ID BPI_HUMAN Reviewed; 487 AA. AC P17213; B2RCY2; Q1ZZU8; Q5JRW0; Q8IW58; Q9BYZ9; Q9H1L2; Q9H1M8; Q9H203; AC Q9UCT4; Q9UD65; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 4. DT 24-JAN-2024, entry version 205. DE RecName: Full=Bactericidal permeability-increasing protein; DE Short=BPI; DE AltName: Full=CAP 57; DE Flags: Precursor; GN Name=BPI; 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], PROTEIN SEQUENCE OF 32-68, FUNCTION, RP SUBCELLULAR LOCATION, DOMAIN, AND VARIANTS VAL-16 AND LYS-216. RX PubMed=2722846; DOI=10.1016/s0021-9258(18)60560-5; RA Gray P.W., Flaggs G., Leong S.R., Gumina R.J., Weiss J., Ooi C.E., RA Elsbach P.; RT "Cloning of the cDNA of a human neutrophil bactericidal protein. Structural RT and functional correlations."; RL J. Biol. Chem. 264:9505-9509(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7517398; DOI=10.1016/s0021-9258(17)32454-7; RA Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., Lane J.C., RA Leong S.R., Thornton M.B., Miller K.L., Scott R.W.; RT "Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)- RT binding protein. LPS binding properties and effects on LPS-mediated cell RT activation."; RL J. Biol. Chem. 269:17411-17416(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-16. RA Ma H., Cao X., Sun Y., Lei W.; RT "cDNA cloning and sequence analysis of human bactericidal/permeability RT protein."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-404. RC TISSUE=Fetal heart; 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=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-216. RC TISSUE=Leukocyte; 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 [MRNA] OF 5-487, AND VARIANTS LYS-216 AND ASP-404. RA Xu J., Wang H.; RT "Cloning of cDNA of human bactericidal/permeability-increasing protein."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP PROTEIN SEQUENCE OF 32-53, AND FUNCTION. RC TISSUE=Leukocyte; RX PubMed=1937776; DOI=10.1128/iai.59.11.4193-4200.1991; RA Wasiluk K.R., Skubitz K.M., Gray B.H.; RT "Comparison of granule proteins from human polymorphonuclear leukocytes RT which are bactericidal toward Pseudomonas aeruginosa."; RL Infect. Immun. 59:4193-4200(1991). RN [9] RP PROTEIN SEQUENCE OF 32-51. RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610; RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., RA Seeger M., Nathan C.F.; RT "Antibiotic proteins of human polymorphonuclear leukocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989). RN [10] RP PROTEIN SEQUENCE OF 32-48. RX PubMed=3667613; DOI=10.1016/s0021-9258(18)48110-0; RA Ooi C.E., Weiss J., Elsbach P., Frangione B., Mannion B.; RT "A 25-kDa NH2-terminal fragment carries all the antibacterial activities of RT the human neutrophil 60-kDa bactericidal/permeability-increasing protein."; RL J. Biol. Chem. 262:14891-14894(1987). RN [11] RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-49; CYS-163; CYS-166 RP AND CYS-206. RX PubMed=8812832; DOI=10.1006/prep.1996.0071; RA Horwitz A.H., Leigh S.D., Abrahamson S., Gazzano-Santoro H., Liu P.-S., RA Williams R.E., Carroll S.F., Theofan G.; RT "Expression and characterization of cysteine-modified variants of an amino- RT terminal fragment of bactericidal/permeability-increasing protein."; RL Protein Expr. Purif. 8:28-40(1996). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 32-487. RX PubMed=9188532; DOI=10.1126/science.276.5320.1861; RA Beamer L.J., Carroll S.F., Eisenberg D.; RT "Crystal structure of human BPI and two bound phospholipids at 2.4-A RT resolution."; RL Science 276:1861-1864(1997). