ID TNF10_HUMAN Reviewed; 281 AA. AC P50591; A1Y9B3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 214. DE RecName: Full=Tumor necrosis factor ligand superfamily member 10; DE AltName: Full=Apo-2 ligand; DE Short=Apo-2L; DE AltName: Full=TNF-related apoptosis-inducing ligand; DE Short=Protein TRAIL; DE AltName: CD_antigen=CD253; GN Name=TNFSF10; Synonyms=APO2L, TRAIL; 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=8777713; DOI=10.1016/1074-7613(95)90057-8; RA Wiley S.R., Schooley K., Smolak P.J., Din W.S., Huang C.-P., Nicholl J.K., RA Sutherland G.R., Davis-Smith T., Rauch C., Smith C.A., Goodwin R.G.; RT "Identification and characterization of a new member of the TNF family that RT induces apoptosis."; RL Immunity 3:673-682(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=8663110; DOI=10.1074/jbc.271.22.12687; RA Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., RA Ashkenazi A.; RT "Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis RT factor cytokine family."; RL J. Biol. Chem. 271:12687-12690(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RX PubMed=21859711; DOI=10.1074/jbc.m111.274639; RA Schnepple D.J., Shepard B., Bren G.D., Cummins N.W., Natesampillai S., RA Trushin S., Algeciras-Schimnich A., Meng X.W., Sainski A.M., Rizza S.A., RA Kaufmann S.H., Badley A.D.; RT "Isolation of a TRAIL antagonist from the serum of HIV-infected patients."; RL J. Biol. Chem. 286:35742-35754(2011). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Woods D.C., Haugen M.J., Johnson A.L.; RT "Novel TRAIL splice variant TRAIL-delta."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Thalamus; 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 GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 SUBCELLULAR LOCATION. RX PubMed=14609566; DOI=10.1016/s1043-4666(03)00094-2; RA Ehrlich S., Infante-Duarte C., Seeger B., Zipp F.; RT "Regulation of soluble and surface-bound TRAIL in human T cells, B cells, RT and monocytes."; RL Cytokine 24:244-253(2003). RN [9] RP PHOSPHORYLATION. RX PubMed=25171405; DOI=10.1016/j.cell.2014.06.048; RA Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr., RA Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L., Asara J.M., RA Dixon J.E., Yeo C.Y., Whitman M.; RT "A secreted tyrosine kinase acts in the extracellular environment."; RL Cell 158:1033-1044(2014). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 114-281 IN COMPLEX WITH TNFRSF10B, RP AND ZINC-BINDING SITE. RX PubMed=10549288; DOI=10.1016/s1097-2765(00)80207-5; RA Hymowitz S.G., Christinger H.W., Fuh G., Ultsch M., O'Connell M., RA Kelley R.F., Ashkenazi A., de Vos A.M.; RT "Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex RT with death receptor 5."; RL Mol. Cell 4:563-571(1999). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 119-281 IN COMPLEX WITH TNFRSF10B. RX PubMed=10542098; DOI=10.1038/14935; RA Mongkolsapaya J., Grimes J.M., Chen N., Xu X.-N., Stuart D.I., Jones E.Y., RA Screaton G.R.; RT "Structure of the TRAIL-DR5 complex reveals mechanisms conferring RT specificity in apoptotic initiation."; RL Nat. Struct. Biol. 6:1048-1053(1999). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-281. RX PubMed=10485660; DOI=10.1016/s1074-7613(00)80100-4; RA Cha S.-S., Kim M.S., Choi Y.H., Sung B.J., Shin N.K., Shin H.C., Sung Y.C., RA Oh B.-H.; RT "2.8 A resolution crystal structure of human TRAIL, a cytokine with RT selective antitumor activity."; RL Immunity 11:253-261(1999). RN [13] {ECO:0007744|PDB:5CIR} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 114-281 IN COMPLEX WITH RP TNFRSF10A, SUBUNIT, FUNCTION, AND ZINC-BINDING SITE. RX PubMed=26457518; DOI=10.1107/s2053230x15016416; RA Ramamurthy V., Yamniuk A.P., Lawrence E.J., Yong W., Schneeweis L.A., RA Cheng L., Murdock M., Corbett M.J., Doyle M.L., Sheriff S.; RT "The structure of the death receptor 4-TNF-related apoptosis-inducing RT ligand (DR4-TRAIL) complex."; RL Acta Crystallogr. F 71:1273-1281(2015). CC -!