ID TNF15_HUMAN Reviewed; 251 AA. AC O95150; Q3SX69; Q5VJK8; Q5VWH1; Q8NFE9; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Tumor necrosis factor ligand superfamily member 15; DE AltName: Full=TNF ligand-related molecule 1; DE AltName: Full=Vascular endothelial cell growth inhibitor; DE Contains: DE RecName: Full=Tumor necrosis factor ligand superfamily member 15, membrane form; DE Contains: DE RecName: Full=Tumor necrosis factor ligand superfamily member 15, secreted form; GN Name=TNFSF15; Synonyms=TL1, VEGI; 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 3), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Umbilical vein; RX PubMed=9872942; DOI=10.1096/fasebj.13.1.181; RA Zhai Y., Ni J., Jiang G.-W., Lu J., Xing L., Lincoln C., Carter K.C., RA Janat F., Kozak D., Xu S., Rojas L., Aggarwal B.B., Ruben S., Li L.-Y., RA Gentz R., Yu G.-L.; RT "VEGI, a novel cytokine of the tumor necrosis factor family, is an RT angiogenesis inhibitor that suppresses the growth of colon carcinomas in RT vivo."; RL FASEB J. 13:181-189(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11923219; DOI=10.1096/fj.01-0757fje; RA Chew L.-J., Pan H., Yu J., Tian S., Huang W.-Q., Zhang J.Y., Pang S., RA Li L.-Y.; RT "A novel secreted splice variant of vascular endothelial cell growth RT inhibitor."; RL FASEB J. 16:742-744(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF N-TERMINUS, RP FUNCTION, INTERACTION WITH TNFRSF25 AND TNFRSF6B, SUBCELLULAR LOCATION, RP PROTEOLYTIC PROCESSING, INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=11911831; DOI=10.1016/s1074-7613(02)00283-2; RA Migone T.-S., Zhang J., Luo X., Zhuang L., Chen C., Hu B., Hong J.S., RA Perry J.W., Chen S.-F., Zhou J.X.H., Cho Y.H., Ullrich S., Kanakaraj P., RA Carrell J., Boyd E., Olsen H.S., Hu G., Pukac L., Liu D., Ni J., Kim S., RA Gentz R., Feng P., Moore P.A., Ruben S.M., Wei P.; RT "TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell RT costimulator."; RL Immunity 16:479-492(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [8] RP IDENTIFICATION (ISOFORM 3), AND TISSUE SPECIFICITY. RX PubMed=9434163; DOI=10.1016/s0378-1119(97)00509-x; RA Tan K.B., Harrop J., Reddy M., Young P., Terrett J., Emery J., Moore G., RA Truneh A.; RT "Characterization of a novel TNF-like ligand and recently described TNF RT ligand and TNF receptor superfamily genes and their constitutive and RT inducible expression in hematopoietic and non-hematopoietic cells."; RL Gene 204:35-46(1997). RN [9] RP FUNCTION. RX PubMed=10597252; DOI=10.1038/sj.onc.1203059; RA Haridas V., Shrivastava A., Su J., Yu G.-L., Ni J., Liu D., Chen S.-F., RA Ni Y., Ruben S.M., Gentz R., Aggarwal B.B.; RT "VEGI, a new member of the TNF family activates nuclear factor-kappa B and RT c-Jun N-terminal kinase and modulates cell growth."; RL Oncogene 18:6496-6504(1999). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 71-251, DISULFIDE BOND, AND RP SUBUNIT. RX PubMed=17935696; DOI=10.1016/j.bbrc.2007.09.097; RA Jin T., Guo F., Kim S., Howard A., Zhang Y.-Z.; RT "X-ray crystal structure of TNF ligand family member TL1A at 2.1A."; RL Biochem. Biophys. Res. Commun. 364:1-6(2007). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 72-251 IN COMPLEX WITH TNFRSF6B. RX PubMed=21300286; DOI=10.1016/j.str.2010.12.004; RA Zhan C., Patskovsky Y., Yan Q., Li Z., Ramagopal U., Cheng H., RA Brenowitz M., Hui X., Nathenson S.G., Almo S.C.; RT "Decoy strategies: the structure of TL1A:DcR3 complex."; RL Structure 19:162-171(2011). CC -!- FUNCTION: Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of CC NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in CC vitro). Promotes activation of caspases and apoptosis. CC {ECO:0000269|PubMed:10597252, ECO:0000269|PubMed:11911831, CC ECO:0000269|PubMed:11923219, ECO:0000269|PubMed:9872942}. