. Autoimmun. 39:189-198(2012).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Farrah T., Gross J., Piddington C., O'Hara P.;
RT "Homo sapiens homolog of tumor necrosis factor.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Zhang W., Wan T., Yu Y., Cao X.;
RT "A novel dendritic cell-derived TNF-like molecule.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Gao H., He F., Li R.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [13]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135, AND VARIANT THR-105.
RA Kawasaki A., Tsuchiya N., Fukazawa T., Hashimoto H., Tokunaga K.;
RT "New polymorphisms of human BLyS gene.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [16]
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 [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 142-285.
RX PubMed=11853672; DOI=10.1016/s0092-8674(02)00631-1;
RA Liu Y., Xu L., Opalka N., Kappler J., Shu H.-B., Zhang G.;
RT "Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family
RT ligands.";
RL Cell 108:383-394(2002).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 136-285.
RX PubMed=11827482; DOI=10.1006/jmbi.2001.5296;
RA Karpusas M., Cachero T.G., Qian F., Boriack-Sjodin A., Mullen C.,
RA Strauch K., Hsu Y.-M., Kalled S.L.;
RT "Crystal structure of extracellular human BAFF, a TNF family member that
RT stimulates B lymphocytes.";
RL J. Mol. Biol. 315:1145-1154(2002).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-285.
RX PubMed=11862220; DOI=10.1038/nsb769;
RA Oren D.A., Li Y., Volovik Y., Morris T.S., Dharia C., Das K., Galperina O.,
RA Gentz R., Arnold E.;
RT "Structural basis of BLyS receptor recognition.";
RL Nat. Struct. Biol. 9:288-292(2002).
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:10973284}.
CC -!- FUNCTION: Isoform 2 seems to inhibit isoform 1 secretion and
CC bioactivity. {ECO:0000250}.
CC -!- FUNCTION: [Isoform 3]: Acts as a transcription factor for its own
CC parent gene, in association with NF-kappa-B p50 subunit, at least in
CC autoimmune and proliferative B-cell diseases. The presence of
CC Delta4BAFF is essential for soluble BAFF release by IFNG/IFN-gamma-
CC stimulated monocytes and for B-cell survival. It can directly or
CC indirectly regulate the differential expression of a large number of
CC genes involved in the innate immune response and the regulation of
CC apoptosis. {ECO:0000269|PubMed:10973284}.
CC -!- SUBUNIT: Homotrimer. Isoform 2 heteromultimerizes with isoform 1,
CC probably limiting the amount of functional isoform 1 on the cell
CC surface. Isoform 3 is unlikely form trimers or bind to BAFF receptors.
CC {ECO:0000269|PubMed:12867412, ECO:0000269|PubMed:22749832}.
CC -!- INTERACTION:
CC Q9Y275; P55060: CSE1L; NbExp=2; IntAct=EBI-519169, EBI-286709;
CC Q9Y275; Q14974: KPNB1; NbExp=2; IntAct=EBI-519169, EBI-286758;
CC Q9Y275; O14836: TNFRSF13B; NbExp=7; IntAct=EBI-519169, EBI-519160;
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=3;
CC Name=1;
CC IsoId=Q9Y275-1; Sequence=Displayed;
CC Name=2; Synonyms=DeltaBAFF;
CC IsoId=Q9Y275-2; Sequence=VSP_041183;
CC Name=3; Synonyms=Delta4BAFF;
CC IsoId=Q9Y275-3; Sequence=VSP_047591, VSP_047592;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in peripheral blood Leukocytes
CC and is specifically expressed in monocytes and macrophages. Also found
CC in the spleen, lymph node, bone marrow, T-cells and dendritic cells. A
CC lower expression seen in placenta, heart, lung, fetal liver, thymus,
CC and pancreas. Isoform 2 is expressed in many myeloid cell lines.
CC {ECO:0000269|PubMed:12867412}.
CC -!- INDUCTION: Up-regulated by exposure to IFNG/IFN-gamma. Down-regulated
CC by phorbol myristate acetate/ionomycin treatment.
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. {ECO:0000250}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Proteic grace - Issue 77 of
CC December 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/077";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF136293; AAD29421.1; -; mRNA.
DR EMBL; AF116456; AAD25356.1; -; mRNA.