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 32-487, AND DISULFIDE BOND. RX PubMed=10843855; DOI=10.1006/jmbi.2000.3805; RA Kleiger G., Beamer L.J., Grothe R., Mallick P., Eisenberg D.; RT "The 1.7 A crystal structure of BPI: a study of how two dissimilar amino RT acid sequences can adopt the same fold."; RL J. Mol. Biol. 299:1019-1034(2000). CC -!- FUNCTION: The cytotoxic action of BPI is limited to many species of CC Gram-negative bacteria; this specificity may be explained by a strong CC affinity of the very basic N-terminal half for the negatively charged CC lipopolysaccharides that are unique to the Gram-negative bacterial CC outer envelope. Has antibacterial activity against the Gram-negative CC bacterium P.aeruginosa, this activity is inhibited by LPS from CC P.aeruginosa. {ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2722846}. CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked. CC {ECO:0000269|PubMed:8812832}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8812832}. CC Cytoplasmic granule membrane {ECO:0000269|PubMed:2722846}. CC Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) CC granules. {ECO:0000269|PubMed:2722846}. CC -!- TISSUE SPECIFICITY: Restricted to cells of the myeloid series. CC -!- DOMAIN: The N-terminal region may be exposed to the interior of the CC granule, whereas the C-terminal portion may be embedded in the CC membrane. During phagocytosis and degranulation, proteases may be CC released and activated and cleave BPI at the junction of the N- and C- CC terminal portions of the molecule, providing controlled release of the CC N-terminal antibacterial fragment when bacteria are ingested. CC {ECO:0000269|PubMed:2722846}. CC -!- DOMAIN: The N- and C-terminal barrels adopt an identical fold despite CC having only 13% of conserved residues. {ECO:0000269|PubMed:10843855}. CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. CC {ECO:0000305}. 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; J04739; AAA51841.1; -; mRNA. DR EMBL; DQ414688; ABD66755.1; -; mRNA. DR EMBL; AK315328; BAG37729.1; -; mRNA. DR EMBL; AL359555; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391095; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL499625; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL583962; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040955; AAH40955.1; -; mRNA. DR EMBL; AF322588; AAG42844.1; -; mRNA. DR PIR; A33850; A30909. DR RefSeq; NP_001716.2; NM_001725.2. DR PDB; 1BP1; X-ray; 2.40 A; A=32-487. DR PDB; 1EWF; X-ray; 1.70 A; A=32-487. DR PDBsum; 1BP1; -. DR PDBsum; 1EWF; -. DR AlphaFoldDB; P17213; -. DR SMR; P17213; -. DR BioGRID; 107139; 16. DR IntAct; P17213; 1. DR STRING; 9606.ENSP00000262865; -. DR DrugBank; DB04178; Di-Stearoyl-3-Sn-Phosphatidylcholine. DR TCDB; 1.C.40.1.1; the bactericidal permeability increasing protein (bpip) family. DR GlyCosmos; P17213; 1 site, No reported glycans. DR GlyGen; P17213; 1 site. DR iPTMnet; P17213; -. DR PhosphoSitePlus; P17213; -. DR BioMuta; BPI; -. DR DMDM; 215274242; -. DR EPD; P17213; -. DR jPOST; P17213; -. DR MassIVE; P17213; -. DR MaxQB; P17213; -. DR PaxDb; 9606-ENSP00000262865; -. DR PeptideAtlas; P17213; -. DR PRIDE; P17213; -. DR ProteomicsDB; 53463; -. DR Pumba; P17213; -. DR Antibodypedia; 26835; 404 antibodies from 31 providers. DR DNASU; 671; -. DR Ensembl; ENST00000262865.9; ENSP00000262865.4; ENSG00000101425.14. DR GeneID; 671; -. DR KEGG; hsa:671; -. DR UCSC; uc002xib.3; human. DR AGR; HGNC:1095; -. DR CTD; 671; -. DR DisGeNET; 671; -. DR GeneCards; BPI; -. DR HGNC; HGNC:1095; BPI. DR HPA; ENSG00000101425; Tissue enriched (bone). DR MIM; 109195; gene. DR neXtProt; NX_P17213; -. DR OpenTargets; ENSG00000101425; -. DR PharmGKB; PA25403; -. DR VEuPathDB; HostDB:ENSG00000101425; -. DR eggNOG; KOG4160; Eukaryota. DR GeneTree; ENSGT01100000263545; -. DR HOGENOM; CLU_028970_3_2_1; -. DR InParanoid; P17213; -. DR OrthoDB; 2876641at2759; -. DR PhylomeDB; P17213; -. DR TreeFam; TF315617; -. DR PathwayCommons; P17213; -. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR SignaLink; P17213; -. DR SIGNOR; P17213; -. DR BioGRID-ORCS; 671; 14 hits in 1146 CRISPR screens. DR ChiTaRS; BPI; human. DR EvolutionaryTrace; P17213; -. DR GenomeRNAi; 671; -. DR Pharos; P17213; Tbio. DR PRO; PR:P17213; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P17213; Protein. DR Bgee; ENSG00000101425; Expressed in trabecular bone tissue and 111 other cell types or tissues. DR ExpressionAtlas; P17213; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL. DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:BHF-UCL. DR GO; GO:0043031; P:negative regulation of macrophage activation; IDA:BHF-UCL. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL. DR CDD; cd00025; BPI1; 1. DR CDD; cd00026; BPI2; 1. DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom. DR InterPro; IPR030675; BPI/LBP. DR InterPro; IPR032942; BPI/LBP/Plunc. DR InterPro; IPR001124; Lipid-bd_serum_glycop_C. DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS. DR InterPro; IPR017942; Lipid-bd_serum_glycop_N. DR PANTHER; PTHR10504; BACTERICIDAL PERMEABILITY-INCREASING BPI PROTEIN-RELATED; 1. DR PANTHER; PTHR10504:SF84; BACTERICIDAL PERMEABILITY-INCREASING PROTEIN; 1. DR Pfam; PF01273; LBP_BPI_CETP; 1. DR Pfam; PF02886; LBP_BPI_CETP_C; 1. DR PIRSF; PIRSF002417; Lipid_binding_protein; 1. DR SMART; SM00328; BPI1; 1. DR SMART; SM00329; BPI2; 1. DR SUPFAM; SSF55394; Bactericidal permeability-increasing protein, BPI; 2. DR PROSITE; PS00400; LBP_BPI_CETP; 1. DR Genevisible; P17213; HS. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Membrane; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..31 FT /evidence="ECO:0000269|PubMed:1937776, FT ECO:0000269|PubMed:2501794, ECO:0000269|PubMed:2722846, FT ECO:0000269|PubMed:3667613" FT CHAIN 32..487 FT /note="Bactericidal permeability-increasing protein" FT /id="PRO_0000017154" FT REGION 32..42 FT /note="Central sheet, part 1" FT /evidence="ECO:0000269|PubMed:10843855" FT REGION 41..224 FT /note="N-terminal barrel" FT /evidence="ECO:0000269|PubMed:10843855" FT REGION 226..290 FT /note="Central sheet, part 2" FT /evidence="ECO:0000269|PubMed:10843855" FT REGION 240..245 FT /note="Cleavage sites for elastase" FT /evidence="ECO:0000255" FT REGION 291..461 FT /note="C-terminal barrel" FT /evidence="ECO:0000269|PubMed:10843855" FT REGION 468..487 FT /note="Central sheet, part 3" FT /evidence="ECO:0000269|PubMed:10843855" FT CARBOHYD 380 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 166..206 FT /evidence="ECO:0000269|PubMed:10843855" FT VARIANT 12 FT /note="A -> T (in dbSNP:rs5743497)" FT /id="VAR_049728" FT VARIANT 12 FT /note="A -> V (in dbSNP:rs5743498)" FT /id="VAR_049729" FT VARIANT 16 FT /note="A -> V (in dbSNP:rs1341023)" FT /evidence="ECO:0000269|PubMed:2722846, ECO:0000269|Ref.3" FT /id="VAR_018401" FT VARIANT 90 FT /note="R -> C (in dbSNP:rs5743500)" FT /id="VAR_049730" FT VARIANT 140 FT /note="E -> Q (in dbSNP:rs5743506)" FT /id="VAR_049732" FT VARIANT 196 FT /note="A -> V (in dbSNP:rs5743509)" FT /id="VAR_018402" FT VARIANT 216 FT /note="E -> K (in dbSNP:rs4358188)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2722846, ECO:0000269|Ref.7" FT /id="VAR_018403" FT VARIANT 280 FT /note="A -> V (in