ID LBP_HUMAN Reviewed; 481 AA. AC P18428; B2R938; O43438; Q92672; Q9H403; Q9UD66; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 04-NOV-2026, entry version 205. DE RecName: Full=Lipopolysaccharide-binding protein; DE Short=LBP; DE Flags: Precursor; GN Name=LBP; 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 26-40, VARIANT LEU-436, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=2402637; DOI=10.1126/science.2402637; RA Schumann R.R., Leong S.R., Flaggs G.W., Gray P.W., Wright S.D., RA Mathison J.C., Tobias P.S., Ulevitch R.J.; RT "Structure and function of lipopolysaccharide binding protein."; RL Science 249:1429-1431(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. 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 [GENOMIC DNA], AND VARIANT LEU-436. RX PubMed=9240454; DOI=10.1006/bbrc.1997.6970; RA Hubacek J.A., Buchler C., Aslanidis C., Schmitz G.; RT "The genomic organization of the genes for human lipopolysaccharide binding RT protein (LBP) and bactericidal permeability increasing protein (BPI) is RT highly conserved."; RL Biochem. Biophys. Res. Commun. 236:427-430(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9441745; DOI=10.1006/geno.1997.5030; RA Kirschning C.J., Au-Young J., Lamping N., Reuter D., Pfeil D., RA Seilhamer J.J., Schumann R.R.; RT "Similar organization of the lipopolysaccharide-binding protein (LBP) and RT phospholipid transfer protein (PLTP) genes suggests a common gene family of RT lipid-binding proteins."; RL Genomics 46:416-425(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-436. RC TISSUE=Liver; RA Long J.Y., Liu J.Q., Xue Y.N., Wang H.X.; RT "Cloning and sequencing of human lipopolysaccharide-binding protein gene."; RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 25:469-471(1998). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [7] 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 [8] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41. RA Sutton C.L., Smith R.I.F., Centola M.B., Theofan G.; RT "Cloning and characterization of the human LBP upstream sequence."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [10] RP FUNCTION, AND INTERACTION WITH CD14 AND LIPOPOLYSACCHARIDE. RX PubMed=1698311; DOI=10.1126/science.1698311; RA Wright S.D., Ramos R.A., Tobias P.S., Ulevitch R.J., Mathison J.C.; RT "CD14, a receptor for complexes of lipopolysaccharide (LPS) and LPS binding RT protein."; RL Science 249:1431-1433(1990). RN [11] RP REVIEW. RX PubMed=17481951; DOI=10.1016/j.ijmm.2007.04.001; RA Jerala R.; RT "Structural biology of the LPS recognition."; RL Int. J. Med. Microbiol. 297:353-363(2007). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-394. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [13] RP FUNCTION. RX PubMed=20133493; DOI=10.1093/intimm/dxq005; RA Tsukamoto H., Fukudome K., Takao S., Tsuneyoshi N., Kimoto M.; RT "Lipopolysaccharide-binding protein-mediated Toll-like receptor 4 RT dimerization enables rapid signal transduction against lipopolysaccharide RT stimulation on membrane-associated CD14-expressing cells."; RL Int. Immunol. 22:271-280(2010). RN [14] RP FUNCTION, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP GLYCOSYLATION, VARIANT LEU-333, AND CHARACTERIZATION OF VARIANT LEU-333. RX PubMed=24120359; DOI=10.1016/j.immuni.2013.09.005; RA Eckert J.K., Kim Y.J., Kim J.I., Guertler K., Oh D.Y., Sur S., Lundvall L., RA Hamann L., van der Ploeg A., Pickkers P., Giamarellos-Bourboulis E., RA Kubarenko A.V., Weber A.N., Kabesch M., Kumpf O., An H.J., Lee J.O., RA Schumann R.R.; RT "The crystal structure of lipopolysaccharide binding protein reveals the RT location of a frequent mutation that impairs innate immunity."; RL Immunity 39:647-660(2013). CC -!- FUNCTION: Plays a role in the innate immune response. Binds to the CC lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid CC present in the outer membrane of all Gram-negative bacteria CC (PubMed:24120359, PubMed:7517398). Acts as an affinity enhancer for CC CD14, facilitating its association with LPS. Promotes the release of CC cytokines in response to bacterial lipopolysaccharide (PubMed:24120359, CC PubMed:7517398). {ECO:0000269|PubMed:1698311, CC ECO:0000269|PubMed:20133493, ECO:0000269|PubMed:24120359, CC ECO:0000269|PubMed:7517398, ECO:0000305|PubMed:17481951}. CC -!- SUBUNIT: When bound to LPS, interacts (via C-terminus) with soluble and CC membrane-bound CD14. {ECO:0000269|PubMed:1698311, CC ECO:0000305|PubMed:17481951}. CC -!