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17935696, CC ECO:0000269|PubMed:21300286}. CC -!- INTERACTION: CC O95150; O43464: HTRA2; NbExp=3; IntAct=EBI-16355546, EBI-517086; CC O95150; P42858: HTT; NbExp=3; IntAct=EBI-16355546, EBI-466029; CC O95150-1; O95407: TNFRSF6B; NbExp=3; IntAct=EBI-15910629, EBI-524171; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:11911831, CC ECO:0000305|PubMed:11923219}; Single-pass type II membrane protein CC {ECO:0000305|PubMed:11911831, ECO:0000305|PubMed:11923219}. CC -!- SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member CC 15, secreted form]: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=TL1A, VEGI-251; CC IsoId=O95150-1; Sequence=Displayed; CC Name=2; Synonyms=VEGI-192; CC IsoId=O95150-2; Sequence=VSP_033492; CC Name=3; Synonyms=VEGI-174; CC IsoId=O95150-3; Sequence=VSP_033493, VSP_033494; CC -!- TISSUE SPECIFICITY: Specifically expressed in endothelial cells. CC Detected in monocytes, placenta, lung, liver, kidney, skeletal muscle, CC pancreas, spleen, prostate, small intestine and colon. CC {ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219, CC ECO:0000269|PubMed:9434163, ECO:0000269|PubMed:9872942}. CC -!- INDUCTION: Up-regulated by IL1A/interleukin-1 alpha and TNF. CC {ECO:0000269|PubMed:11911831, ECO:0000269|PubMed:11923219}. CC -!- SIMILARITY: Belongs to the tumor necrosis factor family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42638/TNFSF15"; 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; AF039390; AAD08783.1; -; mRNA. DR EMBL; AY434464; AAR98573.1; -; mRNA. DR EMBL; AF520785; AAM77366.1; -; mRNA. DR EMBL; AK291642; BAF84331.1; -; mRNA. DR EMBL; AL390240; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87431.1; -; Genomic_DNA. DR EMBL; BC069435; AAH69435.1; -; mRNA. DR EMBL; BC074940; AAH74940.1; -; mRNA. DR EMBL; BC074941; AAH74941.1; -; mRNA. DR EMBL; BC104462; AAI04463.1; -; mRNA. DR EMBL; BC104463; AAI04464.1; -; mRNA. DR CCDS; CCDS6809.1; -. [O95150-1] DR RefSeq; NP_001191273.1; NM_001204344.1. [O95150-2] DR RefSeq; NP_005109.2; NM_005118.3. [O95150-1] DR PDB; 2O0O; X-ray; 3.00 A; A/B/C=72-251. DR PDB; 2QE3; X-ray; 2.50 A; A=72-251. DR PDB; 2RE9; X-ray; 2.10 A; A/B/C=72-251. DR PDB; 2RJK; X-ray; 2.30 A; A=72-251. DR PDB; 2RJL; X-ray; 2.05 A; A=72-251. DR PDB; 3K51; X-ray; 2.45 A; A=72-251. DR PDB; 3MI8; X-ray; 2.95 A; A=72-251. DR PDBsum; 2O0O; -. DR PDBsum; 2QE3; -. DR PDBsum; 2RE9; -. DR PDBsum; 2RJK; -. DR PDBsum; 2RJL; -. DR PDBsum; 3K51; -. DR PDBsum; 3MI8; -. DR AlphaFoldDB; O95150; -. DR SMR; O95150; -. DR BioGRID; 115291; 5. DR DIP; DIP-59562N; -. DR IntAct; O95150; 6. DR STRING; 9606.ENSP00000363157; -. DR GlyCosmos; O95150; 2 sites, No reported glycans. DR GlyGen; O95150; 2 sites. DR BioMuta; TNFSF15; -. DR MassIVE; O95150; -. DR PaxDb; 9606-ENSP00000363157; -. DR PeptideAtlas; O95150; -. DR ProteomicsDB; 50663; -. [O95150-1] DR ProteomicsDB; 50664; -. [O95150-2] DR Antibodypedia; 2153; 878 antibodies from 39 providers. DR DNASU; 9966; -. DR Ensembl; ENST00000374045.5; ENSP00000363157.3; ENSG00000181634.8. [O95150-1] DR GeneID; 9966; -. DR KEGG; hsa:9966; -. DR MANE-Select; ENST00000374045.5; ENSP00000363157.3; NM_005118.4; NP_005109.2. DR UCSC; uc004bjh.4; human. [O95150-1] DR AGR; HGNC:11931; -. DR CTD; 9966; -. DR DisGeNET; 9966; -. DR GeneCards; TNFSF15; -. DR HGNC; HGNC:11931; TNFSF15. DR HPA; ENSG00000181634; Tissue enhanced (intestine). DR MalaCards; TNFSF15; -. DR MIM; 604052; gene. DR neXtProt; NX_O95150; -. DR OpenTargets; ENSG00000181634; -. DR Orphanet; 186; Primary biliary cholangitis. DR PharmGKB; PA36623; -. DR VEuPathDB; HostDB:ENSG00000181634; -. DR eggNOG; ENOG502S4Q1; Eukaryota. DR GeneTree; ENSGT01060000248544; -. DR HOGENOM; CLU_070352_3_0_1; -. DR InParanoid; O95150; -. DR OMA; EACVFQT; -. DR OrthoDB; 2909163at2759; -. DR