ID   TNR9_HUMAN              Reviewed;         255 AA.
AC   Q07011;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 9;
DE   AltName: Full=4-1BB ligand receptor;
DE   AltName: Full=CDw137;
DE   AltName: Full=T-cell antigen 4-1BB homolog;
DE   AltName: Full=T-cell antigen ILA;
DE   AltName: CD_antigen=CD137;
DE   Flags: Precursor;
GN   Name=TNFRSF9; Synonyms=CD137, ILA;
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].
RC   TISSUE=Blood;
RX   PubMed=8088337; DOI=10.1002/eji.1830240943;
RA   Alderson M.R., Smith C.A., Tough T.W., Davis-Smith T., Armitage R.J.,
RA   Falk B., Roux E., Baker E., Sutherland G.R., Din W.S., Goodwin R.G.;
RT   "Molecular and biological characterization of human 4-1BB and its ligand.";
RL   Eur. J. Immunol. 24:2219-2227(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RX   PubMed=8262389; DOI=10.1016/0378-1119(93)90110-o;
RA   Schwarz H., Tuckwell J., Lotz M.;
RT   "A receptor induced by lymphocyte activation (ILA): a new member of the
RT   human nerve-growth-factor/tumor-necrosis-factor receptor family.";
RL   Gene 134:295-298(1993).
RN   [3]
RP   SEQUENCE REVISION TO 107.
RA   Schwarz H.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RX   PubMed=7622190; DOI=10.1016/0165-2478(94)00227-i;
RA   Zhou Z., Kim S., Hurtado J., Lee Z.H., Kim K.K., Pollok K.E., Kwon B.S.;
RT   "Characterization of human homologue of 4-1BB and its ligand.";
RL   Immunol. Lett. 45:67-73(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-56; ASN-115 AND
RP   ASP-176.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   PROTEIN SEQUENCE OF 24-38.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [9]
RP   INTERACTION WITH TRAF1; TRAF2 AND TRAF3.
RX   PubMed=9418902; DOI=10.1128/mcb.18.1.558;
RA   Arch R.H., Thompson C.B.;
RT   "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth
RT   factor receptor subfamily that bind TNF receptor-associated factors and
RT   activate nuclear factor kappaB.";
RL   Mol. Cell. Biol. 18:558-565(1998).
RN   [10]
RP   INTERACTION WITH TRAF1 AND TRAF2.
RX   PubMed=9607925; DOI=10.1084/jem.187.11.1849;
RA   Saoulli K., Lee S.Y., Cannons J.L., Yeh W.C., Santana A., Goldstein M.D.,
RA   Bangia N., DeBenedette M.A., Mak T.W., Choi Y., Watts T.H.;
RT   "CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-
RT   1BB ligand.";
RL   J. Exp. Med. 187:1849-1862(1998).
RN   [11]
RP   INTERACTION WITH LRR-REPEAT PROTEIN 1/LRR-1.
RX   PubMed=11804328;
RA   Jang I.-K., Lee Z.-H., Kim H.-H., Hill J.M., Kim J.-D., Kwon B.S.;
RT   "A novel leucine-rich repeat protein (LRR-1): potential involvement in 4-
RT   1BB-mediated signal transduction.";
RL   Mol. Cells 12:304-312(2001).
RN   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] GLY-250.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [13]
RP   INVOLVEMENT IN IMD109, VARIANT IMD109 SER-109, CHARACTERIZATION OF VARIANT
RP   IMD109 SER-109, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=30872117; DOI=10.1016/j.jaci.2019.03.002;
RA   Alosaimi M.F., Hoenig M., Jaber F., Platt C.D., Jones J., Wallace J.,
RA   Debatin K.M., Schulz A., Jacobsen E., Moeller P., Shamseldin H.E.,
RA   Abdulwahab F., Ibrahim N., Alardati H., Almuhizi F., Abosoudah I.F.,
RA   Basha T.A., Chou J., Alkuraya F.S., Geha R.S.;
RT   "Immunodeficiency and EBV-induced lymphoproliferation caused by 4-1BB
RT   deficiency.";
RL   J. Allergy Clin. Immunol. 144:574-583(2019).
CC   -!- FUNCTION: Receptor for TNFSF9/4-1BBL. Conveys a signal that enhances
CC       CD8(+) T-cell survival, cytotoxicity, and mitochondrial activity,
CC       thereby promoting immunity against viruses and tumors (Probable).
CC       {ECO:0000305|PubMed:30872117}.
CC   -!- SUBUNIT: Predominantly homodimeric, but may also exist as a monomer (By
CC       similarity). Interacts with TRAF1, TRAF2 and TRAF3 (PubMed:9418902,
CC       PubMed:9607925). Interacts with LRR-repeat protein 1/LRR-1
CC       (PubMed:11804328). {ECO:0000250|UniProtKB:P20334,
CC       ECO:0000269|PubMed:11804328, ECO:0000269|PubMed:9418902,
CC       ECO:0000269|PubMed:9607925}.