DR EMBL; AF132600; AAD21092.1; -; mRNA.
DR EMBL; AY302751; AAP83164.1; -; mRNA.
DR EMBL; HM636064; ADK91575.1; -; mRNA.
DR EMBL; AF186114; AAF01432.1; -; mRNA.
DR EMBL; AF134715; AAF60219.1; -; mRNA.
DR EMBL; AY129225; AAN08421.1; -; mRNA.
DR EMBL; EF064706; ABK41889.1; -; Genomic_DNA.
DR EMBL; AY358881; AAQ89240.1; -; mRNA.
DR EMBL; CR541818; CAG46617.1; -; mRNA.
DR EMBL; AL157762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09099.1; -; Genomic_DNA.
DR EMBL; BC020674; AAH20674.1; -; mRNA.
DR EMBL; AB073225; BAB90856.1; -; Genomic_DNA.
DR CCDS; CCDS45067.1; -. [Q9Y275-2]
DR CCDS; CCDS9509.1; -. [Q9Y275-1]
DR RefSeq; NP_001139117.1; NM_001145645.2. [Q9Y275-2]
DR RefSeq; NP_006564.1; NM_006573.4. [Q9Y275-1]
DR PDB; 1JH5; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=142-285.
DR PDB; 1KD7; X-ray; 2.80 A; A/B/C/K/L/M=133-285.
DR PDB; 1KXG; X-ray; 2.00 A; A/B/C/D/E/F=134-285.
DR PDB; 1OQD; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=142-285.
DR PDB; 1OQE; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=142-285.
DR PDB; 1OSG; X-ray; 3.00 A; A/B/C/D/E/F=82-285.
DR PDB; 3V56; X-ray; 3.00 A; A/B/C/D/E/F=82-285.
DR PDB; 4V46; X-ray; 3.30 A; A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/AW/AX/AY/AZ/Aa/Ab/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Aq/Ar/As/At/Au/Av/Aw/Ax=138-285.
DR PDB; 4ZCH; X-ray; 2.43 A; A/B=140-285.
DR PDB; 5Y9J; X-ray; 2.05 A; A=134-285.
DR PDB; 6FXN; X-ray; 2.90 A; A/B/C/J/K/L=134-285.
DR PDBsum; 1JH5; -.
DR PDBsum; 1KD7; -.
DR PDBsum; 1KXG; -.
DR PDBsum; 1OQD; -.
DR PDBsum; 1OQE; -.
DR PDBsum; 1OSG; -.
DR PDBsum; 3V56; -.
DR PDBsum; 4V46; -.
DR PDBsum; 4ZCH; -.
DR PDBsum; 5Y9J; -.
DR PDBsum; 6FXN; -.
DR AlphaFoldDB; Q9Y275; -.
DR SMR; Q9Y275; -.
DR BioGRID; 115915; 124.
DR CORUM; Q9Y275; -.
DR DIP; DIP-6225N; -.
DR IntAct; Q9Y275; 103.
DR STRING; 9606.ENSP00000365048; -.
DR ChEMBL; CHEMBL2364158; -.
DR DrugBank; DB03316; 1,4-Dioxane.
DR DrugBank; DB08879; Belimumab.
DR DrugCentral; Q9Y275; -.
DR GlyGen; Q9Y275; 2 sites.
DR iPTMnet; Q9Y275; -.
DR PhosphoSitePlus; Q9Y275; -.
DR BioMuta; TNFSF13B; -.
DR DMDM; 13124573; -.
DR EPD; Q9Y275; -.
DR jPOST; Q9Y275; -.
DR MassIVE; Q9Y275; -.
DR PaxDb; Q9Y275; -.
DR PeptideAtlas; Q9Y275; -.
DR PRIDE; Q9Y275; -.
DR ProteomicsDB; 15188; -.
DR ProteomicsDB; 85677; -. [Q9Y275-1]
DR ProteomicsDB; 85678; -. [Q9Y275-2]
DR ABCD; Q9Y275; 27 sequenced antibodies.
DR Antibodypedia; 3364; 1511 antibodies from 47 providers.
DR DNASU; 10673; -.