PhylomeDB; O95150; -. DR TreeFam; TF332169; -. DR PathwayCommons; O95150; -. DR Reactome; R-HSA-5669034; TNFs bind their physiological receptors. DR SignaLink; O95150; -. DR SIGNOR; O95150; -. DR BioGRID-ORCS; 9966; 12 hits in 1148 CRISPR screens. DR ChiTaRS; TNFSF15; human. DR EvolutionaryTrace; O95150; -. DR GeneWiki; Vascular_endothelial_growth_inhibitor; -. DR GenomeRNAi; 9966; -. DR Pharos; O95150; Tbio. DR PRO; PR:O95150; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; O95150; Protein. DR Bgee; ENSG00000181634; Expressed in cartilage tissue and 99 other cell types or tissues. DR ExpressionAtlas; O95150; baseline and differential. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. 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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI. DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. 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 PANTHER; PTHR11471; TUMOR NECROSIS FACTOR FAMILY MEMBER; 1. DR PANTHER; PTHR11471:SF24; TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 15; 1. DR Pfam; PF00229; TNF; 1. DR PRINTS; PR01234; TNECROSISFCT. DR SMART; SM00207; TNF; 1. DR SUPFAM; SSF49842; TNF-like; 1. DR PROSITE; PS50049; TNF_2; 1. DR Genevisible; O95150; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytokine; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted; KW Signal-anchor; Transmembrane; Transmembrane helix. FT CHAIN 1..251 FT /note="Tumor necrosis factor ligand superfamily member 15, FT membrane form" FT /id="PRO_0000185505" FT CHAIN 72..251 FT /note="Tumor necrosis factor ligand superfamily member 15, FT secreted form" FT /id="PRO_0000333234" FT TOPO_DOM 1..35 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 36..56 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 57..251 FT /note="Extracellular" FT /evidence="ECO:0000255" FT SITE 71..72 FT /note="Cleavage" FT SITE 187 FT /note="Important for binding TNFRSF6B" FT SITE 190 FT /note="Important for binding TNFRSF6B" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 229 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 162..202 FT /evidence="ECO:0000269|PubMed:17935696" FT VAR_SEQ 1..85 FT /note="MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTT FT YLLVSQLRAQGEACVQFQALKGQEFAPSHQQVY -> MQLTKGRLHFSHPLSHTKHISP FT FVTD (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11923219" FT /id="VSP_033492" FT VAR_SEQ 1..77 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9872942" FT /id="VSP_033493" FT VAR_SEQ 78..100 FT /note="APSHQQVYAPLRADGDKPRAHLT -> MRRFLSKVYSFPMRKLILFLVFP FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9872942" FT /id="VSP_033494" FT VARIANT 110 FT /note="F -> L (in dbSNP:rs16931745)" FT /id="VAR_043130" FT CONFLICT 34 FT /note="R -> H (in Ref. 7; AAI04463)" FT /evidence="ECO:0000305" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2RE9" FT STRAND 120..123 FT /evidence="ECO:0007829|PDB:2O0O" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 145..156 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:2RE9" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:2RE9" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:2RE9" FT STRAND 192..200 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:2RJK" FT STRAND 209..220 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:2RJL" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:2RJL" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:2RJL" FT STRAND 244..250 FT /evidence="ECO:0007829|PDB:2RJL" SQ SEQUENCE 251 AA; 28087 MW; 65ED70E367E3446D CRC64; MAEDLGLSFG ETASVEMLPE HGSCRPKARS SSARWALTCC LVLLPFLAGL TTYLLVSQLR AQGEACVQFQ ALKGQEFAPS HQQVYAPLRA DGDKPRAHLT VVRQTPTQHF KNQFPALHWE HELGLAFTKN RMNYTNKFLL IPESGDYFIY SQVTFRGMTS ECSEIRQAGR PNKPDSITVV ITKVTDSYPE PTQLLMGTKS VCEVGSNWFQ PIYLGAMFSL QEGDKLMVNV SDISLVDYTK EDKTFFGAFL L //