CC   -!- INTERACTION:
CC       Q07011; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-12945620, EBI-10329948;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein {ECO:0000305|PubMed:30872117}.
CC   -!- TISSUE SPECIFICITY: Expressed on the surface of activated T-cells.
CC       {ECO:0000269|PubMed:30872117}.
CC   -!- DISEASE: Immunodeficiency 109 with lymphoproliferation (IMD109)
CC       [MIM:620282]: An autosomal recessive primary immune disorder
CC       characterized by recurrent sinopulmonary infections, susceptibility to
CC       infection with Epstein-Barr virus (EBV), persistent EBV viremia, and
CC       EBV-induced lymphoproliferation or B-cell lymphoma.
CC       {ECO:0000269|PubMed:30872117}. Note=The disease may be caused by
CC       variants affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/tnfrsf9/";
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; U03397; AAA53133.1; -; mRNA.
DR   EMBL; L12964; AAA62478.2; -; mRNA.
DR   EMBL; AY438976; AAR05440.1; -; Genomic_DNA.
DR   EMBL; AL009183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006196; AAH06196.1; -; mRNA.
DR   CCDS; CCDS92.1; -.
DR   PIR; I38426; I38426.
DR   RefSeq; NP_001552.2; NM_001561.5.
DR   RefSeq; XP_011539688.1; XM_011541386.2.
DR   PDB; 6A3V; X-ray; 3.39 A; B/D/F/H/J/L/N/P/R/T/V/X=24-180.
DR   PDB; 6A3W; X-ray; 2.00 A; C/F/I/L=24-180.
DR   PDB; 6BWV; X-ray; 2.40 A; D/E=24-160.
DR   PDB; 6CPR; X-ray; 2.70 A; D/E/F=23-160.
DR   PDB; 6CU0; X-ray; 3.20 A; G/H/I/J/K/L=23-160.
DR   PDB; 6MGP; X-ray; 2.13 A; X/Y/Z=25-162.
DR   PDB; 6MHR; X-ray; 2.80 A; C/F=25-162.
DR   PDB; 6MI2; X-ray; 2.72 A; C/F=25-162.
DR   PDB; 6Y8K; X-ray; 2.01 A; AAA=24-160.
DR   PDB; 7D4B; X-ray; 3.14 A; A=25-162.
DR   PDB; 7YXU; X-ray; 2.31 A; A=24-160.
DR   PDB; 8GYE; X-ray; 2.30 A; A/D=24-186.
DR   PDBsum; 6A3V; -.
DR   PDBsum; 6A3W; -.
DR   PDBsum; 6BWV; -.
DR   PDBsum; 6CPR; -.
DR   PDBsum; 6CU0; -.
DR   PDBsum; 6MGP; -.
DR   PDBsum; 6MHR; -.
DR   PDBsum; 6MI2; -.
DR   PDBsum; 6Y8K; -.
DR   PDBsum; 7D4B; -.
DR   PDBsum; 7YXU; -.
DR   PDBsum; 8GYE; -.
DR   AlphaFoldDB; Q07011; -.
DR   SMR; Q07011; -.
DR   BioGRID; 109817; 36.
DR   DIP; DIP-3021N; -.
DR   ELM; Q07011; -.
DR   IntAct; Q07011; 5.
DR   STRING; 9606.ENSP00000478699; -.
DR   BindingDB; Q07011; -.
DR   ChEMBL; CHEMBL3712857; -.
DR   DrugBank; DB12077; Urelumab.
DR   GuidetoPHARMACOLOGY; 1878; -.
DR   TCDB; 9.B.87.4.2; the selenoprotein p receptor (selp-receptor) family.
DR   GlyCosmos; Q07011; 2 sites, No reported glycans.
DR   GlyGen; Q07011; 2 sites.
DR   iPTMnet; Q07011; -.
DR   PhosphoSitePlus; Q07011; -.
DR   BioMuta; TNFRSF9; -.
DR   DMDM; 728738; -.
DR   CPTAC; CPTAC-5974; -.
DR   MassIVE; Q07011; -.
DR   PaxDb; 9606-ENSP00000478699; -.
DR   PeptideAtlas; Q07011; -.
DR   ProteomicsDB; 58498; -.
DR   ABCD; Q07011; 3 sequenced antibodies.
DR   Antibodypedia; 3718; 1604 antibodies from 48 providers.
DR   CPTC; Q07011; 6 antibodies.
DR   DNASU; 3604; -.
DR   Ensembl; ENST00000377507.8; ENSP00000366729.3; ENSG00000049249.10.
DR   GeneID; 3604; -.
DR   KEGG; hsa:3604; -.
DR   MANE-Select; ENST00000377507.8; ENSP00000366729.3; NM_001561.6; NP_001552.2.