dbSNP:rs5741804)" FT /id="VAR_049733" FT VARIANT 377 FT /note="V -> I (in dbSNP:rs5743524)" FT /id="VAR_049734" FT VARIANT 404 FT /note="N -> D (in dbSNP:rs5741809)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.7" FT /id="VAR_049735" FT VARIANT 451 FT /note="K -> E (in dbSNP:rs5743542)" FT /id="VAR_049736" FT MUTAGEN 49 FT /note="S->C: No impairment of secretion and increased FT propensity for dimer formation." FT /evidence="ECO:0000269|PubMed:8812832" FT MUTAGEN 163 FT /note="C->A: No impairment of secretion and/or biological FT activity. Loss of dimer formation." FT /evidence="ECO:0000269|PubMed:8812832" FT MUTAGEN 166 FT /note="C->S: Poorly secreted. Loss of LPS-binding and FT biological activity." FT /evidence="ECO:0000269|PubMed:8812832" FT MUTAGEN 206 FT /note="C->A: Not secreted." FT /evidence="ECO:0000269|PubMed:8812832" FT CONFLICT 5 FT /note="M -> L (in Ref. 6; AAH40955)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="T -> R (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 355 FT /note="P -> S (in Ref. 7; AAG42844)" FT /evidence="ECO:0000305" FT CONFLICT 375 FT /note="F -> L (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 411 FT /note="K -> R (in Ref. 7; AAG42844)" FT /evidence="ECO:0000305" FT CONFLICT 433 FT /note="Q -> L (in Ref. 4; BAG37729)" FT /evidence="ECO:0000305" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 42..60 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 81..93 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:1EWF" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 106..126 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 129..153 FT /evidence="ECO:0007829|PDB:1EWF" FT TURN 154..157 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 158..169 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 183..192 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 194..215 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 217..221 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 226..229 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 248..255 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 282..290 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 291..303 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 326..330 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 336..339 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 344..350 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 363..367 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 369..377 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 383..392 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 395..401 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 403..412 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 416..424 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 433..443 FT /evidence="ECO:0007829|PDB:1EWF" FT HELIX 445..454 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 464..474 FT /evidence="ECO:0007829|PDB:1EWF" FT STRAND 477..486 FT /evidence="ECO:0007829|PDB:1EWF" SQ SEQUENCE 487 AA; 53900 MW; 30BC73B1B465B62D CRC64; MRENMARGPC NAPRWASLMV LVAIGTAVTA AVNPGVVVRI SQKGLDYASQ QGTAALQKEL KRIKIPDYSD SFKIKHLGKG HYSFYSMDIR EFQLPSSQIS MVPNVGLKFS ISNANIKISG KWKAQKRFLK MSGNFDLSIE GMSISADLKL GSNPTSGKPT ITCSSCSSHI NSVHVHISKS KVGWLIQLFH KKIESALRNK MNSQVCEKVT NSVSSELQPY FQTLPVMTKI DSVAGINYGL VAPPATTAET LDVQMKGEFY SENHHNPPPF APPVMEFPAA HDRMVYLGLS DYFFNTAGLV YQEAGVLKMT LRDDMIPKES KFRLTTKFFG TFLPEVAKKF PNMKIQIHVS ASTPPHLSVQ PTGLTFYPAV DVQAFAVLPN SSLASLFLIG MHTTGSMEVS AESNRLVGEL KLDRLLLELK HSNIGPFPVE LLQDIMNYIV PILVLPRVNE KLQKGFPLPT PARVQLYNVV LQPHQNFLLF GADVVYK //