- FUNCTION: Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, CC TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG CC (PubMed:26457518, PubMed:10549288). Induces apoptosis. Its activity may CC be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, CC TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis. CC {ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:26457518}. CC -!- SUBUNIT: Homotrimer (PubMed:26457518). One TNFSF10 homotrimer interacts CC with three TNFSF10A mononers (PubMed:26457518). One TNFSF10 homotrimer CC interacts with three TNFSF10B mononers (PubMed:10549288). CC {ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:26457518}. CC -!- INTERACTION: CC P50591; Q13618: CUL3; NbExp=2; IntAct=EBI-495373, EBI-456129; CC P50591; O00220: TNFRSF10A; NbExp=4; IntAct=EBI-495373, EBI-518861; CC P50591; O14763: TNFRSF10B; NbExp=21; IntAct=EBI-495373, EBI-518882; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14609566}; CC Single-pass type II membrane protein {ECO:0000305}. Secreted CC {ECO:0000269|PubMed:14609566}. Note=Exists both as membrane-bound and CC soluble form. {ECO:0000269|PubMed:14609566}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P50591-1; Sequence=Displayed; CC Name=2; Synonyms=TRAIL-short, TRAIL-s; CC IsoId=P50591-2; Sequence=VSP_043507, VSP_043508; CC -!- TISSUE SPECIFICITY: Widespread; most predominant in spleen, lung and CC prostate. CC -!- PTM: Tyrosine phosphorylated by PKDCC/VLK. CC {ECO:0000269|PubMed:25171405}. CC -!- MISCELLANEOUS: [Isoform 2]: Induced upon HIV infection, antagonizes CC signaling via TRAIL receptor R2 (TNFRSF10B). {ECO:0000305}. 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/42632/TNFSF10"; 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; U37518; AAC50332.1; -; mRNA. DR EMBL; U57059; AAB01233.1; -; mRNA. DR EMBL; DQ848564; ABI24016.1; -; mRNA. DR EMBL; EU183231; ABW24658.1; -; mRNA. DR EMBL; AK296085; BAG58840.1; -; mRNA. DR EMBL; AC007919; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC016938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC032722; AAH32722.1; -; mRNA. DR CCDS; CCDS3219.1; -. [P50591-1] DR CCDS; CCDS54680.1; -. [P50591-2] DR RefSeq; NP_001177871.1; NM_001190942.1. [P50591-2] DR RefSeq; NP_003801.1; NM_003810.3. [P50591-1] DR PDB; 1D0G; X-ray; 2.40 A; A/B/D=114-281. DR PDB; 1D2Q; X-ray; 2.80 A; A/B=114-281. DR PDB; 1D4V; X-ray; 2.20 A; B=119-281. DR PDB; 1DG6; X-ray; 1.30 A; A=91-281. DR PDB; 1DU3; X-ray; 2.20 A; D/E/F/J/K/L=114-281. DR PDB; 4N90; X-ray; 3.30 A; A/B/C=114-281. DR PDB; 5CIR; X-ray; 3.00 A; A/B/D=114-281. DR PDBsum; 1D0G; -. DR PDBsum; 1D2Q; -. DR PDBsum; 1D4V; -. DR PDBsum; 1DG6; -. DR PDBsum; 1DU3; -. DR PDBsum; 4N90; -. DR PDBsum; 5CIR; -. DR AlphaFoldDB; P50591; -. DR SMR; P50591; -. DR BioGRID; 114280; 93. DR CORUM; P50591; -. DR DIP; DIP-6230N; -. DR IntAct; P50591; 19. DR MINT; P50591; -. DR STRING; 9606.ENSP00000241261; -. DR BindingDB; P50591; -. DR ChEMBL; CHEMBL5813; -. DR TCDB; 8.A.77.1.9; the sheddase (sheddase) family. DR iPTMnet; P50591; -. DR PhosphoSitePlus; P50591; -. DR BioMuta; TNFSF10; -. DR DMDM; 1730015; -. DR EPD; P50591; -. DR jPOST; P50591; -. DR MassIVE; P50591; -. DR PaxDb; 9606-ENSP00000241261; -. DR PeptideAtlas; P50591; -. DR ProteomicsDB; 56254; -. [P50591-1] DR Antibodypedia; 3728; 1433 antibodies from 51 providers. DR DNASU; 8743; -. DR Ensembl; ENST00000241261.7; ENSP00000241261.2; ENSG00000121858.11. [P50591-1] DR Ensembl; ENST00000420541.6; ENSP00000389931.2; ENSG00000121858.11. [P50591-2] DR GeneID; 8743; -. DR KEGG; hsa:8743; -. DR MANE-Select; ENST00000241261.7; ENSP00000241261.2; NM_003810.4; NP_003801.1. DR UCSC; uc003fie.4; human. [P50591-1] DR AGR; HGNC:11925; -. DR CTD; 8743; -. DR DisGeNET; 8743; -. DR GeneCards; TNFSF10; -. DR HGNC; HGNC:11925; TNFSF10. DR HPA; ENSG00000121858; Low tissue specificity. DR MIM; 603598; gene. DR neXtProt; NX_P50591; -. DR OpenTargets; ENSG00000121858; -. DR PharmGKB; PA36618; -. DR VEuPathDB; HostDB:ENSG00000121858; -. DR eggNOG; ENOG502QQ3R; Eukaryota. DR GeneTree; ENSGT01070000253816; -. DR HOGENOM; CLU_070352_1_0_1; -. DR InParanoid; P50591; -. DR OMA; EPIMLMK; -. DR OrthoDB; 5348190at2759; -. DR PhylomeDB; P50591; -. DR TreeFam; TF332169; -. DR PathwayCommons; P50591; -. DR