DR   UCSC; uc001aot.4; human.
DR   AGR; HGNC:11924; -.
DR   DisGeNET; 3604; -.
DR   GeneCards; TNFRSF9; -.
DR   HGNC; HGNC:11924; TNFRSF9.
DR   HPA; ENSG00000049249; Tissue enhanced (lymphoid).
DR   MalaCards; TNFRSF9; -.
DR   MIM; 602250; gene.
DR   MIM; 620282; phenotype.
DR   neXtProt; NX_Q07011; -.
DR   OpenTargets; ENSG00000049249; -.
DR   PharmGKB; PA36617; -.
DR   VEuPathDB; HostDB:ENSG00000049249; -.
DR   eggNOG; ENOG502S017; Eukaryota.
DR   GeneTree; ENSGT00730000111279; -.
DR   HOGENOM; CLU_076906_0_0_1; -.
DR   InParanoid; Q07011; -.
DR   OMA; YLFKQPF; -.
DR   OrthoDB; 5471029at2759; -.
DR   PhylomeDB; Q07011; -.
DR   TreeFam; TF336151; -.
DR   PathwayCommons; Q07011; -.
DR   Reactome; R-HSA-5669034; TNFs bind their physiological receptors.
DR   SignaLink; Q07011; -.
DR   BioGRID-ORCS; 3604; 16 hits in 1155 CRISPR screens.
DR   GeneWiki; CD137; -.
DR   GenomeRNAi; 3604; -.
DR   Pharos; Q07011; Tbio.
DR   PRO; PR:Q07011; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q07011; Protein.
DR   Bgee; ENSG00000049249; Expressed in buccal mucosa cell and 110 other cell types or tissues.
DR   ExpressionAtlas; Q07011; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0033084; P:regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR   CDD; cd13410; TNFRSF9; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR   InterPro; IPR020413; TNFR_9.
DR   InterPro; IPR034020; TNFRSF9_N.
DR   PANTHER; PTHR47139; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 9; 1.
DR   PANTHER; PTHR47139:SF1; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 9; 1.
DR   Pfam; PF00020; TNFR_c6; 1.
DR   PRINTS; PR01924; TNFACTORR9.
DR   SMART; SM00208; TNFR; 2.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
DR   Genevisible; Q07011; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           24..255
FT                   /note="Tumor necrosis factor receptor superfamily member 9"
FT                   /id="PRO_0000034577"
FT   TOPO_DOM        24..186
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          24..45
FT                   /note="TNFR-Cys 1"
FT   REPEAT          47..86
FT                   /note="TNFR-Cys 2"
FT   REPEAT          87..118
FT                   /note="TNFR-Cys 3"
FT   REPEAT          119..159
FT                   /note="TNFR-Cys 4"
FT   REGION          161..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..255
FT                   /note="Interaction with LRR-1"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        31..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        48..62
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        65..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        68..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        88..94
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        99..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        102..117
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        121..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   DISULFID        139..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT   VARIANT         56
FT                   /note="A -> T (in dbSNP:rs9657963)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_018920"
FT   VARIANT         109
FT                   /note="G -> S (in IMD109; uncertain significance; contrary
FT                   to wild-type, undetectable in patient's stimulated
FT                   peripheral blood mononuclear cells; patient's cells show
FT                   defective expansion, reduced expression of IFNG and
FT                   perforin/PRF1 and impaired allospecific and EBV-specific
FT                   cytotoxic activity, as well as reduced mitochondrial
FT                   function)"
FT                   /evidence="ECO:0000269|PubMed:30872117"
FT                   /id="VAR_088225"
FT   VARIANT         115
FT                   /note="K -> N (in dbSNP:rs9657965)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_018921"
FT   VARIANT         176
FT                   /note="A -> D (in dbSNP:rs9657979)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_018922"
FT   VARIANT         250
FT                   /note="E -> G (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs776878260)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035478"
FT   HELIX           27..30
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   TURN            39..42
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:6BWV"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:6MGP"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:6MGP"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:6MGP"
FT   STRAND          101..104
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   HELIX           139..142
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          145..148
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:6A3W"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:6A3W"
SQ   SEQUENCE   255 AA;  27899 MW;  F3A563FE5EF00460 CRC64;
     MGNSCYNIVA TLLLVLNFER TRSLQDPCSN CPAGTFCDNN RNQICSPCPP NSFSSAGGQR
     TCDICRQCKG VFRTRKECSS TSNAECDCTP GFHCLGAGCS MCEQDCKQGQ ELTKKGCKDC
     CFGTFNDQKR GICRPWTNCS LDGKSVLVNG TKERDVVCGP SPADLSPGAS SVTPPAPARE
     PGHSPQIISF FLALTSTALL FLLFFLTLRF SVVKRGRKKL LYIFKQPFMR PVQTTQEEDG
     CSCRFPEEEE GGCEL
//