TNF14_HUMAN
ID TNF14_HUMAN Reviewed; 240 AA.
AC O43557; A8K7M2; C9J5H4; O75476; Q6FHA1; Q8WVF8; Q96LD2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Tumor necrosis factor ligand superfamily member 14;
DE AltName: Full=Herpes virus entry mediator ligand;
DE Short=HVEM-L;
DE Short=Herpesvirus entry mediator ligand;
DE AltName: CD_antigen=CD258;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 14, membrane form;
DE Contains:
DE RecName: Full=Tumor necrosis factor ligand superfamily member 14, soluble form;
GN Name=TNFSF14; Synonyms=HVEML, LIGHT; ORFNames=UNQ391/PRO726;
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), VARIANT GLU-214, FUNCTION, SUBUNIT,
RP INTERACTION WITH TNFRSF14, AND TISSUE SPECIFICITY.
RX PubMed=9462508; DOI=10.1016/s1074-7613(00)80455-0;
RA Mauri D.N., Ebner R., Montgomery R.I., Kochel K.D., Cheung T.C., Yu G.-L.,
RA Ruben S., Murphy M., Eisenberg R.J., Cohen G.H., Spear P.G., Ware C.F.;
RT "LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are
RT ligands for herpesvirus entry mediator.";
RL Immunity 8:21-30(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=9765287; DOI=10.1074/jbc.273.42.27548;
RA Harrop J.A., McDonnell P.C., Brigham-Burke M., Lyn S.D., Minton J.,
RA Tan K.B., Dede K., Spampanato J., Silverman C., Hensley P., DiPrinzio R.,
RA Emery J.G., Deen K., Eichman C., Chabot-Fletcher M., Truneh A., Young P.R.;
RT "Herpesvirus entry mediator ligand (HVEM-L), a novel ligand for HVEM/TR2,
RT stimulates proliferation of T cells and inhibits HT29 cell growth.";
RL J. Biol. Chem. 273:27548-27556(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEOLYTIC PROCESSING, AND VARIANT
RP GLU-214.
RX PubMed=11673523; DOI=10.4049/jimmunol.167.9.5122;
RA Granger S.W., Butrovich K.D., Houshmand P., Edwards W.R., Ware C.F.;
RT "Genomic characterization of LIGHT reveals linkage to an immune response
RT locus on chromosome 19p13.3 and distinct isoforms generated by alternate
RT splicing or proteolysis.";
RL J. Immunol. 167:5122-5128(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-214.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-214.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-214.
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 [9]
RP FUNCTION.
RX PubMed=10754304; DOI=10.4049/jimmunol.164.8.4105;
RA Tamada K., Shimozaki K., Chapoval A.I., Zhai Y., Su J., Chen S.F.,
RA Hsieh S.L., Nagata S., Ni J., Chen L.;
RT "LIGHT, a TNF-like molecule, costimulates T cell proliferation and is
RT required for dendritic cell-mediated allogeneic T cell response.";
RL J. Immunol. 164:4105-4110(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 83-240, GLYCOSYLATION AT ASN-102,
RP AND DISULFIDE BOND.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of LIGHT.";
RL Submitted (MAY-2012) to the PDB data bank.
CC -!- FUNCTION: Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy
CC receptor TNFRSF6B modulates its effects. Acts as a ligand for
CC TNFRSF14/HVEM (PubMed:9462508, PubMed:10754304). Upon binding to
CC TNFRSF14/HVEM, delivers costimulatory signals to T cells, leading to T
CC cell proliferation and IFNG production (PubMed:10754304).
CC {ECO:0000269|PubMed:10754304, ECO:0000269|PubMed:9462508}.
CC -!- SUBUNIT: Homotrimer. Interacts with TNFRSF14.
CC {ECO:0000269|PubMed:9462508}.