Reactome; R-HSA-140534; Caspase activation via Death Receptors in the presence of ligand. DR Reactome; R-HSA-3371378; Regulation by c-FLIP. DR Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis. DR Reactome; R-HSA-5218900; CASP8 activity is inhibited. DR Reactome; R-HSA-69416; Dimerization of procaspase-8. DR Reactome; R-HSA-75158; TRAIL signaling. DR SignaLink; P50591; -. DR SIGNOR; P50591; -. DR BioGRID-ORCS; 8743; 23 hits in 1150 CRISPR screens. DR ChiTaRS; TNFSF10; human. DR EvolutionaryTrace; P50591; -. DR GeneWiki; TRAIL; -. DR GenomeRNAi; 8743; -. DR Pharos; P50591; Tchem. DR PRO; PR:P50591; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P50591; Protein. DR Bgee; ENSG00000121858; Expressed in nasal cavity epithelium and 199 other cell types or tissues. DR ExpressionAtlas; P50591; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0045569; F:TRAIL binding; IEA:Ensembl. DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEP:UniProtKB. DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB. DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB. DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00184; TNF; 1. DR Gene3D; 2.60.120.40; -; 1. DR InterPro; IPR021184; TNF_CS. DR InterPro; IPR006052; TNF_dom. DR InterPro; IPR017355; TNF_ligand_10/11. DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom. DR PANTHER; PTHR11471; TUMOR NECROSIS FACTOR FAMILY MEMBER; 1. DR PANTHER; PTHR11471:SF27; TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 10; 1. DR Pfam; PF00229; TNF; 1. DR PIRSF; PIRSF038013; TNF10_TNF11; 1. DR SMART; SM00207; TNF; 1. DR SUPFAM; SSF49842; TNF-like; 1. DR PROSITE; PS00251; TNF_1; 1. DR PROSITE; PS50049; TNF_2; 1. DR Genevisible; P50591; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane; Cytokine; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Secreted; KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1..281 FT /note="Tumor necrosis factor ligand superfamily member 10" FT /id="PRO_0000185503" FT TOPO_DOM 1..17 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 18..38 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 39..281 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 124..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 127..144 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 230 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between all trimeric partners" FT /evidence="ECO:0000269|PubMed:10549288, FT ECO:0000269|PubMed:26457518, ECO:0007744|PDB:5CIR" FT VAR_SEQ 91..101 FT /note="MILRTSEETIS -> TPRMKRLWAAK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:21859711, ECO:0000303|Ref.4" FT /id="VSP_043507" FT VAR_SEQ 102..281 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:21859711, ECO:0000303|Ref.4" FT /id="VSP_043508" FT VARIANT 33 FT /note="V -> I (in dbSNP:rs6763816)" FT /id="VAR_052584" FT VARIANT 47 FT /note="D -> E (in dbSNP:rs16845759)" FT /id="VAR_052585" FT STRAND 123..127 FT /evidence="ECO:0007829|PDB:1DG6" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:1D4V" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:1D2Q" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:1DG6" FT TURN 158..161 FT /evidence="ECO:0007829|PDB:1D0G" FT STRAND 163..170 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 180..193 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:5CIR" FT STRAND 205..213 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 220..228 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 237..250 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 255..262 FT /evidence="ECO:0007829|PDB:1DG6" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:1DG6" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:1DG6" FT STRAND 273..279 FT /evidence="ECO:0007829|PDB:1DG6" SQ SEQUENCE 281 AA; 32509 MW; DDAAAF78DAAB2F6D CRC64; MAMMEVQGGP SLGQTCVLIV IFTVLLQSLC VAVTYVYFTN ELKQMQDKYS KSGIACFLKE DDSYWDPNDE ESMNSPCWQV KWQLRQLVRK MILRTSEETI STVQEKQQNI SPLVRERGPQ RVAAHITGTR GRSNTLSSPN SKNEKALGRK INSWESSRSG HSFLSNLHLR NGELVIHEKG FYYIYSQTYF RFQEEIKENT KNDKQMVQYI YKYTSYPDPI LLMKSARNSC WSKDAEYGLY SIYQGGIFEL KENDRIFVSV TNEHLIDMDH EASFFGAFLV G //