ID   TNFL4_HUMAN             Reviewed;         183 AA.
AC   P23510; Q5JZA5; Q8IV74; Q9HCN9;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 184.
DE   RecName: Full=Tumor necrosis factor ligand superfamily member 4;
DE   AltName: Full=Glycoprotein Gp34;
DE   AltName: Full=OX40 ligand;
DE            Short=OX40L;
DE   AltName: Full=TAX transcriptionally-activated glycoprotein 1;
DE   AltName: CD_antigen=CD252;
GN   Name=TNFSF4; Synonyms=TXGP1;
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=1996093; DOI=10.1128/mcb.11.3.1313-1325.1991;
RA   Miura S., Ohtani K., Numata N., Niki M., Ohbo K., Ina Y., Gojobori T.,
RA   Tanaka Y., Tozawa H., Nakamura M., Sugamura K.;
RT   "Molecular cloning and characterization of a novel glycoprotein, gp34, that
RT   is specifically induced by the human T-cell leukemia virus type I
RT   transactivator p40tax.";
RL   Mol. Cell. Biol. 11:1313-1325(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7913952; DOI=10.1084/jem.180.2.757;
RA   Godfrey W.R., Fagnoni F.F., Harara M.A., Buck D., Engleman E.G.;
RT   "Identification of a human OX-40 ligand, a costimulator of CD4+ T cells
RT   with homology to tumor necrosis factor.";
RL   J. Exp. Med. 180:757-762(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67.
RX   PubMed=11197696; DOI=10.1038/sj.gene.6363709;
RA   Hikami K., Tsuchiya N., Tokunaga K.;
RT   "New variations in human OX40 ligand (CD134L) gene.";
RL   Genes Immun. 1:521-522(2000).
RN   [8]
RP   CHARACTERIZATION.
RX   PubMed=8076595; DOI=10.1002/j.1460-2075.1994.tb06715.x;
RA   Baum P.R., Gayle R.B. III, Ramsdell F., Srinivasan S., Sorensen R.A.,
RA   Watson M.L., Seldin M.F., Baker E., Sutherland G.R., Clifford K.N.,
RA   Alderson M.R., Goodwin R.G., Fanslow W.C.;
RT   "Molecular characterization of murine and human OX40/OX40 ligand systems:
RT   identification of a human OX40 ligand as the HTLV-1-regulated protein
RT   gp34.";
RL   EMBO J. 13:3992-4001(1994).
RN   [9]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO SLE.
RX   PubMed=18059267; DOI=10.1038/ng.2007.47;
RA   Cunninghame Graham D.S., Graham R.R., Manku H., Wong A.K., Whittaker J.C.,
RA   Gaffney P.M., Moser K.L., Rioux J.D., Altshuler D., Behrens T.W.,
RA   Vyse T.J.;
RT   "Polymorphism at the TNF superfamily gene TNFSF4 confers susceptibility to
RT   systemic lupus erythematosus.";
RL   Nat. Genet. 40:83-89(2008).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 48-183 IN COMPLEX WITH TNFRSF4,
RP   SUBUNIT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-152.
RX   PubMed=16905106; DOI=10.1016/j.str.2006.06.015;
RA   Compaan D.M., Hymowitz S.G.;
RT   "The crystal structure of the costimulatory OX40-OX40L complex.";
RL   Structure 14:1321-1330(2006).
CC   -!- FUNCTION: Cytokine that binds to TNFRSF4. Co-stimulates T-cell
CC       proliferation and cytokine production.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16905106}.
CC   -!- INTERACTION:
CC       P23510; P43489: TNFRSF4; NbExp=2; IntAct=EBI-11724451, EBI-15596193;
CC       P23510; P43488: Tnfsf4; Xeno; NbExp=2; IntAct=EBI-11724451, EBI-519690;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P23510-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P23510-2; Sequence=VSP_056288;
CC   -!- INDUCTION: By HTLV-1 transactivator p40-Tax.
CC   -!- DISEASE: Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic,
CC       relapsing, inflammatory, and often febrile multisystemic disorder of
CC       connective tissue, characterized principally by involvement of the
CC       skin, joints, kidneys and serosal membranes. It is of unknown etiology,
CC       but is thought to represent a failure of the regulatory mechanisms of
CC       the autoimmune system. The disease is marked by a wide range of system
CC       dysfunctions, an elevated erythrocyte sedimentation rate, and the
CC       formation of LE cells in the blood or bone marrow.