DR Ensembl; ENST00000375887.9; ENSP00000365048.3; ENSG00000102524.12. [Q9Y275-1]
DR Ensembl; ENST00000430559.5; ENSP00000389540.1; ENSG00000102524.12. [Q9Y275-2]
DR Ensembl; ENST00000542136.1; ENSP00000445334.1; ENSG00000102524.12. [Q9Y275-3]
DR GeneID; 10673; -.
DR KEGG; hsa:10673; -.
DR MANE-Select; ENST00000375887.9; ENSP00000365048.3; NM_006573.5; NP_006564.1.
DR UCSC; uc001vqr.4; human. [Q9Y275-1]
DR CTD; 10673; -.
DR DisGeNET; 10673; -.
DR GeneCards; TNFSF13B; -.
DR HGNC; HGNC:11929; TNFSF13B.
DR HPA; ENSG00000102524; Tissue enhanced (lymphoid).
DR MIM; 603969; gene.
DR neXtProt; NX_Q9Y275; -.
DR OpenTargets; ENSG00000102524; -.
DR PharmGKB; PA434; -.
DR VEuPathDB; HostDB:ENSG00000102524; -.
DR eggNOG; ENOG502RX35; Eukaryota.
DR GeneTree; ENSGT00940000157536; -.
DR HOGENOM; CLU_063693_0_0_1; -.
DR InParanoid; Q9Y275; -.
DR OMA; YMDSTFT; -.
DR PhylomeDB; Q9Y275; -.
DR TreeFam; TF332331; -.
DR PathwayCommons; Q9Y275; -.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR Reactome; R-HSA-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR SignaLink; Q9Y275; -.
DR SIGNOR; Q9Y275; -.
DR BioGRID-ORCS; 10673; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; TNFSF13B; human.
DR EvolutionaryTrace; Q9Y275; -.
DR GeneWiki; B-cell_activating_factor; -.
DR GenomeRNAi; 10673; -.
DR Pharos; Q9Y275; Tclin.
DR PRO; PR:Q9Y275; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y275; protein.
DR Bgee; ENSG00000102524; Expressed in monocyte and 154 other tissues.
DR ExpressionAtlas; Q9Y275; baseline and differential.
DR Genevisible; Q9Y275; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0048018; F:receptor ligand activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0031296; P:B cell costimulation; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
DR GO; GO:0002467; P:germinal center formation; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:AgBase.
DR GO; GO:0002636; P:positive regulation of germinal center formation; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
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 3D-structure; Alternative splicing; Cell membrane;
KW Cleavage on pair of basic residues; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Membrane; Reference proteome;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..285
FT /note="Tumor necrosis factor ligand superfamily member 13b,
FT membrane form"
FT /id="PRO_0000034528"
FT CHAIN 134..285
FT /note="Tumor necrosis factor ligand superfamily member 13b,
FT soluble form"
FT /id="PRO_0000034529"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 133..134
FT /note="Cleavage"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT DISULFID 232..245
FT VAR_SEQ 142..160
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12867412"
FT /id="VSP_041183"
FT VAR_SEQ 162..164
FT /note="SYT -> FIY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:22749832"
FT /id="VSP_047591"
FT VAR_SEQ 165..285
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:22749832"
FT /id="VSP_047592"
FT VARIANT 105
FT /note="A -> T (in dbSNP:rs201543678)"
FT /evidence="ECO:0000269|Ref.15"
FT /id="VAR_013483"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 168..181
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 191..201
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 205..215
FT /evidence="ECO:0007829|PDB:1KXG"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:4ZCH"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:1KXG"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1KXG"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1KXG"
SQ SEQUENCE 285 AA; 31223 MW; 48ED0D7AB38C8867 CRC64;
MDDSTEREQS RLTSCLKKRE EMKLKECVSI LPRKESPSVR SSKDGKLLAA TLLLALLSCC
LTVVSFYQVA ALQGDLASLR AELQGHHAEK LPAGAGAPKA GLEEAPAVTA GLKIFEPPAP
GEGNSSQNSR NKRAVQGPEE TVTQDCLQLI ADSETPTIQK GSYTFVPWLL SFKRGSALEE
KENKILVKET GYFFIYGQVL YTDKTYAMGH LIQRKKVHVF GDELSLVTLF RCIQNMPETL
PNNSCYSAGI AKLEEGDELQ LAIPRENAQI SLDGDVTFFG ALKLL