CC -!- INTERACTION:
CC O43557; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-524131, EBI-10225815;
CC O43557; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-524131, EBI-10827839;
CC O43557; O95393: BMP10; NbExp=3; IntAct=EBI-524131, EBI-3922513;
CC O43557; O75508: CLDN11; NbExp=3; IntAct=EBI-524131, EBI-12820543;
CC O43557; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-524131, EBI-12256978;
CC O43557; Q07325: CXCL9; NbExp=3; IntAct=EBI-524131, EBI-3911467;
CC O43557; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-524131, EBI-10266796;
CC O43557; Q86UP9: LHFPL3; NbExp=3; IntAct=EBI-524131, EBI-12925734;
CC O43557; P36941: LTBR; NbExp=3; IntAct=EBI-524131, EBI-3509981;
CC O43557; P21145: MAL; NbExp=5; IntAct=EBI-524131, EBI-3932027;
CC O43557; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-524131, EBI-2804156;
CC O43557; Q9Y342: PLLP; NbExp=3; IntAct=EBI-524131, EBI-3919291;
CC O43557; P53801: PTTG1IP; NbExp=3; IntAct=EBI-524131, EBI-3906138;
CC O43557; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-524131, EBI-8652744;
CC O43557; Q15436: SEC23A; NbExp=3; IntAct=EBI-524131, EBI-81088;
CC O43557; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-524131, EBI-13075176;
CC O43557; P17152: TMEM11; NbExp=3; IntAct=EBI-524131, EBI-723946;
CC O43557; Q92956: TNFRSF14; NbExp=5; IntAct=EBI-524131, EBI-1056653;
CC O43557; O95407: TNFRSF6B; NbExp=2; IntAct=EBI-524131, EBI-524171;
CC O43557; O00526: UPK2; NbExp=3; IntAct=EBI-524131, EBI-10179682;
CC O43557; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-524131, EBI-10254561;
CC O43557; P50284: Ltbr; Xeno; NbExp=2; IntAct=EBI-524131, EBI-647023;
CC O43557; Q71F55: Tnfrsf14; Xeno; NbExp=2; IntAct=EBI-524131, EBI-11687219;
CC O43557-1; O95407: TNFRSF6B; NbExp=4; IntAct=EBI-15910661, EBI-524171;
CC O43557-1; O43557-1: TNFSF14; NbExp=3; IntAct=EBI-15910661, EBI-15910661;
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
CC 14, membrane form]: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member
CC 14, soluble form]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43557-1; Sequence=Displayed;
CC Name=2; Synonyms=LIGHT delta-TM;
CC IsoId=O43557-2; Sequence=VSP_006452;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the spleen but also
CC found in the brain. Weakly expressed in peripheral lymphoid tissues and
CC in heart, placenta, liver, lung, appendix, and kidney, and no
CC expression seen in fetal tissues, endocrine glands, or nonhematopoietic
CC tumor lines. {ECO:0000269|PubMed:9462508}.
CC -!- INDUCTION: Up-regulated after T-cell activation.
CC -!- PTM: N-glycosylated. {ECO:0000269|Ref.10}.
CC -!- PTM: The soluble form of isoform 1 derives from the membrane form by
CC proteolytic processing. {ECO:0000269|PubMed:11673523}.
CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR EMBL; AF036581; AAC39563.1; -; mRNA.
DR EMBL; AF064090; AAC25169.1; -; mRNA.
DR EMBL; AY028261; AAK26160.1; -; mRNA.
DR EMBL; AY358812; AAQ89171.1; -; mRNA.
DR EMBL; AK292037; BAF84726.1; -; mRNA.
DR EMBL; CR541854; CAG46652.1; -; mRNA.
DR EMBL; CR541871; CAG46669.1; -; mRNA.
DR EMBL; AC008760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471139; EAW69072.1; -; Genomic_DNA.
DR CCDS; CCDS12171.1; -. [O43557-1]
DR CCDS; CCDS45939.1; -. [O43557-2]
DR RefSeq; NP_003798.2; NM_003807.4. [O43557-1]
DR RefSeq; NP_742011.2; NM_172014.3. [O43557-2]
DR RefSeq; XP_016882906.1; XM_017027417.1.
DR PDB; 4EN0; X-ray; 2.59 A; A/B/C=83-240.
DR PDB; 4J6G; X-ray; 2.40 A; A/B=83-240.
DR PDB; 4KG8; X-ray; 2.25 A; A/B/C=83-240.
DR PDB; 4KGG; X-ray; 2.78 A; A/B=83-240.
DR PDB; 4KGQ; X-ray; 2.27 A; A/B=83-240.
DR PDB; 4RSU; X-ray; 2.30 A; A/B/C/G/H/I=83-240.
DR PDB; 7MSG; X-ray; 3.50 A; A/B/C=83-240.
DR PDBsum; 4EN0; -.
DR PDBsum; 4J6G; -.
DR PDBsum; 4KG8; -.
DR PDBsum; 4KGG; -.
DR PDBsum; 4KGQ; -.
DR PDBsum; 4RSU; -.
DR PDBsum; 7MSG; -.
DR AlphaFoldDB; O43557; -.
DR SMR; O43557; -.
DR BioGRID; 114277; 88.
DR DIP; DIP-3016N; -.
DR IntAct; O43557; 24.
DR STRING; 9606.ENSP00000469049; -.
DR ChEMBL; CHEMBL3712914; -.
DR GlyGen; O43557; 1 site.
DR iPTMnet; O43557; -.
DR PhosphoSitePlus; O43557; -.
DR SwissPalm; O43557; -.
DR BioMuta; TNFSF14; -.