- INTERACTION: CC P18428; P23560-2: BDNF; NbExp=3; IntAct=EBI-3927059, EBI-12275524; CC P18428; Q13162: PRDX4; NbExp=4; IntAct=EBI-3927059, EBI-2211957; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402637, CC ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398}. Cytoplasmic CC granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane- CC associated in polymorphonuclear Leukocytes (PMN) granules. CC {ECO:0000250|UniProtKB:P17213}. CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level). CC {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:24120359}. 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; M35533; AAA59493.1; -; mRNA. DR EMBL; X98657; CAA67226.1; -; Genomic_DNA. DR EMBL; X98658; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98659; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98660; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98661; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98662; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98663; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98664; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98665; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98666; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98667; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; X98668; CAA67226.1; JOINED; Genomic_DNA. DR EMBL; AF013512; AAC39547.1; -; Genomic_DNA. DR EMBL; AF013500; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013501; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013502; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013503; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013504; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013505; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013506; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013507; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013508; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013509; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013510; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF013511; AAC39547.1; JOINED; Genomic_DNA. DR EMBL; AF105067; AAD21962.1; -; mRNA. DR EMBL; AK313625; BAG36385.1; -; mRNA. DR EMBL; AL080249; CAC10462.1; -; Genomic_DNA. DR EMBL; CH471077; EAW76034.1; -; Genomic_DNA. DR EMBL; L42172; AAA66446.1; -; Genomic_DNA. DR CCDS; CCDS13304.1; -. DR PIR; A35843; A35843. DR PIR; A54136; A54136. DR RefSeq; NP_004130.2; NM_004139.5. DR AlphaFoldDB; P18428; -. DR SMR; P18428; -. DR BioGRID; 110121; 18. DR DIP; DIP-90N; -. DR FunCoup; P18428; 190. DR IntAct; P18428; 15. DR NDEx; IQUERY-CP-LBP; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000217407; -. DR TCDB; 1.C.40.1.2; the bactericidal permeability increasing protein (bpip) family. DR GlyConnect; P18428; 6 N-Linked glycans (1 site). DR GlyCosmos; P18428; 4 sites, 7 glycans. DR GlyGen; P18428; 4 sites, 7 N-linked glycans (1 site). DR iPTMnet; P18428; -. DR PhosphoSitePlus; P18428; -. DR BioMuta; LBP; -. DR DMDM; 116242615; -. DR CPTAC; non-CPTAC-1140; -. DR MassIVE; P18428; -. DR PaxDb; 9606-ENSP00000217407; -. DR PeptideAtlas; P18428; -. DR ProteomicsDB; 53558; -. DR TopDownProteomics; P18428; -. DR Antibodypedia; 777; 482 antibodies from 40 providers. DR DNASU; 3929; -. DR Ensembl; ENST00000217407.3; ENSP00000217407.2; ENSG00000129988.7. DR GeneID; 3929; -. DR KEGG; hsa:3929; -. DR MANE-Select; ENST00000217407.3; ENSP00000217407.2; NM_004139.5; NP_004130.2. DR UCSC; uc002xic.3; human. DR AGR; HGNC:6517; -. DR ClinPGx; PA30303; -. DR CTD; 3929; -. DR DisGeNET; 3929; -. DR GeneCards; LBP; -. DR HGNC; HGNC:6517; LBP. DR HPA; ENSG00000129988; Tissue enriched (liver). DR MIM; 151990; gene. DR OpenTargets; ENSG00000129988; -. DR VEuPathDB; HostDB:ENSG00000129988; -. DR eggNOG; KOG4160; Eukaryota. DR GeneTree; ENSGT01100000263546; -. DR HOGENOM; CLU_028970_3_2_1; -. DR InParanoid; P18428; -. DR OMA; AAMNMEK; -. DR OrthoDB; 10255543at2759; -. DR PAN-GO; P18428; 9 GO annotations based on evolutionary models. DR PhylomeDB; P18428; -. DR PathwayCommons; P18428; -. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-HSA-166020; Transfer of LPS from LBP carrier to CD14. DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR SignaLink; P18428; -. DR Agora; ENSG00000129988; -. DR BioGRID-ORCS; 3929; 14 hits in 1159 CRISPR screens. DR ChiTaRS; LBP; human. DR GeneWiki; Lipopolysaccharide-binding_protein; -. DR GenomeRNAi; 3929; -. DR Pharos; P18428; Tbio. DR PRO; PR:P18428; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P18428; protein. DR Bgee; ENSG00000129988; Expressed in right lobe of liver and 107 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0015026; F:coreceptor activity; IPI:AgBase. DR GO; GO:0071723; F:lipopeptide binding; IDA:AgBase. DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI. DR GO; GO:0070891; F:lipoteichoic acid binding; IDA:MGI. DR GO; GO:0140104; F:molecular carrier activity; IDA:UniProt. DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL. DR GO; GO:0006953; P:acute-phase response; IEP:BHF-UCL. DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:AgBase. DR GO; GO:0006968; P:cellular defense response; ISS:BHF-UCL. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI. DR GO; GO:0071223; P:cellular response to lipoteichoic acid; IDA:MGI. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:BHF-UCL. DR GO; GO:0032490; P:detection of molecule of bacterial origin; IDA:BHF-UCL. DR GO; GO:0045087; P:innate immune response; ISS:BHF-UCL. DR GO; GO:0015920; P:lipopolysaccharide transport; IDA:BHF-UCL. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:BHF-UCL. DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL. DR GO; GO:0008228; P:opsonization; ISS:BHF-UCL. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL. DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL. DR GO; GO:0060265; P:positive regulation of respiratory burst involved in inflammatory response; ISS:BHF-UCL. DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IDA:BHF-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL. DR CDD; cd00025; BPI1; 1. DR CDD; cd00026; BPI2; 1. DR FunFam; 3.15.20.10:FF:000001; Phospholipid transfer protein; 1. DR FunFam; 3.15.10.10:FF:000001; phospholipid transfer protein-like; 1. DR Gene3D; 3.15.10.10; Bactericidal permeability-increasing protein, domain 1; 1. DR Gene3D; 3.15.20.10; Bactericidal permeability-increasing protein, domain 2; 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:SF66; LIPOPOLYSACCHARIDE-BINDING 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. PE 1: Evidence at protein level; KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunity; Innate immunity; Lipid transport; Membrane; KW Proteomics identification; Reference proteome; Secreted; Signal; Transport. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:2402637" FT CHAIN 26..481 FT /note="Lipopolysaccharide-binding protein" FT /id="PRO_0000017158" FT CARBOHYD 300 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 386 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 394 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 159..198 FT /evidence="ECO:0000250|UniProtKB:Q61805" FT VARIANT 9 FT /note="P -> L (in dbSNP:rs2232580)" FT /id="VAR_028243" FT VARIANT 111 FT /note="R -> Q (in dbSNP:rs2232583)" FT /id="VAR_049737" FT VARIANT 125 FT /note="L -> I (in dbSNP:rs2232585)" FT /id="VAR_028244" FT VARIANT 147 FT /note="E -> K (in dbSNP:rs36015492)" FT /id="VAR_049738" FT VARIANT 157 FT /note="S -> C (in dbSNP:rs2232586)" FT /id="VAR_061293" FT VARIANT 166 FT /note="V -> M (in dbSNP:rs5744204)" FT /id="VAR_028245" FT VARIANT 242 FT /note="M -> I (in dbSNP:rs2232601)" FT /id="VAR_028246" FT VARIANT 283 FT /note="D -> G (in dbSNP:rs2232607)" FT /id="VAR_028247" FT VARIANT 294 FT /note="H -> R (in dbSNP:rs2232608)" FT /id="VAR_028248" FT VARIANT 333 FT /note="P -> L (abolishes lipopolysaccharide binding and FT causes increased proteolytic degradation of the protein; FT dbSNP:rs2232613)" FT /evidence="ECO:0000269|PubMed:24120359" FT /id="VAR_028249" FT VARIANT 339 FT /note="L -> F (in dbSNP:rs5744212)" FT /id="VAR_028250" FT VARIANT 364 FT /note="I -> T (in dbSNP:rs2232615)" FT /id="VAR_049739" FT VARIANT 436 FT /note="F -> L (in dbSNP:rs2232618)" FT /evidence="ECO:0000269|PubMed:2402637, FT ECO:0000269|PubMed:9240454, ECO:0000269|Ref.5" FT /id="VAR_028251" FT VARIANT 445 FT /note="A -> T (in dbSNP:rs2232619)" FT /id="VAR_028252" FT CONFLICT 6 FT /note="R -> H (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="E -> C (in Ref. 2)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="N -> K (in Ref. 4; AAC39547)" FT /evidence="ECO:0000305" FT CONFLICT 128 FT /note="S -> F (in Ref. 4; AAC39547)" FT /evidence="ECO:0000305" FT CONFLICT 154..157 FT /note="VTAS -> GYCL (in Ref. 1; AAA59493)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="L -> S (in Ref. 1; AAA59493)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="R -> S (in Ref. 4; AAC39547)" FT /evidence="ECO:0000305" FT CONFLICT 266..270 FT /note="VMSLP -> A (in Ref. 1; AAA59493)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="L -> H (in Ref. 4; AAC39547)" FT /evidence="ECO:0000305" SQ SEQUENCE 481 AA; 53384 MW; 5A0E4B9E5E604C72 CRC64; MGALARALPS ILLALLLTST PEALGANPGL VARITDKGLQ YAAQEGLLAL QSELLRITLP DFTGDLRIPH VGRGRYEFHS LNIHSCELLH SALRPVPGQG LSLSISDSSI RVQGRWKVRK SFFKLQGSFD VSVKGISISV NLLLGSESSG RPTVTASSCS SDIADVEVDM SGDLGWLLNL FHNQIESKFQ KVLESRICEM IQKSVSSDLQ PYLQTLPVTT EIDSFADIDY SLVEAPRATA QMLEVMFKGE IFHRNHRSPV TLLAAVMSLP EEHNKMVYFA ISDYVFNTAS LVYHEEGYLN FSITDDMIPP DSNIRLTTKS FRPFVPRLAR LYPNMNLELQ GSVPSAPLLN FSPGNLSVDP YMEIDAFVLL PSSSKEPVFR LSVATNVSAT LTFNTSKITG FLKPGKVKVE LKESKVGLFN AELLEALLNY YILNTFYPKF NDKLAEGFPL PLLKRVQLYD LGLQIHKDFL FLGANVQYMR V //