CC       {ECO:0000269|PubMed:18059267}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC       The upstream region of TNFSF4 contains a single risk haplotype for SLE,
CC       which is correlated with increased expression of both cell-surface
CC       TNFSF4 and TNFSF4 transcripts. Increased levels of TNFSF4 are thought
CC       to augment T-cell-APC interaction and the functional consequences of T-
CC       cell activation, thereby destabilizing peripheral tolerance.
CC   -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}.
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DR   EMBL; D90224; BAA14259.1; -; mRNA.
DR   EMBL; X79929; CAA56284.1; -; mRNA.
DR   EMBL; AK297932; BAG60249.1; -; mRNA.
DR   EMBL; AL022310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471067; EAW90938.1; -; Genomic_DNA.
DR   EMBL; BC041663; AAH41663.1; -; mRNA.
DR   EMBL; AB042988; BAB18304.1; -; Genomic_DNA.
DR   CCDS; CCDS1306.1; -. [P23510-1]
DR   CCDS; CCDS72985.1; -. [P23510-2]
DR   PIR; A39680; A39680.
DR   RefSeq; NP_001284491.1; NM_001297562.1. [P23510-2]
DR   RefSeq; NP_003317.1; NM_003326.4. [P23510-1]
DR   PDB; 2HEV; X-ray; 2.41 A; F=51-183.
DR   PDBsum; 2HEV; -.
DR   AlphaFoldDB; P23510; -.
DR   SMR; P23510; -.
DR   DIP; DIP-3023N; -.
DR   IntAct; P23510; 3.
DR   MINT; P23510; -.
DR   STRING; 9606.ENSP00000281834; -.
DR   ChEMBL; CHEMBL3712900; -.
DR   GlyCosmos; P23510; 4 sites, No reported glycans.
DR   GlyGen; P23510; 4 sites.
DR   iPTMnet; P23510; -.
DR   PhosphoSitePlus; P23510; -.
DR   BioMuta; TNFSF4; -.
DR   DMDM; 121540; -.
DR   jPOST; P23510; -.
DR   MassIVE; P23510; -.
DR   PaxDb; 9606-ENSP00000281834; -.
DR   PeptideAtlas; P23510; -.
DR   ProteomicsDB; 54122; -. [P23510-1]
DR   ProteomicsDB; 70669; -.
DR   ABCD; P23510; 51 sequenced antibodies.
DR   Antibodypedia; 34389; 817 antibodies from 40 providers.
DR   DNASU; 7292; -.
DR   Ensembl; ENST00000281834.4; ENSP00000281834.3; ENSG00000117586.11. [P23510-1]
DR   Ensembl; ENST00000367718.5; ENSP00000356691.1; ENSG00000117586.11. [P23510-2]
DR   GeneID; 7292; -.
DR   KEGG; hsa:7292; -.
DR   MANE-Select; ENST00000281834.4; ENSP00000281834.3; NM_003326.5; NP_003317.1.
DR   UCSC; uc001giv.4; human. [P23510-1]
DR   AGR; HGNC:11934; -.
DR   CTD; 7292; -.
DR   DisGeNET; 7292; -.
DR   GeneCards; TNFSF4; -.
DR   HGNC; HGNC:11934; TNFSF4.
DR   HPA; ENSG00000117586; Low tissue specificity.
DR   MalaCards; TNFSF4; -.
DR   MIM; 152700; phenotype.
DR   MIM; 603594; gene.
DR   neXtProt; NX_P23510; -.
DR   OpenTargets; ENSG00000117586; -.
DR   Orphanet; 2073; Narcolepsy type 1.
DR   Orphanet; 536; Systemic lupus erythematosus.
DR   PharmGKB; PA36625; -.
DR   VEuPathDB; HostDB:ENSG00000117586; -.
DR   eggNOG; ENOG502ST4X; Eukaryota.
DR   GeneTree; ENSGT00390000015127; -.
DR   HOGENOM; CLU_091735_0_0_1; -.
DR   InParanoid; P23510; -.