DR MassIVE; O43557; -.
DR PaxDb; O43557; -.
DR PeptideAtlas; O43557; -.
DR PRIDE; O43557; -.
DR ProteomicsDB; 49049; -. [O43557-1]
DR ProteomicsDB; 49050; -. [O43557-2]
DR Antibodypedia; 11882; 680 antibodies from 41 providers.
DR DNASU; 8740; -.
DR Ensembl; ENST00000245912.7; ENSP00000245912.3; ENSG00000125735.11. [O43557-2]
DR Ensembl; ENST00000599359.1; ENSP00000469049.1; ENSG00000125735.11. [O43557-1]
DR Ensembl; ENST00000675206.1; ENSP00000502837.1; ENSG00000125735.11. [O43557-1]
DR GeneID; 8740; -.
DR KEGG; hsa:8740; -.
DR MANE-Select; ENST00000675206.1; ENSP00000502837.1; NM_001376887.1; NP_001363816.1.
DR UCSC; uc002mfk.3; human. [O43557-1]
DR CTD; 8740; -.
DR DisGeNET; 8740; -.
DR GeneCards; TNFSF14; -.
DR HGNC; HGNC:11930; TNFSF14.
DR HPA; ENSG00000125735; Tissue enriched (liver).
DR MIM; 604520; gene.
DR neXtProt; NX_O43557; -.
DR OpenTargets; ENSG00000125735; -.
DR PharmGKB; PA36622; -.
DR VEuPathDB; HostDB:ENSG00000125735; -.
DR eggNOG; ENOG502RZ4W; Eukaryota.
DR GeneTree; ENSGT01050000244957; -.
DR HOGENOM; CLU_070352_5_0_1; -.
DR InParanoid; O43557; -.
DR OMA; IFVRIRT; -.
DR OrthoDB; 1371007at2759; -.
DR PhylomeDB; O43557; -.
DR TreeFam; TF332169; -.
DR PathwayCommons; O43557; -.
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; O43557; -.
DR SIGNOR; O43557; -.
DR BioGRID-ORCS; 8740; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; TNFSF14; human.
DR GeneWiki; TNFSF14; -.
DR GenomeRNAi; 8740; -.
DR Pharos; O43557; Tbio.
DR PRO; PR:O43557; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43557; protein.
DR Bgee; ENSG00000125735; Expressed in right lobe of liver and 107 other tissues.
DR Genevisible; O43557; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR GO; GO:0010818; P:T cell chemotaxis; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; NAS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; NAS:UniProtKB.
DR CDD; cd00184; TNF; 1.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR006053; TNF.
DR InterPro; IPR006052; TNF_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00229; TNF; 1.
DR PRINTS; PR01234; TNECROSISFCT.
DR SMART; SM00207; 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; Cytokine; Cytoplasm;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..240
FT /note="Tumor necrosis factor ligand superfamily member 14,
FT membrane form"
FT /id="PRO_0000034532"
FT CHAIN ?83..240
FT /note="Tumor necrosis factor ligand superfamily member 14,
FT soluble form"
FT /id="PRO_0000034533"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT SITE 82..83
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.10"
FT DISULFID 154..187
FT /evidence="ECO:0000269|Ref.10"
FT VAR_SEQ 38..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11673523"
FT /id="VSP_006452"
FT VARIANT 32
FT /note="S -> L (in dbSNP:rs2291667)"
FT /id="VAR_027677"
FT VARIANT 120
FT /note="L -> V (in dbSNP:rs17851606)"
FT /id="VAR_027678"
FT VARIANT 214
FT /note="K -> E (in dbSNP:rs344560)"
FT /evidence="ECO:0000269|PubMed:11673523,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:9462508,
FT ECO:0000269|Ref.6, ECO:0000269|Ref.8"
FT /id="VAR_027679"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4KGQ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4KGQ"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:4KG8"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4EN0"
FT STRAND 197..209
FT /evidence="ECO:0007829|PDB:4KG8"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:4KG8"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4KGQ"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:4KG8"
SQ SEQUENCE 240 AA; 26350 MW; 49D0B1870F390B39 CRC64;
MEESVVRPSV FVVDGQTDIP FTRLGRSHRR QSCSVARVGL GLLLLLMGAG LAVQGWFLLQ
LHWRLGEMVT RLPDGPAGSW EQLIQERRSH EVNPAAHLTG ANSSLTGSGG PLLWETQLGL
AFLRGLSYHD GALVVTKAGY YYIYSKVQLG GVGCPLGLAS TITHGLYKRT PRYPEELELL
VSQQSPCGRA TSSSRVWWDS SFLGGVVHLE AGEKVVVRVL DERLVRLRDG TRSYFGAFMV