DR   OMA; TTHNTSC; -.
DR   OrthoDB; 4334524at2759; -.
DR   PhylomeDB; P23510; -.
DR   TreeFam; TF336384; -.
DR   PathwayCommons; P23510; -.
DR   Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR   SignaLink; P23510; -.
DR   SIGNOR; P23510; -.
DR   BioGRID-ORCS; 7292; 9 hits in 1148 CRISPR screens.
DR   ChiTaRS; TNFSF4; human.
DR   EvolutionaryTrace; P23510; -.
DR   GenomeRNAi; 7292; -.
DR   Pharos; P23510; Tbio.
DR   PRO; PR:P23510; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P23510; Protein.
DR   Bgee; ENSG00000117586; Expressed in primordial germ cell in gonad and 116 other cell types or tissues.
DR   ExpressionAtlas; P23510; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
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:0032813; F:tumor necrosis factor receptor superfamily binding; ISS:BHF-UCL.
DR   GO; GO:0002526; P:acute inflammatory response; ISS:BHF-UCL.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL.
DR   GO; GO:0002215; P:defense response to nematode; ISS:BHF-UCL.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0035709; P:memory T cell activation; ISS:BHF-UCL.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:BHF-UCL.
DR   GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:BHF-UCL.
DR   GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0032689; P:negative regulation of type II interferon production; ISS:BHF-UCL.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; ISS:BHF-UCL.
DR   GO; GO:0050871; P:positive regulation of B cell activation; ISS:BHF-UCL.
DR   GO; GO:1900281; P:positive regulation of CD4-positive, alpha-beta T cell costimulation; ISS:BHF-UCL.
DR   GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0032722; P:positive regulation of chemokine production; ISS:BHF-UCL.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; ISS:BHF-UCL.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:BHF-UCL.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
DR   GO; GO:0032736; P:positive regulation of interleukin-13 production; ISS:BHF-UCL.
DR   GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:BHF-UCL.
DR   GO; GO:2000572; P:positive regulation of interleukin-4-dependent isotype switching to IgE isotypes; ISS:BHF-UCL.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL.
DR   GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0002726; P:positive regulation of T cell cytokine production; ISS:BHF-UCL.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
DR   GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0002830; P:positive regulation of type 2 immune response; ISS:BHF-UCL.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; IDA:BHF-UCL.
DR   GO; GO:0002819; P:regulation of adaptive immune response; ISS:BHF-UCL.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:BHF-UCL.
DR   GO; GO:0035713; P:response to nitrogen dioxide; ISS:BHF-UCL.
DR   GO; GO:0009615; P:response to virus; ISS:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0035712; P:T-helper 2 cell activation; ISS:BHF-UCL.
DR   CDD; cd00184; TNF; 1.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR021184; TNF_CS.
DR   InterPro; IPR006052; TNF_dom.
DR   InterPro; IPR042338; TNFSF4.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR17534; OX40 LIGAND; 1.
DR   PANTHER; PTHR17534:SF4; TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 4; 1.
DR   SMART; SM00207; TNF; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS00251; TNF_1; 1.
DR   Genevisible; P23510; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytokine; Disulfide bond; Glycoprotein;
KW   Membrane; Reference proteome; Signal-anchor; Systemic lupus erythematosus;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..183
FT                   /note="Tumor necrosis factor ligand superfamily member 4"
FT                   /id="PRO_0000185493"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..50
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..183
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16905106"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        97..181
FT                   /evidence="ECO:0000269|PubMed:16905106"
FT   VAR_SEQ         1..51
FT                   /note="MERVQPLEENVGNAARPRFERNKLLLVASVIQGLGLLLCFTYICLHFSALQ
FT                   -> M (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056288"
FT   STRAND          61..70
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   STRAND          99..120
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   STRAND          126..143
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:2HEV"
FT   STRAND          165..174
FT                   /evidence="ECO:0007829|PDB:2HEV"
SQ   SEQUENCE   183 AA;  21050 MW;  0D5604AD29D529CF CRC64;
     MERVQPLEEN VGNAARPRFE RNKLLLVASV IQGLGLLLCF TYICLHFSAL QVSHRYPRIQ
     SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ
     KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF
     CVL
//